1. 1-Hydroxyethane
2. Absolute alcohol
3. Absolute ethanol
4. Absolute ethyl alcohol
5. Aethanol
6. Aethylalkohol
7. Alcare Hand Degermer
8. Alcohol
9. Alcohols
10. Alcool ethylique
11. Alcool etilico
12. Algrain
13. Alkohol
14. Alkoholu etylowego
15. Anhydrol
16. Anhydrous alcohol
17. Cologne spirit
18. Cologne spirits
19. Dehydrated alcohol
20. Dehydrated ethanol
21. Denatured alcohol
22. Denatured ethanol
23. Desinfektol EL
24. Distilled spirits
25. Ethanol 200 proof
26. Ethanol solution
27. Ethicap
28. Ethyl alc
29. Ethyl alcohol
30. Ethyl alcohol anhydrous
31. Ethyl alcohol in alcoholic beverages
32. Ethyl alcohol usp
33. Ethyl hydrate
34. Ethyl hydroxide
35. Fermentation alcohol
36. Grain alcohol
37. Hinetoless
38. Hydroxyethane
39. Infinity Pure
40. Jaysol
41. Jaysol S
42. Lux
43. Methylcarbinol
44. Molasses alcohol
45. Potato alcohol
46. Punctilious ethyl alcohol
47. Pyro
48. Spirit
49. Spirits of wine
50. Spirt
51. Synasol
52. Tecsol
53. Tecsol C
54. Thanol
55. diluted Alcohol
56. silent spirit
57. undenatured Ethanol

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• Cytoplasm
• Extracellular
• peroxisome

• Blood
• Cerebrospinal Fluid
• Saliva
• Urine

• 211980 (Lung Cancer)

1. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed ]
2. Gordon Z, Parsons CL, Monga M: Intravesical ethanol test: an ineffective measure of bladder hyperpermeability. Urology. 2003 Mar;61(3):555-7. [PubMed ]
3. Huang JS, She QB, Crilly KS, Kiss Z: Ethanol, Zn2+ and insulin interact as progression factors to enhance DNA synthesis synergistically in the presence of Ca2+ and other cell cycle initiators in fibroblasts. Biochem J. 2000 Feb 15;346 Pt 1:241-7. [PubMed ]
4. Friedman GD, Klatsky AL, Siegelaub AB: Alcohol, tobacco, and hypertension. Hypertension. 1982 Sep-Oct;4(5 Pt 2):III143-50. [PubMed ]
5. Uemura M, Lehmann WD, Schneider W, Seitz HK, Benner A, Keppler-Hafkemeyer A, Hafkemeyer P, Kojima H, Fujimoto M, Tsujii T, Fukui H, Keppler D: Enhanced urinary excretion of cysteinyl leukotrienes in patients with acute alcohol intoxication. Gastroenterology. 2000 Jun;118(6):1140-8. [PubMed ]
6. Hemmingsen R, Barry DI, Hertz MM, Klinken L: Cerebral blood flow and oxygen consumption during ethanol withdrawal in the rat. Brain Res. 1979 Sep 14;173(2):259-69. [PubMed ]
7. Lopez JM, Bombi JA, Valderrama R, Gimenez A, Pares A, Caballeria J, Imperial S, Navarro S: Effects of prolonged ethanol intake and malnutrition on rat pancreas. Gut. 1996 Feb;38(2):285-92. [PubMed ]
8. Yamashina S, Ikejima K, Enomoto N, Takei Y, Sato N: [Ethanol changes sensitivity of Kupffer cells to endotoxin] Nihon Arukoru Yakubutsu Igakkai Zasshi. 2003 Oct;38(5):415-24. [PubMed ]
9. Aye MM, Ma C, Lin H, Bower KA, Wiggins RC, Luo J: Ethanol-induced in vitro invasion of breast cancer cells: the contribution of MMP-2 by fibroblasts. Int J Cancer. 2004 Dec 10;112(5):738-46. [PubMed ]
10. De Martinis BS, de Paula CM, Braga A, Moreira HT, Martin CC: Alcohol distribution in different postmortem body fluids. Hum Exp Toxicol. 2006 Feb;25(2):93-7. [PubMed ]
11. Pohorecky LA: Influence of alcohol on peripheral neurotransmitter function. Fed Proc. 1982 Jun;41(8):2452-5. [PubMed ]
12. Dean RA, Zhang J, Brzezinski MR, Bosron WF: Tissue distribution of cocaine methyl esterase and ethyl transferase activities: correlation with carboxylesterase protein. J Pharmacol Exp Ther. 1995 Nov;275(2):965-71. [PubMed ]
13. Elias AN, Meshkinpour H, Valenta LJ, Grossman MK: Pseudo-Cushing's syndrome: the role of alcohol. J Clin Gastroenterol. 1982 Apr;4(2):137-9. [PubMed ]
14. Henriksson J, Knol M: A single bout of exercise is followed by a prolonged decrease in the interstitial glucose concentration in skeletal muscle. Acta Physiol Scand. 2005 Dec;185(4):313-20. [PubMed ]
15. Rosdahl H, Lind L, Millgard J, Lithell H, Ungerstedt U, Henriksson J: Effect of physiological hyperinsulinemia on blood flow and interstitial glucose concentration in human skeletal muscle and adipose tissue studied by microdialysis. Diabetes. 1998 Aug;47(8):1296-301. [PubMed ]
16. Boschmann M, Adams F, Schaller K, Franke G, Sharma AM, Klaus S, Luft FC, Jordan J: Hemodynamic and metabolic responses to interstitial angiotensin II in normal weight and obese men. J Hypertens. 2006 Jun;24(6):1165-71. [PubMed ]
17. Igawa Y, Satoh T, Mizusawa H, Seki S, Kato H, Ishizuka O, Nishizawa O: The role of capsaicin-sensitive afferents in autonomic dysreflexia in patients with spinal cord injury. BJU Int. 2003 May;91(7):637-41. [PubMed ]
18. Enocksson S, Shimizu M, Lonnqvist F, Nordenstrom J, Arner P: Demonstration of an in vivo functional beta 3-adrenoceptor in man. J Clin Invest. 1995 May;95(5):2239-45. [PubMed ]
19. Collins JW, Macdermott S, Bradbrook RA, Keeley FX Jr, Timoney AG: Is using ethanol-glycine irrigating fluid monitoring and 'good surgical practice' enough to prevent harmful absorption during transurethral resection of the prostate? BJU Int. 2006 Jun;97(6):1247-51. [PubMed ]
20. Sokolik VV, Chursina VS, Artemchuk AA, Artemchuk AF, Bozhko GKh: [Depression of serum esterase and lipoprotein lipase activities in acute and longitudinal actions of ethanol] Biomed Khim. 2006 Jan-Feb;52(1):95-100. [PubMed ]
21. Wikipedia

1. Serum paraoxonase/lactonase 3
2. Serum paraoxonase/arylesterase 1
3. Serum paraoxonase/arylesterase 2
4. Intestinal alkaline phosphatase precursor
5. Lysosomal acid phosphatase precursor
6. Alkaline phosphatase, tissue-nonspecific isozyme precursor
7. Tartrate-resistant acid phosphatase type 5 precursor
8. Alkaline phosphatase, placental-like precursor
9. Aldehyde dehydrogenase, mitochondrial precursor
10. Aldehyde dehydrogenase X, mitochondrial precursor
11. Sulfotransferase family cytosolic 2B member 1
12. Sorbitol dehydrogenase
13. Alcohol dehydrogenase [NADP+]
14. Alcohol dehydrogenase 4
15. Aldehyde dehydrogenase 3B2
16. Aldehyde dehydrogenase 3B1
17. Alcohol dehydrogenase class 3
18. 3-mercaptopyruvate sulfurtransferase
19. Alcohol dehydrogenase 1B
20. Alcohol dehydrogenase class 4 mu/sigma chain
21. Alcohol dehydrogenase 1A
22. Alcohol dehydrogenase 6
23. Alcohol dehydrogenase 1C
24. Beta-glucuronidase precursor
25. Plasma alpha-L-fucosidase precursor
26. Trans-2-enoyl-CoA reductase, mitochondrial precursor
27. Cytochrome P450 2E1
28. Lecithin retinol acyltransferase
29. Orphan nuclear receptor NR1I3
30. Zinc-binding alcohol dehydrogenase domain-containing protein 2
31. Alcohol dehydrogenase iron-containing 1
32. Fatty acyl-CoA reductase 2
33. Acyl-CoA wax alcohol acyltransferase 2
34. cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
35. Klotho precursor
36. Glutamate [NMDA] receptor subunit 3A precursor
37. Gamma-aminobutyric acid receptor subunit alpha-1 precursor
38. Glycine receptor subunit alpha-1 precursor
39. Glycine receptor subunit alpha-2 precursor
40. CDNA FLJ16165 fis, clone BRCOC2019841
41. cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
42. Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
43. Testicular acid phosphatase
44. Carboxylesterase 7
45. cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
46. Acid phosphatase-like protein 2
47. Synaptic vesicle membrane protein VAT-1 homolog-like
48. Putative quinone oxidoreductase
49. Synaptic vesicle membrane protein VAT-1 homolog
50. cDNA FLJ52809, highly similar to Zinc-binding alcohol dehydrogenasedomain-containing protein 2 (EC 1.-.-.-)
51. Reticulon-4-interacting protein 1, mitochondrial

MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL

• Arylesterase (PF01731 )

• 1-

• 5-24

ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATATTCCTCAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCACTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTA

1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
2. Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]

1. PON 1
2. Serum aryldialkylphosphatase 1
3. A-esterase 1
4. Aromatic esterase 1
5. K-45

MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDMEILPN
GLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTF
TDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYG
TNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAEL
LAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPP
ASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL

• gamma-Hexachlorocyclohexane Degradation (map00361 )

• An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol

• Arylesterase (PF01731 )

• 1-

• None

ATGGCGAAGCTGATTGCGCTCACCCTCTTGGGGATGGGACTGGCACTCTTCAGGAACCAC
CAGTCTTCTTACCAAACACGACTTAATGCTCTCCGAGAGGTACAACCCGTAGAACTTCCT
AACTGTAATTTAGTTAAAGGAATCGAAACTGGCTCTGAAGACATGGAGATACTGCCTAAT
GGACTGGCTTTCATTAGCTCTGGATTAAAGTATCCTGGAATAAAGAGCTTCAACCCCAAC
AGTCCTGGAAAAATACTTCTGATGGACCTGAATGAAGAAGATCCAACAGTGTTGGAATTG
GGGATCACTGGAAGTAAATTTGATGTATCTTCATTTAACCCTCATGGGATTAGCACATTC
ACAGATGAAGATAATGCCATGTACCTCCTGGTGGTGAACCATCCAGATGCCAAGTCCACA
GTGGAGTTGTTTAAATTTCAAGAAGAAGAAAAATCGCTTTTGCATCTAAAAACCATCAGA
CATAAACTTCTGCCTAATTTGAATGATATTGTTGCTGTGGGACCTGAGCACTTTTATGGC
ACAAATGATCACTATTTTCTTGACCCCTACTTACAATCCTGGGAGATGTATTTGGGTTTA
GCGTGGTCGTATGTTGTCTACTATAGTCCAAGTGAAGTTCGAGTGGTGGCAGAAGGATTT
GATTTTGCTAATGGAATCAACATTTCACCCGATGGCAAGTATGTCTATATAGCTGAGTTG
CTGGCTCATAAGATTCATGTGTATGAAAAGCATGCTAATTGGACTTTAACTCCATTGAAG
TCCCTTGACTTTAATACCCTCGTGGATAACATATCTGTGGATCCTGAGACAGGAGACCTT
TGGGTTGGATGCCATCCCAATGGCATGAAAATCTTCTTCTATGACTCAGAGAATCCTCCT
GCATCAGAGGTGCTTCGAATCCAGAACATTCTAACAGAAGAACCTAAAGTGACACAGGTT
TATGCAGAAAATGGCACAGTGTTGCAAGGCAGTACAGTTGCCTCTGTGTACAAAGGGAAA
CTGCTGATTGGCACAGTGTTTCACAAAGCTCTTTACTGTGAGCTCTAA

1. Hassett C, Richter RJ, Humbert R, Chapline C, Crabb JW, Omiecinski CJ, Furlong CE: Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence. Biochemistry. 1991 Oct 22;30(42):10141-9. [PubMed ]
2. Adkins S, Gan KN, Mody M, La Du BN: Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes. Am J Hum Genet. 1993 Mar;52(3):598-608. [PubMed ]
3. La Du BN, Adkins S, Kuo CL, Lipsig D: Studies on human serum paraoxonase/arylesterase. Chem Biol Interact. 1993 Jun;87(1-3):25-34. [PubMed ]
4. Furlong CE, Costa LG, Hassett C, Richter RJ, Sundstrom JA, Adler DA, Disteche CM, Omiecinski CJ, Chapline C, Crabb JW, et al.: Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification. Chem Biol Interact. 1993 Jun;87(1-3):35-48. [PubMed ]
5. Clendenning JB, Humbert R, Green ED, Wood C, Traver D, Furlong CE: Structural organization of the human PON1 gene. Genomics. 1996 Aug 1;35(3):586-9. [PubMed ]
6. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
7. Blatter MC, James RW, Messmer S, Barja F, Pometta D: Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase. Eur J Biochem. 1993 Feb 1;211(3):871-9. [PubMed ]
8. Furlong CE, Richter RJ, Chapline C, Crabb JW: Purification of rabbit and human serum paraoxonase. Biochemistry. 1991 Oct 22;30(42):10133-40. [PubMed ]
9. Gan KN, Smolen A, Eckerson HW, La Du BN: Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab Dispos. 1991 Jan-Feb;19(1):100-6. [PubMed ]
10. Sorenson RC, Primo-Parmo SL, Kuo CL, Adkins S, Lockridge O, La Du BN: Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7187-91. [PubMed ]
11. Humbert R, Adler DA, Disteche CM, Hassett C, Omiecinski CJ, Furlong CE: The molecular basis of the human serum paraoxonase activity polymorphism. Nat Genet. 1993 Jan;3(1):73-6. [PubMed ]
12. Marchesani M, Hakkarainen A, Tuomainen TP, Kaikkonen J, Pukkala E, Uimari P, Seppala E, Matikainen M, Kallioniemi OP, Schleutker J, Lehtimaki T, Salonen JT: New paraoxonase 1 polymorphism I102V and the risk of prostate cancer in Finnish men. J Natl Cancer Inst. 2003 Jun 4;95(11):812-8. [PubMed ]

1. PON 2
2. Serum aryldialkylphosphatase 2
3. A-esterase 2
4. Aromatic esterase 2

MGAWVGCGLAGDRAGFLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPN
GLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFI
DNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYAT
NDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADIL
AHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPS
SEVLRIQNILCEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL

• gamma-Hexachlorocyclohexane Degradation (map00361 )

• An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol

• Arylesterase (PF01731 )

• 1-

• None

ATGGGGGCCTGGGTGGGCTGTGGGCTTGCTGGGGATCGCGCTGGCTTCCTGGGCGAGAGG
CTTCTGGCACTCAGAAATCGACTTAAAGCCTCCAGAGAAGTAGAATCTGTAGACCTTCCA
CACTGCCACCTGATTAAAGGAATTGAAGCTGGCTCTGAAGATATTGACATACTTCCCAAT
GGTCTGGCTTTTTTTAGTGTGGGTCTAAAATTCCCAGGACTCCACAGCTTTGCACCAGAT
AAGCCTGGAGGAATACTAATGATGGATCTAAAAGAAGAAAAACCAAGGGCACGGGAATTA
AGAATCAGTCGTGGGTTTGATTTGGCCTCATTCAATCCACATGGCATCAGCACTTTCATA
GACAACGATGACACAGTTTATCTCTTTGTTGTAAACCACCCAGAATTCAAGAATACAGTG
GAAATTTTTAAATTTGAAGAAGCAGAAAATTCTCTGTTGCATCTGAAAACAGTCAAACAT
GAGCTTCTTCCAAGTGTGAATGACATCACAGCTGTTGGACCGGCACATTTCTATGCCACA
AATGACCACTACTTCTCTGATCCTTTCTTAAAGTATTTAGGAACATACTTGAACTTACAC
TGGGCAAATGTTGTTTACTACAGTCCAAATGAAGTTAAAGTGGTAGCAGAAGGATTTGAT
TCAGCAAATGGGATCAATATTTCACCTGATGATAAGTATATCTATGTTGCTGACATATTG
GCTCATGAAATTCATGTTTTGGAAAAACACACTAATATGAATTTAACTCAGTTGAAGGTA
CTTGAGCTGGATACACTGGTGGATAATTTATCTATTGATCCTTCCTCGGGGGACATCTGG
GTAGGCTGTCATCCTAATGGCCAGAAGCTCTTCGTGTATGACCCGAACAATCCTCCCTCG
TCAGAGGTTCTCCGCATCCAGAACATTCTATGTGAGAAGCCTACAGTGACTACAGTTTAT
GCCAACAATGGGTCTGTTCTCCAAGGAAGTTCTGTAGCCTCAGTGTATGATGGGAAGCTG
CTCATAGGCACTTTATACCACAGAGCCTTGTATTGTGAACTCTAA

1. Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]
2. Mochizuki H, Scherer SW, Xi T, Nickle DC, Majer M, Huizenga JJ, Tsui LC, Prochazka M: Human PON2 gene at 7q21.3: cloning, multiple mRNA forms, and missense polymorphisms in the coding sequence. Gene. 1998 Jun 15;213(1-2):149-57. [PubMed ]
3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
4. Ng CJ, Wadleigh DJ, Gangopadhyay A, Hama S, Grijalva VR, Navab M, Fogelman AM, Reddy ST: Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J Biol Chem. 2001 Nov 30;276(48):44444-9. Epub 2001 Sep 28. [PubMed ]
5. Hegele RA, Connelly PW, Scherer SW, Hanley AJ, Harris SB, Tsui LC, Zinman B: Paraoxonase-2 gene (PON2) G148 variant associated with elevated fasting plasma glucose in noninsulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1997 Oct;82(10):3373-7. [PubMed ]
6. Sanghera DK, Aston CE, Saha N, Kamboh MI: DNA polymorphisms in two paraoxonase genes (PON1 and PON2) are associated with the risk of coronary heart disease. Am J Hum Genet. 1998 Jan;62(1):36-44. [PubMed ]

1. IAP

MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP

• Folate and Pterine Biosynthesis (map00790 )
• gamma-Hexachlorocyclohexane Degradation (map00361 )

• A phosphate monoester + H2O = an alcohol + phosphate

• Alk_phosphatase (PF00245 )

• 1-19

ATGCAGGGGCCCTGGGTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCGTC
ATCCCAGCTGAGGAGGAGAACCCGGCCTTCTGGAACCGCCAGGCAGCTGAGGCCCTGGAT
GCTGCCAAGAAGCTGCAGCCCATCCAGAAGGTCGCCAAGAACCTCATCCTCTTCCTGGGC
GATGGGTTGGGGGTGCCCACGGTGACAGCCACCAGGATCCTAAAGGGGCAGAAGAATGGC
AAACTGGGGCCTGAGACGCCCCTGGCCATGGACCGCTTCCCATACCTGGCTCTGTCCAAG
ACATACAATGTGGACAGACAGGTGCCAGACAGCGCAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGCCAACTTCCAGACCATCGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAATGAGGTCATCTCCGTGATGAACCGGGCCAAGCAAGCAGGAAAG
TCAGTAGGAGTGGTGACCACCACACGGGTGCAGCACGCCTCGCCAGCCGGCACCTACGCA
CACACAGTGAACCGCAACTGGTACTCAGATGCTGACATGCCTGCCTCAGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACTCAGCTCATCTCCAACATGGACATTGACGTGATCCTTGGC
GGAGGCCGCAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGCTGATGCC
AGCCAGAATGGAATCAGGCTGGACGGGAAGAACCTGGTGCAGGAATGGCTGGCAAAGCAC
CAGGGTGCCTGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCGTCCCTGGACCAGTCT
GTGACCCATCTCATGGGCCTCTTTGAGCCCGGAGACACGAAATATGAGATCCTCCGAGAC
CCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTGCTGAGCAGG
AACCCCCGCGGCTTCTACCTCTTTGTGGAGGGCGGCCGCATCGACCATGGTCATCATGAG
GGTGTGGCTTACCAGGCAGTCACTGAGGCGGTCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGACCCTCGTCACCGCTGACCACTCCCATGTC
TTCTCCTTTGGTGGCTACACCTTGCGAGGGAGCTCCATCTTCGGGTTGGCCCCCAGCAAG
GCTCAGGACAGCAAAGCCTACACGTCCATCCTGTACGGCAATGGCCCGGGCTACGTGTTC
AACTCAGGCGTGCGACCAGACGTGAATGAGAGCGAGAGCGGGAGCCCCGATTACCAGCAG
CAGGCGGCGGTGCCCCTGTCGTCCGAGACCCACGGAGGCGAAGACGTGGCGGTGTTTGCG
CGCGGCCCGCAGGCGCACCTGGTGCATGGTGTGCAGGAGCAGAGCTTCGTAGCGCATGTC
ATGGCCTTCGCTGCCTGTCTGGAGCCCTACACGGCCTGCGACCTGGCGCTCCCCGCCTGC
ACCACCGACGCCGCGCACCCAGTTGCCGCGTCGCTGCCACTGCTGGCCGGGACCCTGCTG
CTGCTGGGGGCGTCCGCTGCTCCCTGA

1. Berger J, Garattini E, Hua JC, Udenfriend S: Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. [PubMed ]
2. Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. [PubMed ]
3. Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H: Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12011-9. [PubMed ]
4. Millan JL: Promoter structure of the human intestinal alkaline phosphatase gene. Nucleic Acids Res. 1987 Dec 23;15(24):10599. [PubMed ]
5. Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed ]
6. Hua JC, Berger J, Pan YC, Hulmes JD, Udenfriend S: Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2368-72. [PubMed ]

1. LAP

MAGKRSGWSRAALLQLLLGVNLVVMPPTRARSLRFVTLLYRHGDRSPVKTYPKDPYQEEE
WPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAG
LFPPNGMQRFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNESS
RNAQFLDMVANETGLTDLTLETVWNVYDTLFCEQTHGLRLPPWASPQTMQRLSRLKDFSF
RFLFGIYQQAEKARLQGGVLLAQIRKNLTLMATTSQLPKLLVYSAHDTTLVALQMALDVY
NGEQAPYASCHIFELYQEDSGNFSVEMYFRNESDKAPWPLSLPGCPHRCPLQDFLRLTEP
VVPKDWQQECQLASGPADTEVIVALAVCGSILFLLIVLLLTVLFRMQAQPPGYRHVADGE
DHA

• gamma-Hexachlorocyclohexane Degradation (map00361 )
• Riboflavin Metabolism (map00740 )

• A phosphate monoester + H2O = an alcohol + phosphate

• Acid_phosphat_A (PF00328 )

• 1-30

• 382-404

ATGGCGGGCAAGCGGTCCGGCTGGAGCCGGGCGGCTCTCCTCCAGCTCCTTCTCGGCGTG
AACCTGGTGGTGATGCCGCCCACCCGGGCCCGGAGTCTGCGCTTCGTTACCTTGCTGTAC
CGCCATGGAGACCGTTCACCAGTGAAGACATATCCCAAGGACCCCTATCAGGAAGAAGAA
TGGCCCCAGGGGTTTGGTCAGTTAACCAAGGAGGGGATGCTACAGCACTGGGAACTGGGC
CAGGCCCTGCGGCAGCGCTATCACGGCTTCCTAAACACCTCTTATCACCGGCAAGAGGTT
TATGTGCGAAGCACAGACTTTGACCGGACTCTCATGAGTGCTGAGGCCAACCTGGCTGGA
CTCTTCCCTCCCAACGGGATGCAGCGCTTCAACCCGAACATCTCGTGGCAGCCTATTCCT
GTGCACACTGTGCCCATCACTGAGGACAGGCTGCTGAAGTTCCCGTTGGGCCCATGTCCC
CGTTATGAGCAGCTGCAGAACGAGACCCGGCAGACACCAGAGTATCAGAATGAGAGTTCT
CGGAATGCACAATTTCTGGACATGGTGGCCAACGAGACAGGGCTTACAGACCTGACACTG
GAGACCGTCTGGAATGTCTATGACACACTCTTCTGTGAGCAAACGCACGGGCTGCGCCTG
CCGCCCTGGGCCTCACCCCAAACCATGCAGCGTCTCAGCCGGCTAAAGGACTTCAGCTTC
CGCTTCCTCTTCGGAATCTACCAGCAGGCGGAGAAGGCCCGGCTTCAGGGGGGAGTCCTG
CTGGCTCAGATAAGGAAGAACCTGACCCTAATGGCGACCACCTCCCAGCTCCCCAAGCTG
CTGGTTTACTCTGCGCACGACACTACCCTGGTTGCCCTGCAAATGGCACTGGATGTCTAC
AATGGTGAACAAGCCCCCTACGCCTCCTGCCACATATTTGAACTGTACCAGGAAGATTCT
GGGAATTTCTCAGTGGAGATGTACTTTCGGAACGAGAGTGACAAGGCCCCCTGGCCGCTC
AGCCTGCCTGGCTGCCCTCACCGCTGCCCACTGCAGGACTTCCTTCGCCTCACAGAGCCC
GTCGTGCCCAAGGATTGGCAGCAGGAGTGCCAGCTGGCAAGCGGTCCTGCAGACACAGAG
GTGATTGTGGCCTTGGCTGTATGTGGCTCCATCCTCTTCCTCCTCATAGTGCTGCTCCTC
ACCGTCCTCTTCCGGATGCAGGCCCAGCCTCCTGGCTACCGCCACGTCGCAGATGGGGAG
GACCACGCCTGA

1. Pohlmann R, Krentler C, Schmidt B, Schroder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S, et al.: Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EMBO J. 1988 Aug;7(8):2343-50. [PubMed ]
2. Geier C, von Figura K, Pohlmann R: Structure of the human lysosomal acid phosphatase gene. Eur J Biochem. 1989 Aug 15;183(3):611-6. [PubMed ]
3. Nadler HL, Egan TJ: Deficiency of lysosomal acid phosphatase. A new familial metabolic disorder. N Engl J Med. 1970 Feb 5;282(6):302-7. [PubMed ]

1. AP-TNAP
2. TNSALP
3. Alkaline phosphatase liver/bone/kidney isozyme

MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF

• Folate and Pterine Biosynthesis (map00790 )
• gamma-Hexachlorocyclohexane Degradation (map00361 )

• A phosphate monoester + H2O = an alcohol + phosphate

• Alk_phosphatase (PF00245 )

• 1-17

ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA

1. Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed ]
2. Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed ]
3. Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed ]
4. Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed ]
5. Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed ]
6. Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed ]
7. Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed ]
8. Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed ]
9. Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed ]
10. Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed ]
11. Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed ]
12. Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed ]
13. Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed ]
14. Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed ]
15. Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed ]
16. Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed ]
17. Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed ]
18. Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed ]
19. Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed ]

1. TR- AP
2. Tartrate-resistant acid ATPase
3. TrATPase
4. Acid phosphatase 5, tartrate resistant

MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP

• gamma-Hexachlorocyclohexane Degradation (map00361 )
• Riboflavin Metabolism (map00740 )

• A phosphate monoester + H2O = an alcohol + phosphate

• Metallophos (PF00149 )

• 1-21

ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA

1. Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed ]
2. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed ]
3. Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed ]
4. Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed ]
5. Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed ]
6. Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed ]
7. Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed ]

1. Alkaline phosphatase Nagao isozyme
2. Germ-cell alkaline phosphatase
3. GCAP
4. PLAP-like
5. ALP-1

MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP

• Folate and Pterine Biosynthesis (map00790 )
• gamma-Hexachlorocyclohexane Degradation (map00361 )

• A phosphate monoester + H2O = an alcohol + phosphate

• Alk_phosphatase (PF00245 )

• 1-19

ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATGTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGGTGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCACCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCCCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA

1. Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed ]
2. Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed ]
3. Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed ]
4. Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed ]
5. Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed ]

1. ALDH class 2
2. ALDHI
3. ALDH-E2

MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS

• 1,2-Dichloroethane degradation (map00631 )
• Arginine and Proline Metabolism (map00330 )
• Ascorbate and aldarate metabolism (map00053 )
• Beta Alanine Metabolism (map00410 )
• Bile Acid Biosynthesis (map00120 )
• Butyrate Metabolism (map00650 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Histidine Metabolism (map00340 )
• Limonene and pinene degradation (map00903 )
• Lysine Degradation (map00310 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )
• Tryptophan Metabolism (map00380 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• an aldehyde + NAD+ + H2O = an acid + NADH + H+

• Aldedh (PF00171 )

• 1-24

ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA

1. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed ]
2. Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed ]
3. Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed ]
4. Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed ]
5. Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed ]
6. Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed ]
7. Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed ]
8. Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed ]
9. Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed ]
10. Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed ]
11. Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed ]

1. Aldehyde dehydrogenase family 1 member B1
2. ALDH class 2

MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS

• 1,2-Dichloroethane degradation (map00631 )
• Arginine and Proline Metabolism (map00330 )
• Ascorbate and aldarate metabolism (map00053 )
• Beta Alanine Metabolism (map00410 )
• Bile Acid Biosynthesis (map00120 )
• Butyrate Metabolism (map00650 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Histidine Metabolism (map00340 )
• Limonene and pinene degradation (map00903 )
• Lysine Degradation (map00310 )
• Propanoate Metabolism (map00640 )
• Pyruvate Metabolism (map00620 )
• Tryptophan Metabolism (map00380 )
• Valine, Leucine and Isoleucine Degradation (map00280 )

• an aldehyde + NAD+ + H2O = an acid + NADH + H+

• Aldedh (PF00171 )

• 1-22

ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCTCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGCATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAA

1. Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed ]
2. Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed ]

1. Sulfotransferase 2B1
2. Alcohol sulfotransferase
3. Hydroxysteroid sulfotransferase 2

MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRD
DDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPR
LMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFL
KGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSV
VAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQ
MRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETP
HPRPS

• Androgen and Estrogen Metabolism (map00150 )
• Sulfate and Sulfite Metabolism (map00920 )

• 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate

• Sulfotransfer_1 (PF00685 )

• None

• None

ATGGCGTCTCCCCCACCTTTCCACAGCCAGAAGTTGCCAGGTGAATACTTCCGGTACAAG
GGCGTCCCCTTCCCCGTCGGCCTGTACTCGCTCGAGAGCATCAGCTTGGCGGAGAACACC
CAAGATGTGCGGGACGACGACATCTTTATCATCACCTACCCCAAGTCAGGCACGACCTGG
ATGATCGAGATCATCTGCTTAATCCTGAAGGAAGGGGATCCATCCTGGATCCGCTCCGTG
CCCATCTGGGAGCGGGCACCCTGGTGTGAGACCATTGTGGGTGCTTTCAGCCTCCCGGAC
CAGTACAGCCCCCGCCTCATGAGCTCCCATCTTCCCATCCAGATCTTCACCAAGGCCTTC
TTCAGCTCCAAGGCCAAGGTGATCTACATGGGCCGCAACCCCCGGGACGTTGTGGTCTCC
CTCTATCATTACTCCAAGATCGCCGGGCAGTTAAAGGACCCGGGCACACCCGACCAGTTC
CTGAGGGACTTCCTCAAAGGCGAAGTGCAGTTTGGCTCCTGGTTCGACCACATTAAGGGC
TGGCTTCGGATGAAGGGCAAAGACAACTTCCTATTTATCACCTACGAGGAGCTGCAGCAG
GACTTACAGGGCTCCGTGGAGCGCATCTGTGGGTTCCTGGGCCGTCCGCTGGGCAAGGAG
GCACTGGGCTCCGTCGTGGCACACTCAACCTTCAGCGCCATGAAGGCCAACACCATGTCC
AACTACACGCTGCTGCCTCCCAGCCTGCTGGACCACCGTCGCGGGGCCTTCCTCCGGAAA
GGGGTCTGCGGCGACTGGAAGAACCACTTCACGGTGGCCCAGAGCGAAGCCTTCGATCGT
GCCTACCGCAAGCAGATGCGGGGGATGCCGACCTTCCCCTGGGATGAAGACCCGGAGGAG
GATGGCAGCCCAGATCCTGAGCCCAGCCCTGAGCCTGAGCCCAAGCCCAGCCTTGAGCCC
AACACCAGCCTGGAGCGTGAGCCCAGACCCAACTCCAGCCCCAACCCCAGCCCCGGCCAG
GCCTCTGAGACCCCGCACCCACGACCCTCATAA

1. Her C, Wood TC, Eichler EE, Mohrenweiser HW, Ramagli LS, Siciliano MJ, Weinshilboum RM: Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics. 1998 Nov 1;53(3):284-95. [PubMed ]
2. Fuda H, Lee YC, Shimizu C, Javitt NB, Strott CA: Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem. 2002 Sep 27;277(39):36161-6. Epub 2002 Jul 26. [PubMed ]
3. Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC: Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem. 2003 Nov 7;278(45):44593-9. Epub 2003 Aug 14. [PubMed ]

1. L-iditol 2-dehydrogenase

MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNF
IVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFC
ATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCG
AGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGLL
GCKPEVTIECTGAEASIQAGIYATRSGGTLVLVGLGSEMTTVPLLHAAIREVDIKGVFRY
CNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP

• Fructose and Mannose Metabolism (map00051 )

• L-iditol + NAD+ = L-sorbose + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGGCGGCGGCGGCCAAGCCCAACAACCTTTCCCTGGTGGTGCACGGACCGGGGGACTTG
CGCCTGGAGAACTATCCTATCCCTGAACCAGGCCCAAATGAGGTCTTGCTGAGGATGCAT
TCTGTTGGAATCTGTGGCTCAGATGTCCACTACTGGGAGTATGGTCGAATTGGGAATTTT
ATTGTGAAAAAGCCCATGGTGCTGGGACATGAAGCTTCGGGAACAGTCGAAAAAGTGGGA
TCATCGGTAAAGCACCTAAAACCAGGTGATCGTGTTGCCATCGAGCCTGGTGCTCCCCGA
GAAAATGATGAATTCTGCAAGATGGGCCGATACAATCTGTCACCTTCCATCTTCTTCTGT
GCCACGCCCCCCGATGACGGGAACCTCTGCCGGTTCTATAAGCACAATGCAGCCTTTTGT
TACAAGCTTCCTGACAATGTCACCTTTGAGGAAGGCGCCCTGATCGAGCCACTTTCTGTG
GGGATCCATGCCTGCAGGAGAGGCGGAGTTACCCTGGGACACAAGGTCCTTGTGTGTGGA
GCTGGGCCAATCGGGATGGTCACTTTGCTCGTGGCCAAAGCAATGGGAGCAGCTCAAGTA
GTGGTGACTGATCTGTCTGCTACCCGATTGTCCAAAGCCAAGGAGATTGGGGCTGATTTA
GTCCTCCAGATCTCCAAGGAGAGCCCTCAGGAAATCGCCAGGAAAGTAGAAGGTCAGCTG
GGGTGCAAGCCGGAAGTCACCATCGAGTGCACGGGGGCAGAGGCCTCCATCCAGGCGGGC
ATCTACGCCACTCGCTCTGGTGGGACCCTCGTGCTTGTGGGGCTGGGCTCTGAGATGACC
ACCGTACCCCTACTGCATGCAGCCATCCGGGAGGTGGATATCAAGGGCGTGTTTCGATAC
TGCAACACGTGGCCAGTGGCGATTTCGATGCTTGCGTCCAAGTCTGTGAATGTAAAACCC
CTCGTCACCCATAGGTTTCCTCTGGAGAAAGCTCTGGAGGCCTTTGAAACATTTAAAAAG
GGATTGGGGTTGAAAATCATGCTCAAGTGTGACCCCAGTGACCAGAATCCCTGA

1. Lee FK, Cheung MC, Chung S: The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization. Genomics. 1994 May 15;21(2):354-8. [PubMed ]
2. Iwata T, Popescu NC, Zimonjic DB, Karlsson C, Hoog JO, Vaca G, Rodriguez IR, Carper D: Structural organization of the human sorbitol dehydrogenase gene (SORD). Genomics. 1995 Mar 1;26(1):55-62. [PubMed ]
3. Carr IM, Markham AF, Coletta PL: Identification and characterisation of a sequence related to human sorbitol dehydrogenase. Eur J Biochem. 1997 May 1;245(3):760-7. [PubMed ]
4. Karlsson C, Maret W, Auld DS, Hoog JO, Jornvall H: Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme. Eur J Biochem. 1989 Dec 22;186(3):543-50. [PubMed ]
5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]

1. Aldehyde reductase
2. Aldo- keto reductase family 1 member A1

MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEAL
KEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFER
GDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRP
AVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEK
YGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIV
PMLTVDGKRVPRDAGHPLYPFNDPY

• Caprolactam degradation (map00930 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )

• an alcohol + NADP+ = an aldehyde + NADPH + H+

• Aldo_ket_red (PF00248 )

• None

• None

ATGGCGGCTTCCTGTGTTCTACTGCACACTGGGCAGAAGATGCCTCTGATTGGTCTGGGT
ACCTGGAAGAGTGAGCCTGGTCAGGTAAAAGCAGCTGTTAAGTATGCCCTTAGCGTAGGC
TACCGCCACATTGATTGTGCTGCTATCTACGGCAATGAGCCTGAGATTGGGGAGGCCCTG
AAGGAGGACGTGGGACCAGGCAAGGCGGTGCCTCGGGAGGAGCTGTTTGTGACATCCAAG
CTGTGGAACACCAAGCACCACCCCGAGGATGTGGAGCCTGCCCTCCGGAAGACTCTGGCT
GACCTCCAGCTGGAGTATCTGGACCTGTACCTGATGCACTGGCCTTATGCCTTTGAGCGG
GGAGACAACCCCTTCCCCAAGAATGCTGATGGGACTATATGCTACGACTCCACCCACTAC
AAGGAGACTTGGAAGGCTCTGGAGGCACTGGTGGCTAAGGGGCTGGTGCAGGCGCTGGGC
CTGTCCAACTTCAACAGTCGGCAGATTGATGACATACTCAGTGTGGCCTCCGTGCGTCCA
GCTGTCTTGCAGGTGGAATGCCACCCATACTTGGCTCAAAATGAGCTAATTGCCCACTGC
CAAGCACGTGGCTTGGAGGTAACTGCTTATAGCCCTTTGGGCTCCTCTGATCGTGCATGG
CGTGATCCTGATGAGCCTGTCCTGCTGGAGGAACCAGTAGTCCTGGCATTGGCTGAAAAG
TATGGCCGATCTCCAGCTCAGATCTTGCTCAGGTGGCAGGTCCAGCGGAAAGTGATCTGC
ATCCCCAAAAGTATCACTCCTTCTCGAATCCTTCAGAACATCAAGGTGTTTGACTTCACC
TTTAGCCCAGAAGAGATGAAGCAGCTAAATGCCCTGAACAAAAATTGGAGATATATTGTG
CCTATGCTTACGGTGGATGGGAAGAGAGTCCCAAGGGATGCAGGGCATCCTCTGTACCCC
TTTAATGACCCGTACTGA

1. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989 Jun 5;264(16):9547-51. [PubMed ]
2. Barski OA, Gabbay KH, Bohren KM: Characterization of the human aldehyde reductase gene and promoter. Genomics. 1999 Sep 1;60(2):188-98. [PubMed ]
3. Wermuth B, Omar A, Forster A, di Francesco C, Wolf M, von Wartburg JP, Bullock B, Gabbay KH: Primary structure of aldehyde reductase from human liver. Prog Clin Biol Res. 1987;232:297-307. [PubMed ]
4. Barski OA, Gabbay KH, Grimshaw CE, Bohren KM: Mechanism of human aldehyde reductase: characterization of the active site pocket. Biochemistry. 1995 Sep 5;34(35):11264-75. [PubMed ]

1. Alcohol dehydrogenase class II pi chain

MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEG
LAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLK
SPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGC
GFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKA
LGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGV
AAGSKGLTVFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDK
ISEAFDLMNQGKSIRTILIF

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGGGCACCAAGGGCAAAGTTATTAAATGCAAAGCAGCCATCGCCTGGGAAGCAGGCAAG
CCCCTTTGCATTGAAGAGGTTGAAGTAGCTCCCCCCAAGGCTCATGAAGTTCGCATTCAG
ATCATTGCTACCTCCCTGTGCCATACTGATGCCAGTGTTATCGATTCTAAATTTGAGGGC
CTAGCTTTCCCAGTGATCGTTGGCCATGAGGCTGCAGGTATTGTGGAAAGTATTGGGCCA
GGAGTGACCAACGTCAAACCAGGTGACAAAGTAATTCCACTTTATGCACCTCTATGTAGA
AAATGCAAGTTTTGTCTGAGTCCACTCACAAATTTGTGTGGGAAAATCAGTAATCTCAAA
AGTCCTGCTAGTGATCAACAACTAATGGAAGACAAAACCAGCAGGTTTACCTGCAAAGGA
AAACCAGTTTACCATTTCTTTGGAACCAGTACATTCTCTCAGTACACTGTGGTGTCAGAT
ATCAATCTTGCCAAAATAGATGATGATGCAAATTTAGAGAGAGTTTGTCTGCTTGGATGT
GGGTTTTCAACTGGCTATGGGGCTGCAATCAACAATGCCAAGGTCACCCCTGGTTCGACT
TGTGCTGTCTTTGGCCTAGGAGGTGTGGGTCTTTCTGCTGTAATGGGTTGTAAAGCAGCA
GGAGCTTCCAGAATCATAGGTATTGACATCAACAGTGAGAAGTTTGTGAAGGCTAAAGCC
CTGGGAGCCACTGACTGCCTCAATCCTAGAGACTTACATAAACCGATCCAGGAAGTTATC
ATTGAATTGACCAAGGGAGGTGTGGATTTTGCCCTTGACTGTGCAGGTGGATCTGAAACC
ATGAAAGCAGCCCTGGACTGTACAACCGCAGGCTGGGGATCATGTACTTTCATTGGAGTA
GCTGCTGGTAGCAAAGGATTGACTATTTTTCCAGAGGAGCTAATAATCGGCCGTACTATA
AATGGAACATTCTTTGGTGGTTGGAAAAGTGTAGATTCTATCCCAAAGCTGGTCACTGAC
TATAAGAATAAGAAATTCAATCTGGATGCATTGGTGACCCATACCCTGCCTTTTGACAAA
ATCAGTGAGGCATTTGACCTAATGAACCAAGGAAAAAGCGTCCGAACAATCCTCATCTTT
GGAAGATGCCAGGAGCAATTCAGAATACTATCTGATTGA

1. Hoog JO, von Bahr-Lindstrom H, Heden LO, Holmquist B, Larsson K, Hempel J, Vallee BL, Jornvall H: Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit. Biochemistry. 1987 Apr 7;26(7):1926-32. [PubMed ]
2. von Bahr-Lindstrom H, Jornvall H, Hoog JO: Cloning and characterization of the human ADH4 gene. Gene. 1991 Jul 22;103(2):269-74. [PubMed ]

1. Aldehyde dehydrogenase 8

MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGNCVVLKPSE
ISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAAT
KHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLL
PALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSNESDRYIAPTVL
VDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERT
SSGSFGGNEGFTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEI
RYPPYTDWNQQLLRWGMGSQSCTLL

• Gluconeogenesis (map00010 )
• Histidine Metabolism (map00340 )
• Phenylalanine Metabolism (map00360 )
• Tyrosine Metabolism (map00350 )

• an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+

• Aldedh (PF00171 )

• None

• None

ATGAAGGATGAACCACGGTCCACGAACCTGTTCATGAAGCTGGACTCGGTCTTCATCTGG
AAGGAACCCTTTGGCCTGGTCCTCATCATCGCACCCTGGAACTACCCATTGAACCTGACC
CTGGTGCTCCTGGTGGGCACCCTCCCCGCAGGGAATTGCGTGGTGCTGAAGCCGTCAGAA
ATCAGCCAGGGCACAGAGAAGGTCCTGGCTGAGGTGCTGCCCCAGTACCTGGACCAGAGC
TGCTTTGCCGTGGTGCTGGGCGGACCCCAGGAGACAGGGCAGCTGCTAGAGCACAAGTTG
GACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTCATGACTGCTGCCACC
AAGCACCTGACGCCTGTCACCCTGGAGCTGGGGGGCAAGAACCCCTGCTACGTGGACGAC
AACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCTGCTACTTCAATGCCGGC
CAGACCTGCGTGGCCCCTGACTACGTCCTGTGCAGCCCCGAGATGCAGGAGAGGCTGCTG
CCCGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCAAAC
CTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGCGGC
CGCGTGGCCATTGGGGGCCAGAGCAACGAGAGCGATCGCTACATCGCCCCCACGGTGCTG
GTGGACGTGCAGGAGACGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTGCCC
ATCGTGAACGTGCAGAGCGTGGACGAGGCCATCAAGTTCATCAACCGGCAGGAGAAGCCC
CTGGCCCTGTACGCCTTCTCCAACAGCAGACAGGTTGTGAACCAGATGCTGGAGCGGACC
AGCAGCGGCAGCTTTGGAGGCAATGAGGGCTTCACCTACATATCTCTGCTGTCCGTGCCA
TTCGGGGGAGTCGGCCACAGTGGGATGGGCCGGTACCACGGCAAGTTCACCTTCGACACC
TTCTCCCACCACCGCACCTGCCTGCTCGCCCCCTCCGGCCTGGAGAAATTAAAGGAGATC
CGCTACCCACCCTATACCGACTGGAACCAGCAGCTGTTACGCTGGGGCATGGGCTCCCAG
AGCTGCACCCTCCTGTGA

1. Hsu LC, Chang WC, Lin SW, Yoshida A: Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isozymes. Adv Exp Med Biol. 1995;372:159-68. [PubMed ]
2. Hsu LC, Chang WC: Sequencing and expression of the human ALDH8 encoding a new member of the aldehyde dehydrogenase family. Gene. 1996 Oct 3;174(2):319-22. [PubMed ]

1. Aldehyde dehydrogenase 7

MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESE
VSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNL
TLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHR
FDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNA
GQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGC
GRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREK
PLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFD
TFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL

• Gluconeogenesis (map00010 )
• Histidine Metabolism (map00340 )
• Phenylalanine Metabolism (map00360 )
• Tyrosine Metabolism (map00350 )

• an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+

• Aldedh (PF00171 )

• None

• None

ATGGACCCCCTTGGGGACACGCTGCGGCGACTGCGGGAGGCCTTCCACGCGGGGCGCACG
CGGCCAGCTGAGTTCCGGGCTGCGCAGCTCCAAGGCCTGGGCCGCTTCCTGCAAGAAAAC
AAGCAGCTTCTGCACGACGCACTGGCCCAGGACCTGCACAAGTCAGCCTTCGAGTCGGAG
GTGTCTGAGGTTGCCATCAGCCAGGGCGAGGTCACCCTGGCCCTCAGGAACCTCCGGGCC
TGGATGAAGGACGAGCGTGTGCCCAAGAACCTGGCCACGCAGCTGGACTCCGCCTTCATC
CGGAAGGAGCCCTTTGGCCTGGTCCTCATCATTGCGCCCTGGAACTATCCGCTGAACCTG
ACGCTGGTGCCCCTCGTGGGAGCCCTCGCTGCAGGGAACTGTGTGGTGCTGAAGCCATCG
GAGATTAGCAAGAACGTCGAGAAGATCCTGGCCGAGGTGCTGCCCCAATACGTGGACCAG
AGCTGCTTTGCTGTGGTGCTGGGCGGGCCCCAGGAGACGGGGCAGCTGCTAGAGCACAGG
TTCGACTACATCTTCTTCACAGGGAGCCCTCGTGTGGGCAAGATTGTTATGACTGCTGCC
GCCAAGCACCTGACACCTGTCACCCTGGAGCTGGGGGGCAAGAACCCTTGCTACGTGGAC
GACAACTGCGACCCCCAGACCGTGGCCAACCGCGTGGCCTGGTTCCGCTACTTCAACGCC
GGCCAGACCTGCGTGGCCCCCGACTACGTCCTATGCAGCCCTGAGATGCAGGAGAGGCTG
CTGCCTGCCCTGCAGAGCACCATCACCCGTTTCTATGGCGACGACCCCCAGAGCTCCCCA
AACCTGGGCCGCATCATCAACCAGAAACAGTTCCAGCGGCTGCGGGCATTGCTGGGCTGC
GGCCGTGTGGCCATTGGGGGCCAGAGCGATGAGAGCGATCGCTACATCGCCCCCACGGTG
CTGGTGGATGTGCAGGAGATGGAGCCTGTGATGCAGGAGGAGATCTTCGGGCCCATCCTG
CCCATCGTGAACGTGCAGAGCTTGGACGAGGCCATCGAGTTCATCAACCGGCGGGAGAAG
CCCCTGGCCCTGTACGCCTTCTCCAACAGCAGCCAGGTGGTCAAGCGGGTGCTGACCCAG
ACCAGCAGCGGGGGCTTCTGTGGGAACGACGGCTTCATGCACATGACCCTGGCCAGCCTG
CCTTTTGGAGGAGTGGGTGCCAGTGGGATGGGCCGGTACCATGGCAAGTTCTCCTTCGAC
ACCTTCTCCCACCATCGCGCCTGCCTCCTGCGCAGCCCGGGGATGGAGAAGCTCAACGCC
CTCCGCTACCCGCCGCAATCGCCGCGCCGCCTGAGGATGCTGCTGGTGGCCATGGAGGCC
CAAGGCTGCAGCTGCACACTGCTCTGA

1. Hsu LC, Chang WC, Yoshida A: Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene. 1994 Dec 30;151(1-2):285-9. [PubMed ]

1. Alcohol dehydrogenase class III
2. Alcohol dehydrogenase class chi chain
3. S-
4. hydroxymethylglutathione dehydrogenase
5. Glutathione- dependent formaldehyde dehydrogenase
6. FDH

MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGC
FPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGK
GLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGY
GAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATEC
INPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEE
IATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFE
LMHSGKSIRTVVKI

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGGCGAACGAGGTTATCAAGTGCAAGGCTGCAGTTGCTTGGGAGGCTGGAAAGCCTCTC
TCCATAGAGGAGATAGAGGTGGCACCCCCAAAGGCTCATGAAGTTCGAATCAAGATCATT
GCCACTGCGGTTTGCCACACCGATGCCTATACCCTGAGTGGAGCTGATCCTGAGGGTTGT
TTTCCAGTGATCTTGGGACATGAAGGTGCTGGAATTGTGGAAAGTGTTGGTGAGGGAGTT
ACTAAGCTGAAGGCGGGTGACACTGTCATCCCACTTTACATCCCACAGTGTGGAGAATGC
AAATTTTGTCTAAATCCTAAAACTAACCTTTGCCAGAAGATAAGAGTCACTCAAGGGAAA
GGATTAATGCCAGATGGTACCAGCAGATTTACTTGCAAAGGAAAGACAATTTTGCATTAC
ATGGGAACCAGCACATTTTCTGAATACACAGTTGTGGCTGATATCTCTGTTGCTAAAATA
GATCCTTTAGCACCTTTGGATAAAGTCTGCCTTCTAGGTTGTGGCATTTCAACCGGTTAT
GGTGCTGCTGTGAACACTGCCAAGTTGGAGCCTGGCTCTGTTTGTGCCGTCTTTGGTCTG
GGAGGAGTCGGATTGGCAGTTATCATGGGCTGTAAAGTGGCTGGTGCTTCCCGGATCATT
GGTGTGGACATCAATAAAGATAAATTTGCAAGGGCCAAAGAGTTTGGAGCCACTGAATGT
ATTAACCCTCAGGATTTTAGTAAACCCATCCAGGAAGTGCTCATTGAGATGACCGATGGA
GGAGTGGACTATTCCTTTGAATGTATTGGTAATGTGAAGGTCATGAGAGCAGCACTTGAG
GCATGTCACAAGGGCTGGGGCGTCAGCGTCGTGGTTGGAGTAGCTGCTTCAGGTGAAGAA
ATTGCCACTCGTCCATTCCAGCTGGTAACAGGTCGCACATGGAAAGGCACTGCCTTTGGA
GGATGGAAGAGTGTAGAAAGTGTCCCAAAGTTGGTGTCTGAATATATGTCCAAAAAGATA
AAAGTTGATGAATTTGTGACTCACAATCTGTCTTTTGATGAAATCAACAAAGCCTTTGAA
CTGATGCATTCTGGAAAGAGCATTCGAACTGTTGTAAAGATTTAA

1. Sharma CP, Fox EA, Holmquist B, Jornvall H, Vallee BL: cDNA sequence of human class III alcohol dehydrogenase. Biochem Biophys Res Commun. 1989 Oct 31;164(2):631-7. [PubMed ]
2. Giri PR, Krug JF, Kozak C, Moretti T, O'Brien SJ, Seuanez HN, Goldman D: Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA. Biochem Biophys Res Commun. 1989 Oct 16;164(1):453-60. [PubMed ]
3. Hur MW, Edenberg HJ: Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase. Gene. 1992 Nov 16;121(2):305-11. [PubMed ]
4. Kaiser R, Holmquist B, Hempel J, Vallee BL, Jornvall H: Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes. Biochemistry. 1988 Feb 23;27(4):1132-40. [PubMed ]
5. Holmquist B, Moulis JM, Engeland K, Vallee BL: Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase. Biochemistry. 1993 May 18;32(19):5139-44. [PubMed ]
6. Engeland K, Hoog JO, Holmquist B, Estonius M, Jornvall H, Vallee BL: Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2491-4. [PubMed ]
7. Yang ZN, Bosron WF, Hurley TD: Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J Mol Biol. 1997 Jan 24;265(3):330-43. [PubMed ]

1. MST

MASPQLCRALVSAQWVAEALRAPRAGQPLQLLDASWYLPKLGRDARREFEERHIPGAAFF
DIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAF
GHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQV
VDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDL
SKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRARPEDVISEGRGKTH

• Cysteine Metabolism (map00272 )

• 3-mercaptopyruvate + cyanide = pyruvate + thiocyanate

• Rhodanese (PF00581 )

• None

• None

ATGGCTTCGCCGCAGCTCTGCCGCGCGCTGGTGTCGGCGCAATGGGTGGCGGAGGCGCTG
CGGGCCCCGCGCGCTGGGCAGCCTCTGCAGCTGCTGGACGCCTCCTGGTACCTGCCGAAG
CTGGGGCGCGACGCGACGCAGTTCGAGGAGCGCCACATCCCGGGCGCCGCTTTCTTCGAC
ATCGACCAGTGCAGCGACCGCACCTCGCCCTACGACCACATGCTGCCCGGGGCCGAGCAT
TTCGCGGAGTACGCAGGCCGCCTGGGCGTGGGCGCGGCCACCCACGTCGTGATCTACGAC
GCCAGCGACCAGGGCCTCTACTCCGCCCCGCGCGTCTGGTGGATGTTCCGCGCCTTCGGC
CACCACGCCGTGTCACTGCTTGATGGCGGCCTCCGCCACTGGCTGCGCCAGAACCTCCCG
CTCAGCTCCGGCAAGAGCCAACCTGCTCCCGCCGAGTTCCGCGCTCAGCTCGACCCCGCC
TTCATCAAGACCTACGAGGACATCAAGGAGAACCTGGAATCCCGGCGCTTCCAGGTGGTG
GACTCCCGAGCCACTGGCAGGTTCCGCGGCACCGAGCCCGAGCCCCGAGACGGCATTGAA
CCTGGCCACATCCCAGGTACCGTGAACATCCCCTTCACAGACTTCCTGAGCCAGGAGGGG
CTGGAGAAGAGCCCTGAGGAGATCCGCCATCTGTTCCAGGAGAAGAAAGTGGACCTGTCT
AAGCCACTGGTGGCCACGTGTGGCTCTGGCGTCACAGCCTGCCACGTGGCACTAGGGGCC
TACCTCTGCGGCAAGCCAGACGTGCCCATCTACGATGGCTCCTGGGTGGAGTGGTACATG
CGCGCCCGGCCCGAGGATGTCATCTCAGAGGGCCGGGGGAAGACCCACTGA

1. Pallini R, Guazzi GC, Cannella C, Cacace MG: Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes. Biochem Biophys Res Commun. 1991 Oct 31;180(2):887-93. [PubMed ]
2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]

1. Alcohol dehydrogenase beta subunit

MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNP
RGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQ
NLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTVLTF

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGGTAAAGAAA
CCCTTTTCCATTGAGGATGTGGAGGTTGCACCTCCTAAGGCTTATGAAGTTCGCATTAAG
ATGGTGGCTGTAGGAATCTGTCGCACAGATGACCACGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAGTTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGGGGGAAGCCCATTCACCAC
TTCCTTGGCACCAGCACCTTCTCCCAGTACACGGTGGTGGATGAGAATGCAGTGGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTCTCGACTGGT
TATGGGTCTGCAGTTAACGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAAAAAGCAAAGGCCAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGCGTCATCGTAGGGGTACCTCCTGCTTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACCTGGAAGGGGGCTGTTTAT
GGTGGCTTTAAGAGTAAAGAAGGTATCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCACTGGATGCGTTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCGTCCTGACGTTTTGA

1. Heden LO, Hoog JO, Larsson K, Lake M, Lagerholm E, Holmgren A, Vallee BL, Jornvall H, von Bahr-Lindstrom H: cDNA clones coding for the beta-subunit of human liver alcohol dehydrogenase have differently sized 3'-non-coding regions. FEBS Lett. 1986 Jan 6;194(2):327-32. [PubMed ]
2. Duester G, Smith M, Bilanchone V, Hatfield GW: Molecular analysis of the human class I alcohol dehydrogenase gene family and nucleotide sequence of the gene encoding the beta subunit. J Biol Chem. 1986 Feb 15;261(5):2027-33. [PubMed ]
3. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed ]
4. Carr LG, Xu Y, Ho WH, Edenberg HJ: Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit. Alcohol Clin Exp Res. 1989 Aug;13(4):594-6. [PubMed ]
5. Matsuo Y, Yokoyama R, Yokoyama S: The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide. Eur J Biochem. 1989 Aug 1;183(2):317-20. [PubMed ]
6. Hempel J, Buhler R, Kaiser R, Holmquist B, de Zalenski C, von Wartburg JP, Vallee B, Jornvall H: Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme. Eur J Biochem. 1984 Dec 17;145(3):437-45. [PubMed ]
7. Xu YL, Carr LG, Bosron WF, Li TK, Edenberg HJ: Genotyping of human alcohol dehydrogenases at the ADH2 and ADH3 loci following DNA sequence amplification. Genomics. 1988 Apr;2(3):209-14. [PubMed ]
8. Jornvall H, Hempel J, Vallee BL, Bosron WF, Li TK: Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Proc Natl Acad Sci U S A. 1984 May;81(10):3024-8. [PubMed ]
9. Burnell JC, Carr LG, Dwulet FE, Edenberg HJ, Li TK, Bosron WF: The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding. Biochem Biophys Res Commun. 1987 Aug 14;146(3):1127-33. [PubMed ]
10. Hurley TD, Bosron WF, Hamilton JA, Amzel LM: Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. [PubMed ]
11. Hurley TD, Bosron WF, Stone CL, Amzel LM: Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J Mol Biol. 1994 Jun 10;239(3):415-29. [PubMed ]
12. Davis GJ, Bosron WF, Stone CL, Owusu-Dekyi K, Hurley TD: X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J Biol Chem. 1996 Jul 19;271(29):17057-61. [PubMed ]
13. Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD: Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 2001 Apr;10(4):697-706. [PubMed ]
14. Borras E, Coutelle C, Rosell A, Fernandez-Muixi F, Broch M, Crosas B, Hjelmqvist L, Lorenzo A, Gutierrez C, Santos M, Szczepanek M, Heilig M, Quattrocchi P, Farres J, Vidal F, Richart C, Mach T, Bogdal J, Jornvall H, Seitz HK, Couzigou P, Pares X: Genetic polymorphism of alcohol dehydrogenase in europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Hepatology. 2000 Apr;31(4):984-9. [PubMed ]

1. Alcohol dehydrogenase class IV mu/sigma chain
2. Retinol dehydrogenase
3. Gastric alcohol dehydrogenase

MGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVS
KFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGR
GVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGY
GAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATEC
ISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKM
LTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFE
LLNSGQSIRTVLTF

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGGGCACTGCTGGAAAAGTTATTAAGTGCAAAGCAGCTGTGCTTTGGGAGCAGAAGCAA
CCCTTCTCCATTGAGGAAATAGAAGTTGCCCCACCAAAGACTAAAGAAGTTCGCATTAAG
ATTTTGGCCACAGGAATCTGTCGCACAGATGACCATGTGATAAAAGGAACAATGGTGTCC
AAGTTTCCAGTGATTGTGGGACATGAGGCAACTGGGATTGTAGAGAGCATTGGAGAAGGA
GTGACTACAGTGAAACCAGGTGACAAAGTCATCCCTCTCTTTCTGCCACAATGTAGAGAA
TGCAATGCTTGTCGCAACCCAGATGGCAACCTTTGCATTAGGAGCGATATTACTGGTCGT
GGAGTACTGGCTGATGGCACCACCAGATTTACATGCAAGGGCAAACCAGTCCACCACTTC
ATGAACACCAGTACATTTACCGAGTACACAGTGGTGGATGAATCTTCTGTTGCTAAGATT
GATGATGCAGCTCCTCCTGAGAAAGTCTGTTTAATTGGCTGTGGGTTTTCCACTGGATAT
GGCGCTGCTGTTAAAACTGGCAAGGTCAAACCTGGTTCCACTTGCGTCGTCTTTGGCCTG
GGAGGAGTTGGCCTGTCAGTCATCATGGGCTGTAAGTCAGCTGGTGCATCTAGGATCATT
GGGATTGACCTCAACAAAGACAAATTTGAGAAGGCCATGGCTGTAGGTGCCACTGAGTGT
ATCAGTCCCAAGGACTCTACCAAACCCATCAGTGAGGTGCTGTCAGAAATGACAGGCAAC
AACGTGGGATACACCTTTGAAGTTATTGGGCATCTTGAAACCATGATTGATGCCCTGGCA
TCCTGCCACATGAACTATGGGACCAGCGTGGTTGTAGGAGTTCCTCCATCAGCCAAGATG
CTCACCTATGACCCGATGTTGCTCTTCACTGGACGCACATGGAAGGGATGTGTCTTTGGA
GGTTTGAAAAGCAGAGATGATGTCCCAAAACTAGTGACTGAGTTCCTGGCAAAGAAATTT
GACCTGGACCAGTTGATAACTCATGTTTTACCATTTAAAAAAATCAGTGAAGGATTTGAG
CTGCTCAATTCAGGACAAAGCATTCGAACGGTCCTGACGTTTTGA

1. Satre MA, Zgombic-Knight M, Duester G: The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene. J Biol Chem. 1994 Jun 3;269(22):15606-12. [PubMed ]
2. Zgombic-Knight M, Foglio MH, Duester G: Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro. J Biol Chem. 1995 Mar 3;270(9):4305-11. [PubMed ]
3. Farres J, Moreno A, Crosas B, Peralba JM, Allali-Hassani A, Hjelmqvist L, Jornvall H, Pares X: Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships. Eur J Biochem. 1994 Sep 1;224(2):549-57. [PubMed ]
4. Yokoyama S, Matsuo Y, Ramsbotham R, Yokoyama R: Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7). FEBS Lett. 1994 Sep 12;351(3):411-5. [PubMed ]
5. Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK: Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes. J Biol Chem. 1995 Feb 24;270(8):3625-30. [PubMed ]
6. Cheung B, Anderson JK, Holmes RS, Beacham IR: Human stomach class IV alcohol dehydrogenase: molecular genetic analysis. Alcohol Clin Exp Res. 1995 Feb;19(1):185-6. [PubMed ]
7. Pares X, Cederlund E, Moreno A, Saubi N, Hoog JO, Jornvall H: Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class. FEBS Lett. 1992 May 25;303(1):69-72. [PubMed ]
8. Xie P, Parsons SH, Speckhard DC, Bosron WF, Hurley TD: X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity. J Biol Chem. 1997 Jul 25;272(30):18558-63. [PubMed ]

1. Alcohol dehydrogenase alpha subunit

MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTGGAGGTTGCACCTCCTAAGGCCCATGAAGTTCGTATTAAG
ATGGTGGCTGTAGGAATCTGTGGCACAGATGACCACGTGGTTAGTGGTACCATGGTGACC
CCACTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAGAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCACTCGCTATTCCTCAGTGTGGAAAA
TGCAGAATTTGTAAAAACCCGGAGAGCAACTACTGCTTGAAAAACGATGTAAGCAATCCT
CAGGGGACCCTGCAGGATGGCACCAGCAGGTTCACCTGCAGGAGGAAGCCCATCCACCAC
TTCCTTGGCATCAGCACCTTCTCACAGTACACAGTGGTGGATGAAAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCTCTAGAGAAAGTCTGTCTCATTGGCTGTGGATTTTCAACTGGT
TATGGGTCTGCAGTCAATGTTGCCAAGGTCACCCCAGGCTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGCTATTATGGGCTGTAAAGCAGCTGGGGCAGCCAGAATC
ATTGCGGTGGACATCAACAAGGACAAATTTGCAAAGGCCAAAGAGTTGGGGGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATCCAGGAGGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCATTTGAAGTCATCGGTCGGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATCGTAGGGGTACCTCCTGATTCCCAA
AACCTCTCAATGAACCCTATGCTGCTACTGACTGGACGTACCTGGAAGGGAGCTATTCTT
GGTGGCTTTAAAAGTAAAGAATGTGTCCCAAAACTTGTGGCTGATTTTATGGCTAAGAAG
TTTTCATTGGATGCATTAATAACCCATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCACTCTGGGAAAAGTATCCGTACCATTCTGATGTTTTGA

1. von Bahr-Lindstrom H, Hoog JO, Heden LO, Kaiser R, Fleetwood L, Larsson K, Lake M, Holmquist B, Holmgren A, Hempel J, et al.: cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase. Biochemistry. 1986 May 6;25(9):2465-70. [PubMed ]
2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed ]
3. Matsuo Y, Yokoyama S: Molecular structure of the human alcohol dehydrogenase 1 gene. FEBS Lett. 1989 Jan 16;243(1):57-60. [PubMed ]
4. Yasunami M, Kikuchi I, Sarapata D, Yoshida A: The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome. Genomics. 1990 Jun;7(2):152-8. [PubMed ]

MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLD
LLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSK
TQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTG
FGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATE
CLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASV
QLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAV
ELMKTGKW

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGAGTACTACAGGCCAAGTCATCAGATGCAAAGCAGCCATACTCTGGAAGCCTGGTGCA
CCATTTTCTATTGAAGAGGTAGAAGTGGCCCCACCAAAGGCAAAGGAGGTTCGCATAAAG
GTTGTGGCCACCGGACTGTGTGGTACAGAGATGAAAGTGTTGGGGAGTAAACACTTGGAC
CTCTTGTATCCCACCATCTTGGGCCATGAAGGGGCTGGAATCGTTGAGAGTATTGGAGAA
GGAGTAAGCACAGTGAAACCAGGTGACAAAGTTATCACACTCTTTCTGCCACAGTGTGGA
GAATGTACCTCTTGCCTGAATTCTGAGGGCAATTTTTGTATACAATTCAAACAGTCAAAA
ACCCAACTGATGTCTGATGGTACCAGCAGGTTTACCTGCAAGGGAAAATCAATATATCAC
TTTGGTAATACCAGCACCTTCTGTGAATACACAGTGATAAAGGAAATCTCAGTTGCCAAG
ATTGATGCAGTCGCTCCTCTAGAGAAAGTATGCCTAATTAGCTGTGGCTTTTCCACTGGG
TTTGGTGCTGCAATCAATACTGCCAAGGTGACTCCAGGTTCTACCTGTGCTGTGTTTGGC
CTGGGAGGAGTCGGCTTGTCTGTTGTCATGGGTTGTAAAGCAGCAGGAGCAGCCAGGATC
ATTGGAGTGGATGTCAACAAGGAGAAATTTAAGAAGGCACAGGAATTGGGTGCGACTGAG
TGCCTCAACCCTCAGGACTTAAAGAAACCCATTCAAGAAGTTTTATTTGATATGACAGAT
GCTGGTATAGACTTCTGCTTTGAGGCCATTGGAAATCTGGACGTTCTGGCAGCTGCCCTC
GCCTCCTGCAATGAGAGCTATGGGGTCTGTGTGGTTGTTGGGGTGTTGCCTGCCAGTGTT
CAACTCAAAATCAGTGGCCAGTTGTTCTTCTCAGGACGTTCTTTGAAGGGTTCTGTTTTT
GGAGGCTGGAAGAGCAGACAGCACATCCCTAAACTGGTTGCTGATTATATGGCAGAGAAG
TTGAATCTAGATCCACTAATTACTCATACTCTGAATCTTGATAAAATCAATGAAGCAGTT
GAATTAATGAAAACTGGAAAATGGTAA

1. Yasunami M, Chen CS, Yoshida A: A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7610-4. [PubMed ]

1. Alcohol dehydrogenase gamma subunit

MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP
RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF
DLLRSGKSIRTVLTF

• 1- and 2-Methylnaphthalene degradation (map00624 )
• Bile Acid Biosynthesis (map00120 )
• Fatty Acid Metabolism (map00071 )
• Gluconeogenesis (map00010 )
• Glycerolipid Metabolism (map00561 )
• Tyrosine Metabolism (map00350 )

• an alcohol + NAD+ = an aldehyde or ketone + NADH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• None

• None

ATGAGCACAGCAGGAAAAGTAATCAAATGCAAAGCAGCTGTGCTATGGGAGTTAAAGAAA
CCCTTTTCCATTGAGGAGGTAGAGGTTGCACCTCCTAAGGCTCATGAAGTTCGCATTAAG
ATGGTGGCTGCAGGAATCTGTCGTTCAGATGAGCATGTGGTTAGTGGCAACCTGGTGACC
CCCCTTCCTGTGATTTTAGGCCATGAGGCAGCCGGCATCGTGGAAAGTGTTGGAGAAGGG
GTGACTACAGTCAAACCAGGTGATAAAGTCATCCCGCTCTTTACTCCTCAGTGTGGAAAA
TGCAGAATTTGCAAAAACCCAGAAAGCAACTACTGCTTGAAAAATGATCTAGGCAATCCT
CGGGGGACCCTGCAGGATGGCACCAGGAGGTTCACCTGCAGCGGGAAGCCCATCCACCAC
TTCGTCGGCGTCAGCACCTTCTCCCAGTACACAGTGGTGGATGAGAATGCAGTAGCCAAA
ATTGATGCAGCCTCGCCCCTGGAGAAAGTCTGCCTCATTGGCTGTGGATTTTCGACTGGT
TATGGGTCTGCAGTCAAAGTTGCCAAGGTCACCCCAGGGTCTACCTGTGCTGTGTTTGGC
CTGGGAGGGGTCGGCCTATCTGTTGTTATGGGCTGTAAAGCAGCTGGAGCAGCCAGAATC
ATTGCTGTGGACATCAACAAGGACAAATTTGCAAAGGCTAAAGAGTTGGGTGCCACTGAA
TGCATCAACCCTCAAGACTACAAGAAACCCATTCAGGAAGTGCTAAAGGAAATGACTGAT
GGAGGTGTGGATTTTTCGTTTGAAGTCATCGGTCAGCTTGACACCATGATGGCTTCCCTG
TTATGTTGTCATGAGGCATGTGGCACAAGTGTCATTGTAGGGGTACCTCCTGATTCCCAG
AACCTCTCAATAAACCCTATGCTGCTACTGACTGGACGCACGTGGAAAGGAGCTATTTTT
GGAGGCTTTAAGAGTAAAGAATCTGTCCCCAAACTTGTGGCTGACTTTATGGCTAAGAAG
TTTTCACTGGATGCATTAATAACAAATGTTTTACCTTTTGAAAAAATAAATGAAGGATTT
GACCTGCTTCGCTCTGGAAAGAGTATCCGTACCGTCCTGACGTTTTGA

1. Hoog JO, Heden LO, Larsson K, Jornvall H, von Bahr-Lindstrom H: The gamma 1 and gamma 2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties. Eur J Biochem. 1986 Sep 1;159(2):215-8. [PubMed ]
2. Ikuta T, Szeto S, Yoshida A: Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence. Proc Natl Acad Sci U S A. 1986 Feb;83(3):634-8. [PubMed ]
3. Yokoyama S, Matsuo Y, Rajasekharan S, Yokoyama R: Molecular structure of the human alcohol dehydrogenase 3 gene. Jpn J Genet. 1992 Apr;67(2):167-71. [PubMed ]
4. Buhler R, Hempel J, Kaiser R, de Zalenski C, von Wartburg JP, Jornvall H: Human liver alcohol dehydrogenase. 2. The primary structure of the gamma 1 protein chain. Eur J Biochem. 1984 Dec 17;145(3):447-53. [PubMed ]

1. Beta-G1

MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFE
EQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVV
LRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTT
LPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQD
SGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYL
YSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKG
FDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNN
VSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVT
FVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSE
YGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTR
VLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT

• Glycosaminoglycan degradation (map00531 )
• Porphyrin Metabolism (map00860 )
• Starch and Sucrose Metabolism (map00500 )

• a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol

• Glyco_hydro_2 (PF00703 )
• Glyco_hydro_2_C (PF02836 )
• Glyco_hydro_2_N (PF02837 )

• 1-22

ATGGCCCGGGGGTCGGCGGTTGCCTGGGCGGCGCTCGGGCCGTTGTTGTGGGGCTGCGCG
CTGGGGCTGCAGGGCGGGATGCTGTACCCCCAGGAGAGCCCGTCGCGGGAGTGCAAGGAG
CTGGACGGCCTCTGGAGCTTCCGCGCCGACTTCTCTGACAACCGACGCCGGGGCTTCGAG
GAGCAGTGGTACCGGCGGCCGCTGTGGGAGTCAGGCCCCACCGTGGACATGCCAGTTCCC
TCCAGCTTCAATGACATCAGCCAGGACTGGCGTCTGCGGCATTTTGTCGGCTGGGTGTGG
TACGAACGGGAGGTGATCCTGCCGGAGCGATGGACCCAGGACCTGCGCACAAGAGTGGTG
CTGAGGATTGGCAGTGCCCATTCCTATGCCATCGTGTGGGTGAATGGGGTCGACACGCTA
GAGCATGAGGGGGGCTACCTCCCCTTCGAGGCCGACATCAGCAACCTGGTCCAGGTGGGG
CCCCTGCCCTCCCGGCTCCGAATCACTATCGCCATCAACAACACACTCACCCCCACCACC
CTGCCACCAGGGACCATCCAATACCTGACTGACACCTCCAAGTATCCCAAGGGTTACTTT
GTCCAGAACACATATTTTGACTTTTTCAACTACGCTGGACTGCAGCGGTCTGTACTTCTG
TACACGACACCCACCACCTACATCGATGACATCACCGTCACCACCAGCGTGGAGCAAGAC
AGTGGGCTGGTGAATTACCAGATCTCTGTCAAGGGCAGTAACCTGTTCAAGTTGGAAGTG
CGTCTTTTGGATGCAGAAAACAAAGTCGTGGCGAATGGGACTGGGACCCAGGGCCAACTT
AAGGTGCCAGGTGTCAGCCTCTGGTGGCCGTACCTGATGCACGAACGCCCTGCCTATCTG
TATTCATTGGAGGTGCAGCTGACTGCACAGACGTCACTGGGGCCTGTGTCTGACTTCTAC
ACACTCCCTGTGGGGATCCGCACTGTGGCTGTCACCAAGAGCCAGTTCCTCATCAATGGG
AAACCTTTCTATTTCCACGGTGTCAACAAGCATGAGGATGCGGACATCCGAGGGAAGGGC
TTCGACTGGCCGCTGCTGGTGAAGGACTTCAACCTGCTTCGCTGGCTTGGTGCCAACGCT
TTCCGTACCAGCCACTACCCCTATGCAGAGGAAGTGATGCAGATGTGTGACCGCTATGGG
ATTGTGGTCATCGATGAGTGTCCCGGCGTGGGCCTGGCGCTGCCGCAGTTCTTCAACAAC
GTTTCTCTGCATCACCACATGCAGGTGATGGAAGAAGTGGTGCGTAGGGACAAGAACCAC
CCCGCGGTCGTGATGTGGTCTGTGGCCAACGAGCCTGCGTCCCACCTAGAATCTGCTGGC
TACTACTTGAAGATGGTGATCGCTCACACCAAATCCTTGGACCCCTCCCGGCCTGTGACC
TTTGTGAGCAACTCTAACTATGCAGCAGACAAGGGGGCTCCGTATGTGGATGTGATCTGT
TTGAACAGCTACTACTCTTGGTATCACGACTACGGGCACCTGGAGTTGATTCAGCTGCAG
CTGGCCACCCAGTTTGAGAACTGGTATAAGAAGTATCAGAAGCCCATTATTCAGAGCGAG
TATGGAGCAGAAACGATTGCAGGGTTTCACCAGGATCCACCTCTGATGTTCACTGAAGAG
TACCAGAAAAGTCTGCTAGAGCAGTACCATCTGGGTCTGGATCAAAAACGCAGAAAATAT
GTGGTTGGAGAGCTCATTTGGAATTTTGCCGATTTCATGACTGAACAGTCACCGACGAGA
GTGCTGGGGAATAAAAAGGGGATCTTCACTCGGCAGAGACAACCAAAAAGTGCAGCGTTC
CTTTTGCGAGAGAGATACTGGAAGATTGCCAATGAAACCAGGTATCCCCACTCAGTAGCC
AAGTCACAATGTTTGGAAAACAGCCCGTTTACTTGA

1. Oshima A, Kyle JW, Miller RD, Hoffmann JW, Powell PP, Grubb JH, Sly WS, Tropak M, Guise KS, Gravel RA: Cloning, sequencing, and expression of cDNA for human beta-glucuronidase. Proc Natl Acad Sci U S A. 1987 Feb;84(3):685-9. [PubMed ]
2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
3. Shipley JM, Miller RD, Wu BM, Grubb JH, Christensen SG, Kyle JW, Sly WS: Analysis of the 5' flanking region of the human beta-glucuronidase gene. Genomics. 1991 Aug;10(4):1009-18. [PubMed ]
4. Tanaka J, Gasa S, Sakurada K, Miyazaki T, Kasai M, Makita A: Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase. Biol Chem Hoppe Seyler. 1992 Jan;373(1):57-62. [PubMed ]
5. Guise KS, Korneluk RG, Waye J, Lamhonwah AM, Quan F, Palmer R, Ganschow RE, Sly WS, Gravel RA: Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase. Gene. 1985;34(1):105-10. [PubMed ]
6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed ]
7. Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH: Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat Struct Biol. 1996 Apr;3(4):375-81. [PubMed ]
8. Vervoort R, Lissens W, Liebaers I: Molecular analysis of a patient with hydrops fetalis caused by beta-glucuronidase deficiency, and evidence for additional pseudogenes. Hum Mutat. 1993;2(6):443-5. [PubMed ]
9. Wu BM, Sly WS: Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII. Hum Mutat. 1993;2(6):446-57. [PubMed ]
10. Tomatsu S, Fukuda S, Sukegawa K, Ikedo Y, Yamada S, Yamada Y, Sasaki T, Okamoto H, Kuwahara T, Yamaguchi S, et al.: Mucopolysaccharidosis type VII: characterization of mutations and molecular heterogeneity. Am J Hum Genet. 1991 Jan;48(1):89-96. [PubMed ]
11. Shipley JM, Klinkenberg M, Wu BM, Bachinsky DR, Grubb JH, Sly WS: Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes. Am J Hum Genet. 1993 Mar;52(3):517-26. [PubMed ]

1. Alpha-L-fucosidase 2
2. Alpha-L-fucoside fucohydrolase 2

MRPQELPRLAFPLLLLLLLLLPPPPCPAHSATRFDPTWESLDARQLPAWFDQAKFGIFIH
WGVFSVPSFGSEWFWWYWQKEKIPKYVEFMKDNYPPSFKYEDFGPLFTAKFFNANQWADI
FQASGAKYIVLTSKHHEGFTLWGSEYSWNWNAIDEGPKRDIVKELEVAIRNRTDLRFGLY
YSLFEWFHPLFLEDESSSFHKRQFPVSKTLPELYELVNNYQPEVLWSDGDGGAPDQYWNS
TGFLAWLYNESPVRGTVVTNDRWGAGSICKHGGFYTCSDRYNPGHLLPHKWENCMTIDKL
SWGYRREAGISDYLTIEELVKQLVETVSCGGNLLMNIGPTLDGTISVVFEERLRQVGSWL
KVNGEAIYETYTWRSQNDTVTPDVWYTSKPKEKLVYAIFLKWPTSGQLFLGHPKAILGAT
EVKLLGHGQPLNWISLEQNGIMVELPQLTIHQMPCKWGWALALTNVI

• N-Glycan degradation (map00511 )

• an alpha-L-fucoside + H2O = L-fucose + an alcohol

• Alpha_L_fucos (PF01120 )

• 1-28

ATGCGGCCCCAGGAGCTCCCCAGGCTCGCGTTCCCGTTGCTGCTGTTGCTGTTGCTGCTG
CTGCCGCCGCCGCCGTGCCCTGCCCACAGCGCCACGCGCTTCGACCCCACCTGGGAGTCC
CTGGACGCCCGCCAGCTGCCCGCGTGGTTTGACCAGGCCAAGTTCGGCATCTTCATCCAC
TGGGGAGTGTTTTCCGTGCCCAGCTTCGGTAGCGAGTGGTTCTGGTGGTATTGGCAAAAG
GAAAAGATACCGAAGTATGTGGAATTTATGAAAGATAATTACCCTCCTAGTTTCAAATAT
GAAGATTTTGGACCACTATTTACAGCAAAATTTTTTAATGCCAACCAGTGGGCAGATATT
TTTCAGGCCTCTGGTGCCAAATACATTGTCTTAACTTCCAAACATCATGAAGGCTTTACC
TTGTGGGGGTCAGAATATTCGTGGAACTGGAATGCCATAGATGAGGGGCCCAAGAGGGAC
ATTGTCAAGGAACTTGAGGTAGCCATTAGGAACAGAACTGACCTGCGTTTTGGACTGTAC
TATTCCCTTTTTGAATGGTTTCATCCGCTCTTCCTTGAGGATGAATCCAGTTCATTCCAT
AAGCGGCAATTTCCAGTTTCTAAGACATTGCCAGAGCTCTATGAGTTAGTGAACAACTAT
CAGCCTGAGGTTCTGTGGTCGGATGGTGACGGAGGAGCACCGGATCAATACTGGAACAGC
ACAGGCTTCTTGGCCTGGTTATATAATGAAAGCCCAGTTCGGGGCACAGTAGTCACCAAT
GATCGTTGGGGAGCTGGTAGCATCTGTAAGCATGGTGGCTTCTATACCTGCAGTGATCGT
TATAACCCAGGACATCTTTTGCCACATAAATGGGAAAACTGCATGACAATAGACAAACTG
TCCTGGGGCTATAGGAGGGAAGCTGGAATCTCTGACTATCTTACAATTGAAGAATTGGTG
AAGCAACTTGTAGAGACAGTTTCATGTGGAGGAAATCTTTTGATGAATATTGGGCCCACA
CTAGATGGCACCATTTCTGTAGTTTTTGAGGAGCGACTGAGGCAAGTGGGGTCCTGGCTA
AAAGTCAATGGAGAAGCTATTTATGAAACCTATACCTGGCGATCCCAGAACGACACTGTC
ACCCCAGATGTGTGGTACACATCCAAGCCTAAAGAAAAATTAGTCTATGCCATTTTTCCT
AAATGGCCCACATCAGGACAGCTGTTCCTTGGCCATCCCAAAGCTATTCTGGGGGCAACA
GAGGTGAAACTACTGGGCCATGGACAGCCACTTAACTGGATTTCTTTGGAGCAAAATGGC
ATTATGGTAGAACTGCCACAGCTAACCATTCATCAGATGCCGTGTAAATGGGGCTGGGCT
CTAGCCCTAACTAATGTGATCTAA

1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]

1. HsNrbf-1
2. NRBF-1

MWVCSTLWRVRTPARQWRGLLPASGCHGPAASSYSASAEPARVRALVYGHHGDPAKVVEL
KNLELAAVRGSDVRVKMLAAPINPSDINMIQGNYGLLPELPAVGGNEGVAQVVAVGSNVT
GLKPGDWVIPANAGLGTWRTEAVFSEEALIQVPSDIPLQSAATLGVNPCTAYRMLMDFEQ
LQPGDSVIQNASNSGVGQAVIQIAAALGLRTINVVRDRPDIQKLSDRLKSLGAEHVITEE
ELRRPEMKNFFKDMPQPRLALNCVGGKSSTELLRQLARGGTMVTYGGMAKQPVVASVSLL
IFKDLKLRGFWLSQWKKDHSPDQFKELILTLCDLIRRGQLTAPACSQVPLQDYQSALEAS
MKPFISSKQILTM

• acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

• 1-19

ATGTGGGTCTGCAGTACCCTGTGGCGGGTGCGAACCCCGCCCGGCAGTGGCGGGGGCCTG
CTCCCAGCTTCTGGCTGTCACGGACCTGCCGCCTCCTCCTACTCCGCATCCGCCGAGCCT
GCCCGGGTCCGCGGCGTTGTCTATGGGCACCACGGGGATCCAGCCAAGGTCGTCGAACTC
AAGAACCTGGAGCTAGCTGCTGTGAGAGGATCAGATGTCCGTGTGAAGATGCTGGCGGCC
CCTATCAATCCATCTGACATAAATATGATCCAAGGAAACTACGGACTCCTTCCTGAACTG
CCTGCTGTTGGAGGGAACGAAGGTGTTGCACAGGTGGTAGCGGTGGGCAGCAATGTGACC
GGGCTGAAGCCAGGAGACTGGGTGATTCCAGCAAATGCTGGTTTAGGAACCTGGCGGACC
GAGGCTGTGTTCAGCGAGGAAGCACTGATCCAAGTTCCGAGTGACATCCCTCTTCAGAGC
GCTGCCACCCTGGGTGTCAATCCCTGCACAGCCTACAGGATGTTGATGGACTTCGAGCAA
CTGCAGCCAGGGGATTCTGTCATCCAGAATGCATCCAACAGCGGAGTGGGGCAAGCGGTC
ATCCAGATCGCCGCAGCCCTGGGCCTAAGAACCATCAATGTGGTCCGAGACAGACCTGAT
ATCCAGAAGCTGAGTGACAGACTGAAGAGTCTGGGGGCTGAGCATGTCATCACAGAAGAG
GAGCTAAGAAGGCCCGAAATGAAAAACTTCTTTAAGGACATGCCCCAGCCACGGCTTGCT
CTCAACTGTGTTGGTGGGAAAAGCTCCACAGAGCTGCTGCGCCAGTTAGCGCGTGGAGGA
ACCATGGTAACCTATGGGGGGATGGCCAAGCAGCCCGTCGTAGCCTCTGTGAGCCTGCTC
ATTTTTAAGGATCTCAAACTTCGAGGCTTTTGGTTGTCCCAGTGGAAGAAGGATCACAGT
CCAGACCAGTTCAAGGAGCTGATCCTCACACTGTGCGATCTCATCCGCCGAGGCCAGCTC
ACAGCCCCTGCCTGCTCCCAGGTCCCGCTGCAGGACTACCAGTCTGCCTTGGAAGCCTCC
ATGAAGCCCTTCATATCTTCAAAGCAGATTCTCACCATGTGA

1. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed ]
2. Miinalainen IJ, Chen ZJ, Torkko JM, Pirila PL, Sormunen RT, Bergmann U, Qin YM, Hiltunen JK: Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J Biol Chem. 2003 May 30;278(22):20154-61. Epub 2003 Mar 24. [PubMed ]

1. CYPIIE1
2. P450-J

MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS

• Fatty Acid Metabolism (map00071 )
• gamma-Hexachlorocyclohexane Degradation (map00361 )
• Tryptophan Metabolism (map00380 )

• RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O

• p450 (PF00067 )

• 1-28

ATGTCTGCCCTCGGAGTGACCGTGGCCCTGCTGGTGTGGGCGGCCTTCCTCCTGCTGGTG
TCCATGTGGAGGCAGGTGCACAGCAGCTGGAATCTGCCCCCAGGTCCTTTCCCGCTTCCC
ATCATCGGGAACCTCTTCCAGTTGGAATTGAAGAATATTCCCAAGTCCTTCACCCGGTTG
GCCCAGCGCTTCGGGCCGGTGTTCACGCTGTACGTGGGCTCGCAGCGCATGGTGGTGATG
CACGGCTACAAGGCGGTGAAGGAAGCGCTGCTGGACTACAAGGACGAGTTCTCGGGCAGA
GGCGACCTCCCCGCGTTCCATGCGCACAGGGACAGGGGAATCATTTTTAATAATGGACCT
ACCTGGAAGGACATCCGGCGGTTTTCCCTGACCACCCTCCGGAACTATGGGATGGGGAAA
CAGGGCAATGAGAGCCGGATCCAGAGGGAGGCCCACTTCCTGCTGGAAGCACTCAGGAAG
ACCCAAGGCCAGCCTTTCGACCCCACCTTCCTCATCGGCTGCGCGCCCTGCAACGTCATA
GCCGACATCCTCTTCCGCAAGCATTTTGACTACAATGATGAGAAGTTTCTAAGGCTGATG
TATTTGTTTAATGAGAACTTCCACCTACTCAGCACTCCCTGGCTCCAGCTTTACAATAAT
TTTCCCAGCTTTCTACACTACTTGCCTGGAAGCCACAGAAAAGTCATAAAAAATGTGGCT
GAAGTAAAAGAGTATGTGTCTGAAAGGGTGAAGGAGCACCATCAATCTCTGGACCCCAAC
TGTCCCCGGGACCTCACCGACTGCCTGCTCGTGGAAATGGAGAAGGAAAAGCACAGTGCA
GAGCGCTTGTACACAATGGACGGTATCACCGTGACTGTGGCCGACCTGTTCTTTGCGGGG
ACAGAGACCACCAGCACAACTCTGAGATATGGGCTCCTGATTCTCATGAAATACCCTGAG
ATCGAAGAGAAGCTCCATGAAGAAATTGACAGGGTGATTGGGCCAAGCCGAATCCCTGCC
ATCAAGGATAGGCAAGAGATGCCCTACATGGATGCTGTGGTGCATGAGATTCAGCGGTTC
ATCACCCTCGTGCCCTCCAACCTGCCCCATGAAGCAACCCGAGACACCATTTTCAGAGGA
TACCTCATCCCCAAGGGCACAGTCGTAGTGCCAACTCTGGACTCTGTTTTGTATGACAAC
CAAGAATTTCCTGATCCAGAAAAGTTTAAGCCAGAACACTTCCTGAATGAAAATGGAAAG
TTCAAGTACAGTGACTATTTCAAGCCATTTTCCACAGGAAAACGAGTGTGTGCTGGAGAA
GGCCTGGCTCGCATGGAGTTGTTTCTTTTGTTGTGTGCCATTTTGCAGCATTTTAATTTG
AAGCCTCTCGTTGACCCAAAGGATATCGACCTCAGCCCTATACATATTGGGTTTGGCTGT
ATCCCACCACGTTACAAACTCTGTGTCATTCCCCGCTCATGA

1. Song BJ, Gelboin HV, Park SS, Yang CS, Gonzalez FJ: Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme. J Biol Chem. 1986 Dec 15;261(35):16689-97. [PubMed ]
2. Umeno M, McBride OW, Yang CS, Gelboin HV, Gonzalez FJ: Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry. 1988 Dec 13;27(25):9006-13. [PubMed ]
3. Lasker JM, Raucy J, Kubota S, Bloswick BP, Black M, Lieber CS: Purification and characterization of human liver cytochrome P-450-ALC. Biochem Biophys Res Commun. 1987 Oct 14;148(1):232-8. [PubMed ]
4. Robinson RC, Shorr RG, Varrichio A, Park SS, Gelboin HV, Miller H, Friedman FK: Human liver cytochrome P-450 related to a rat acetone-inducible, nitrosamine-metabolizing cytochrome P-450: identification and isolation. Pharmacology. 1989;39(3):137-44. [PubMed ]
5. Gillam EM, Guo Z, Guengerich FP: Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties. Arch Biochem Biophys. 1994 Jul;312(1):59-66. [PubMed ]
6. Hu Y, Oscarson M, Johansson I, Yue QY, Dahl ML, Tabone M, Arinco S, Albano E, Ingelman-Sundberg M: Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol. 1997 Mar;51(3):370-6. [PubMed ]
7. Fairbrother KS, Grove J, de Waziers I, Steimel DT, Day CP, Crespi CL, Daly AK: Detection and characterization of novel polymorphisms in the CYP2E1 gene. Pharmacogenetics. 1998 Dec;8(6):543-52. [PubMed ]

1. Phosphatidylcholine-- retinol O-acyltransferase

MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG

• phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]

• NC (PF04970 )

• 1-31

• 206-226

ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCAAGGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGCACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA

1. Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D: Molecular and biochemical characterization of lecithin retinol acyltransferase. J Biol Chem. 1999 Feb 5;274(6):3834-41. [PubMed ]
2. Mondal MS, Ruiz A, Bok D, Rando RR: Lecithin retinol acyltransferase contains cysteine residues essential for catalysis. Biochemistry. 2000 May 2;39(17):5215-20. [PubMed ]
3. Thompson DA, Li Y, McHenry CL, Carlson TJ, Ding X, Sieving PA, Apfelstedt-Sylla E, Gal A: Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy. Nat Genet. 2001 Jun;28(2):123-4. [PubMed ]

1. Constitutive androstane receptor
2. CAR
3. Constitutive activator of retinoid response
4. Constitutive active response
5. Orphan nuclear receptor MB67

MASREDELRNCVVCGDQATGYHFNALTCEGCKGFFRRTVSKSIGPTCPFAGSCEVSKTQR
RHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGA
HTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLP
VFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVSPTVGFQV
EFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYI
KGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS

• Hormone_recep (PF00104 )
• zf-C4 (PF00105 )

• None

• None

ATGGCCAGTAGGGAAGATGAGCTGAGGAACTGTGTGGTATGTGGGGACCAAGCCACAGGC
TACCACTTTAATGCGCTGACTTGTGAGGGCTGCAAGGGTTTCTTCAGGAGAACAGTCAGC
AAAAGCATTGGTCCCACCTGCCCCTTTGCTGGAAGCTGTGAAGTCAGCAAGACTCAGAGG
CGCCACTGCCCAGCCTGCAGGTTGCAGAAGTGCTTAGATGCTGGCATGAGGAAAGACATG
ATACTGTCGGCAGAAGCCCTGGCATTGCGGCGAGCAAAGCAGGCCCAGCGGCGGGCACAG
CAAACACCTGTGCAACTGAGTAAGGAGCAAGAAGAGCTGATCCGGACACTCCTGGGGGCC
CACACCCGCCACATGGGCACCATGTTTGAACAGTTTGTGCAGTTTAGGCCTCCAGCTCAT
CTGTTCATCCATCACCAGCCCTTGCCCACCCTGGCCCCTGTGCTGCCTCTGGTCACACAC
TTCGCAGACATCAACACTTTCATGGTACTGCAAGTCATCAAGTTTACTAAGGACCTGCCC
GTCTTCCGTTCCCTGCCCATTGAAGACCAGATCTCCCTTCTCAAGGGAGCAGCTGTGGAA
ATCTGTCACATCGTACTCAATACCACTTTCTGTCTCCAAACACAAAACTTCCTCTGCGGG
CCTCTTCGCTACACAATTGAAGATGGAGCCCGTGTGGGGTTCCAGGTAGAGTTTTTGGAG
TTGCTCTTTCACTTCCATGGAACACTACGAAAACTGCAGCTCCAAGAGCCTGAGTATGTG
CTCTTGGCTGCCATGGCCCTCTTCTCTCCTGACCGACCTGGAGTTACCCAGAGAGATGAG
ATTGATCAGCTGCAAGAGGAGATGGCACTGACTCTGCAAAGCTACATCAAGGGCCAGCAG
CGAAGGCCCCGGGATCGGTTTCTGTATGCGAAGTTGCTAGGCCTGCTGGCTGAGCTCCGG
AGCATTAATGAGGCCTACGGGTACCAAATCCAGCACATCCAGGGCCTGTCTGCCATGATG
CCGCTGCTCCAGGAGATCTGCAGCTGA

1. Baes M, Gulick T, Choi HS, Martinoli MG, Simha D, Moore DD: A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol. 1994 Mar;14(3):1544-52. [PubMed ]
2. Choi HS, Seol W, Moore DD: A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily. J Steroid Biochem Mol Biol. 1996 Jan;56(1-6 Spec No):23-30. [PubMed ]

MLRLVPTGARAIVDMSYARHFLDFQGSAIPQAMQKLVVTRLSPNFREAVTLSRDCPVPLP
GDGDLLVRNRFVGVNASDINYSAGRYDPSVKPPFDIGFEGIGEVVALGLSASARYTVGQA
VAYMAPGSFAEYTVVPASIATPVPSVKPEYLTLLVSGTTAYISLKELGGLSEGKKVLVTA
AAGGTGQFAMQLSKKAKCHVIGTCSSDEKSAFLKSLGCDRPINYKTEPVGTVLKQEYPEG
VDVVYESVGGAMFDLAVDALATKGRLIVIGFISGYQTPTGLSPVKAGTLPAKLLKKSASV
QGFFLNHYLSKYQAAMSHLLEMCVSGDLVCEVDLGDLSPEGRFTGLESIFRAVNYMYMGK
NTGKIVVELPHSVNSKL

• ADH_N (PF08240 )
• ADH_zinc_N (PF00107 )

ATGCTGCGGCTGGTGCCCACCGGGGCCCGGGCCATCGTGGACATGTCGTACGCCCGCCAC
TTCCTGGACTTCCAGGGCTCCGCCATTCCCCAAGCCATGCAGAAGCTGGTGGTGACCCGG
CTGAGCCCCAACTTCCGCGAGGCCGTCACCCTGAGCCGGGACTGCCCGGTGCCGCTCCCC
GGGGACGGAGACCTCCTCGTCCGGAACCGATTTGTTGGTGTTAACGCATCTGACATCAAC
TATTCAGCAGGCCGCTATGACCCCTCAGTTAAGCCTCCCTTTGACATAGGTTTCGAAGGC
ATTGGGGAGGTGGTGGCCCTAGGCCTCTCTGCTAGTGCCAGATACACAGTTGGCCAAGCT
GTGGCTTACATGGCACCTGGTTCTTTTGCTGAGTACACAGTTGTGCCTGCCAGCATTGCA
ACTCCAGTGCCCTCAGTGAAACCCGAGTATCTTACCCTGCTGGTAAGTGGCACCACCGCA
TACATCAGCCTGAAAGAGCTCGGAGGACTGTCGGAAGGGAAAAAAGTTTTGGTGACAGCA
GCAGCTGGGGGAACGGGCCAGTTTGCCATGCAGCTTTCAAAGAAGGCAAAGTGCCATGTA
ATTGGAACCTGCTCTTCTGATGAAAAGTCTGCTTTTCTGAAATCTCTTGGCTGTGATCGT
CCTATCAACTATAAAACTGAACCCGTAGGTACCGTCCTTAAGCAGGAGTACCCTGAAGGT
GTCGATGTGGTCTATGAATCTGTTGGGGGAGCCATGTTTGACTTGGCTGTAGACGCCCTG
GCTACGAAAGGGCGCTTGATAGTAATAGGGTTTATCTCTGGCTACCAAACTCCTACTGGC
CTTTCGCCTGTGAAAGCAGGAACATTGCCAGCCAAACTGCTCAAGAAATCTGCCAGCGTA
CAGGGCTTCTTCCTGAACCATTACCTTTCTAAGTATCAAGCAGCCATGAGCCACTTGCTC
GAGATGTGTGTGAGCGGAGACCTGGTTTGTGAGGTGGACCTTGGAGATCTGTCTCCAGAG
GGCAGGTTTACTGGCCTGGAGTCCATATTCCGTGCTGTCAATTATATGTACATGGGAAAA
AACACTGGAAAAATTGTAGTTGAATTACCTCACTCTGTCAACAGTAAGCTGTAA

MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAV
TKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFM
EAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKP
LIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSG
FDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRN
PDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLS
VVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGL
AAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY

• 3,4-Dihydroxymandelaldehyde + H+ + Nicotinamide adenine dinucleotide - reduced <==> 3,4-Dihydroxyphenylethyleneglycol + Nicotinamide adenine dinucleotide

• Fe-ADH (PF00465 )

• None

• None

1. Deng Y, Wang Z, Gu S, Ji C, Ying K, Xie Y, Mao Y: Cloning and characterization of a novel human alcohol dehydrogenase gene (ADHFe1). DNA Seq. 2002 Oct;13(5):301-6. [PubMed ]

1. Male sterility domain- containing protein 1

MSTIAAFYGGKSILITGATGFLGKVLMEKLFRTSPDLKVIYILVRPKAGQTLQQRVFQIL
DSKLFEKVKEVCPNVHEKIRAIYADLNQNDFAISKEDMQELLSCTNIIFHCAATVRFDDT
LRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKIIDS
LEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPF
PGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKST
LVYHITSGNMNPCNWHKMGVQVLATFEKIPFERPFRRPNANFTSNSFTSQYWNAVSHRAP
AIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRV
FNFDVRQLNWLEYIENYVLGVKKYLLKEDMAGIPKAKQRLKRLRNIHYLFNTALFLIAWR
LLIARSQMARNVWFFIVSFCYKFLSYFRASSTLKV

• NAD_binding_4 (PF07993 )
• Sterile (PF03015 )

• None

• 465-484 491-510

1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed ]

1. Long-chain- alcohol O-fatty-acyltransferase 2
2. Wax synthase
3. hWS
4. Multifunctional O-acyltransferase
5. Diacylglycerol O-acyltransferase 2-like protein 4
6. Diacylglycerol O-acyltransferase candidate 4
7. hDC4

MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII

• acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999] ALL_REAC R01999

• DAGAT (PF03982 )

• None

• 15-35 38-58 130-150

1. ADH1alpha subunit mRNA
2. Alcohol dehydrogenase 1A
3. Class I, alpha polypeptide, isoform CRA_b

MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVT
PLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNP
QGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTG
YGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATE
CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQ
NLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGF
DLLHSGKSIRTILMF

• None

• None

MPASAPPRRPRPPPPSLSLLLVLLGLGGRRLRAEPGDGAQTWARFSRPPAPEAAGLFQGT
FPDGFLWAVGSAAYQTEGGWQQHGKGASIWDTFTHHPLAPPGDSRNASLPLGAPSPLQPA
TGDVASDSYNNVFRDTEALRELGVTHYRFSISWARVLPNGSAGVPNREGLRYYRRLLERL
RELGVQPVVTLYHWDLPQRLQDAYGGWANRALADHFRDYAELCFRHFGGQVKYWITIDNP
YVVAWHGYATGRLAPGIRGSPRLGYLVAHNLLLAHAKVWHLYNTSFRPTQGGQVSIALSS
HWINPRRMTDHSIKECQKSLDFVLGWFAKPVFIDGDYPESMKNNLSSILPDFTESEKKFI
KGTADFFALCFGPTLSFQLLDPHMKFRQLESPNLRQLLSWIDLEFNHPQIFIVENGWFVS
GTTKRDDAKYMYYLKKFIMETLKAIKLDGVDVIGYTAWSLMDGFEWHRGYSIRRGLFYVD
FLSQDKMLLPKSSALFYQKLIEKNGFPPLPENQPLEGTFPCDFAWGVVDNYIQVDTTLSQ
FTDLNVYLWDVHHSKRLIKVDGVVTKKRKSYCVDFAAIQPQIALLQEMHVTHFRFSLDWA
LILPLGNQSQVNHTILQYYRCMASELVRVNITPVVALWQPMAPNQGLPRLLARQGAWENP
YTALAFAEYARLCFQELGHHVKLWITMNEPYTRNMTYSAGHNLLKAHALAWHVYNEKFRH
AQNGKISIALQADWIEPACPFSQKDKEVAERVLEFDIGWLAEPIFGSGDYPWVMRDWLNQ
RNNFLLPYFTEDEKKLIQGTFDFLALSHYTTILVDSEKEDPIKYNDYLEVQEMTDITWLN
SPSQVAVVPWGLRKVLNWLKFKYGDLPMYIISNGIDDGLHAEDDQLRVYYMQNYINEALK
AHILDGINLCGYFAYSFNDRTAPRFGLYRYAADQFEPKASMKHYRKIIDSNGFPGPETLE
RFCPEEFTVCTECSFFHTRKSLLAFIAFLFFASIISLSLIFYYSKKGRRSYK

• Glycan structures - degradation (map01032 )
• Glycosaminoglycan degradation (map00531 )
• Porphyrin Metabolism (map00860 )
• Starch and Sucrose Metabolism (map00500 )

• a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol [RN:R01478] ALL_REAC R01478
• (other) R04979 R07818(G)

• Glyco_hydro_1 (PF00232 )

• 1-33

• 982-1002

ATGCCCGCCAGCGCCCCGCCGCGCCGCCCGCGGCCGCCGCCGCCGTCGCTGTCGCTGCTG
CTGGTGCTGCTGGGCCTGGGCGGCCGCCGCCTGCGTGCGGAGCCGGGCGACGGCGCGCAG
ACCTGGGCCCGTGTCTCGCGGCCTCCTGCCCCCGAGGCCGCGGGCCTCTTCCAGGGCACC
TTCCCCGACGGCTTCCTCTGGGCCGTGGGCAGCGCCGCCTACCAGACCGAGGGCGGCTGG
CAGCAGCACGGCAAGGGTGCGTCCATCTGGGACACGTTCACCCACCACCCCCTGGCACCC
CCGGGAGACTCCCGGAACGCCAGTCTGCCGTTGGGCGCCCCGTCGCCGCTGCAGCCCGCC
ACCGGGGACGTAGCCAGCGACAGCTACAACAACGTCTTCCGCGACACGGAGGCGCTGCGC
GAGCTCGGGGTCACTCACTACCGCTTCTCCATCTCGTGGGCGCGAGTGCTCCCCAATGGC
AGCGCGGGCGTCCCCAACCGCGAGGGGCTGCGCTACTACCGGCGCCTGCTGGAGCGGCTG
CGGGAGCTGGGCGTGCAGCCCGTGGTCACCCTGTACCACTGGGACCTGCCCCAGCGCCTG
CAGGACGCCTACGGCGGCTGGGCCAACCGCGCCCTGGCCGACCACTTCAGGGATTACGCG
GAGCTCTGCTTCCGCCACTTCGGCGGTCAGGTCAAGTACTGGATCACCATCGACAACCCC
TACGTGGTGGCCTGGCACGGCTACGCCACCGGGCGCCTGGCCCCCGGCATCCGGGGCAGC
CCGCGGCTCGGGTACCTGGTGGCGCACAACCTCCTCCTGGCTCATGCCAAAGTCTGGCAT
CTCTACAATACTTCTTTCCGTCCCACTCAGGGAGGTCAGGTGTCCATTGCCCTAAGCTCT
CACTGGATCAATCCTCGAAGAATGACCGACCACAGCATCAAAGAATGTCAAAAATCTCTG
GACTTTGTACTAGGTTGGTTTGCCAAACCCGTATTTATTGATGGTGACTATCCCGAGAGC
ATGAAGAATAACCTTTCATCTATTCTGCCTGATTTTACTGAATCTGAGAAAAAGTTCATC
AAAGGAACTGCTGACTTTTTTGCTCTTTGCTTTGGACCCACCTTGAGTTTTCAACTTTTG
GACCCTCACATGAAGTTCCGCCAATTGGAATCTCCCAACCTGAGGCAACTGCTTTCCTGG
ATTGACCTTGAATTTAACCATCCTCAAATATTTATTGTGGAAAATGGCTGGTTTGTCTCA
GGGACCACCAAGAGAGATGATGCCAAATATATGTATTACCTCAAAAAGTTCATCATGGAA
ACCTTAAAAGCCATCAAGCTGGATGGGGTGGATGTCATCGGGTATACCGCATGGTCCCTC
ATGGATGGTTTCGAGTGGCACAGAGGTTACAGCATCAGGCGTGGACTCTTCTATGTTGAC
TTTCTAAGCCAGGACAAGATGTTGTTGCCAAAGTCTTCAGCCTTGTTCTACCAAAAGCTG
ATAGAGAAAAATGGCTTCCCTCCTTTACCTGAAAATCAGCCCCTAGAAGGGACATTTCCC
TGTGACTTTGCTTGGGGAGTTGTTGACAACTACATTCAAGTAGATACCACTCTGTCTCAG
TTTACCGACCTGAATGTTTACCTGTGGGATGTCCACCACAGTAAAAGGCTTATTAAAGTG
GATGGGGTTGTGACCAAGAAGAGGAAATCCTACTGTGTTGACTTTGCTGCCATCCAGCCC
CAGATCGCTTTACTCCAGGAAATGCACGTTACACATTTTCGCTTCTCCCTGGACTGGGCC
CTGATTCTCCCTCTGGGTAACCAGTCCCAGGTGAACCACACCATCCTGCAGTACTATCGC
TGCATGGCCAGCGAGCTTGTCCGTGTCAACATCACCCCAGTGGTGGCCCTGTGGCAGCCT
ATGGCCCCGAACCAAGGACTGCCGCGCCTCCTGGCCAGGCAGGGCGCCTGGGAGAACCCC
TACACTGCCCTGGCCTTTGCAGAGTATGCCCGACTGTGCTTTCAAGAGCTCGGCCATCAC
GTCAAGCTTTGGATAACGATGAATGAGCCGTATACAAGGAATATGACATACAGTGCTGGC
CACAACCTTCTGAAGGCCCATGCCCTGGCTTGGCATGTGTACAATGAAAAGTTTAGGCAT
GCTCAGAATGGGAAAATATCCATAGCCTTGCAGGCTGATTGGATAGAACCTGCCTGCCCT
TTCTCCCAAAAGGACAAAGAGGTGGCCGAGAGAGTTTTGGAATTTGACATTGGCTGGCTG
GCTGAGCCCATTTTCGGCTCTGGAGATTATCCATGGGTGATGAGGGACTGGCTGAACCAA
AGAAACAATTTTCTTCTTCCTTATTTCACTGAAGATGAAAAAAAGCTAATCCAGGGTACC
TTTGACTTTTTGGCTTTAAGCCATTATACCACCATCCTTGTAGACTCAGAAAAAGAAGAT
CCAATAAAATACAATGATTACCTAGAAGTGCAAGAAATGACCGACATCACGTGGCTCAAC
TCCCCCAGTCAGGTGGCGGTAGTGCCCTGGGGGTTGCGCAAAGTGCTGAACTGGCTGAAG
TTCAAGTACGGAGACCTCCCCATGTACATAATATCCAACGGAATCGATGACGGGCTGCAT
GCTGAGGACGACCAGCTGAGGGTGTATTATATGCAGAATTACATAAACGAAGCTCTCAAA
GCCCACATACTGGATGGTATCAATCTTTGCGGATACTTTGCTTATTCGTTTAACGACCGC
ACAGCTCCGAGGTTTGGCCTCTATCGTTATGCTGCAGATCAGTTTGAGCCCAAGGCATCC
ATGAAACATTACAGGAAAATTATTGACAGCAATGGTTTCCCGGGCCCAGAAACTCTGGAA
AGATTTTGTCCAGAAGAATTCACCGTGTGTACTGAGTGCAGTTTTTTTCACACCCGAAAG
TCTTTACTGGCTTTCATAGCTTTTCTATTTTTTGCTTCTATTATTTCTCTCTCCCTTATA
TTTTACTACTCGAAGAAAGGCAGAAGAAGTTACAAATAG

1. Kuro-o M, Matsumura Y, Aizawa H, Kawaguchi H, Suga T, Utsugi T, Ohyama Y, Kurabayashi M, Kaname T, Kume E, Iwasaki H, Iida A, Shiraki-Iida T, Nishikawa S, Nagai R, Nabeshima YI: Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature. 1997 Nov 6;390(6655):45-51. [PubMed ]
2. Matsumura Y, Aizawa H, Shiraki-Iida T, Nagai R, Kuro-o M, Nabeshima Y: Identification of the human klotho gene and its two transcripts encoding membrane and secreted klotho protein. Biochem Biophys Res Commun. 1998 Jan 26;242(3):626-30. [PubMed ]
3. Yahata K, Mori K, Arai H, Koide S, Ogawa Y, Mukoyama M, Sugawara A, Ozaki S, Tanaka I, Nabeshima Y, Nakao K: Molecular cloning and expression of a novel klotho-related protein. J Mol Med. 2000;78(7):389-94. [PubMed ]

1. N-methyl-D-aspartate receptor subtype NR3A
2. NMDAR-L

MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTT
APRAASRAPDDSRAGAQRDEPEPGTRRSPAPSPGARWLGSTLHGRGPPGSRKPGEGARAE
ALWPRDALLFAVDNLNRVEGLLPYNLSLEVVMAIEAGLGDLPLLPFSSPSSPWSSDPFSF
LQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSLVLHIPVISIVRHEFPRESQNPLHLQL
SLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTQNNSKFHLGSIINITAN
LPSTQDLLSFLQIQLESIKNSTPTVVMFGCDMESIRRIFEITTQFGVMPPELRWVLGDSQ
NMEELRTEGLPLGLIAHGKTTQSVFEHYVQDAMELVARAVATATMIQPELALIPSTMNCM
EVETTNLTSGQYLSRFLANTTFRGLSGSIRVKGSTIVSSENNFFIWNLQHDPMGKPMWTR
LGSWQGRKIVMDYGIWPEQAQRHKTHFQHPSKLHLRVVTLIEHPFVFTREVDDEGLCPAG
QLCLDPMTNDSSTLDSLFSSLHSSNDTVPIKFKKCCYGYCIDLLEKIAEDMNFDFDLYIV
GDGKYGAWKNGHWTGLVGDLLRGTAHMAVTSFSINTARSQVIDFTSPFFSTSLGILVRTR
DTAAPIGAFMWPLHWTMWLGIFVALHITAVFLTLYEWKSPFGLTPKGRNRSKVFSFSSAL
NICYALLFGRTVAIKPPKCWTGRFLMNLWAIFCMFCLSTYTANLAAVMVGEKIYEELSGI
HDPKLHHPSQGFRFGTVRESSAEDYVRQSFPEMHEYMRRYNVPATPDGVEYLKNNPEKLD
AFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPPNSPLTANISELISQYKSHGFM
DMLHDKWYRVVPCGKRSFAVTETLQMGIKHFSGLFVLLCIGFGLSILTTIGEHIVYRLLL
PRIKNKSKLQYWLHTSQRLHRAINTSFIEEKQQHFKTKRVEKRSNVGPRQLTVWNTSNLS
HDNRRKYIFSDEEGQNQLGIRIHQDIPLPPRRRELPALRTTNGKADSLNVSRNSVMQELS
ELEKQIQVIRQELQLAVSRKTELEEYQRTSRTCES

• Lig_chan (PF00060 )

• 1-23

• 675-695 749-769 931-951

ATGAGGAGACTGAGTTTGTGGTGGCTGCTGAGCAGGGTCTGTCTGCTGTTGCCGCCGCCC
TGCGCACTGGTGCTGGCCGGGGTGCCCAGCTCCTCCTCGCACCCGCAGCCCTGCCAGATC
CTCAAGCGCATCGGGCACGCGGTGAGGGTGGGCGCGGTGCACTTGCAGCCCTGGACCACC
GCCCCCCGCGCGGCCAGCCGCGCTCCGGACGACAGCCGAGCAGGAGCCCAGAGGGATGAG
CCGGAGCCAGGGACTAGGCGGTCCCCGGCGCCCTCGCCGGGCGCACGCTGGTTGGGGAGC
ACCCTGCATGGCCGGGGGCCGCCGGGCTCCCGTAAGCCCGGGGAGGGCGCCAGGGCGGAG
GCCCTGTGGCCACGGGACGCCCTCCTATTTGCCGTGGACAACCTGAACCGCGTGGAAGGG
CTGCTACCCTACAACCTGTCTTTGGAAGTAGTGATGGCCATCGAGGCAGGCCTGGGCGAT
CTGCCACTTTTGCCCTTCTCCTCCCCTAGTTCGCCATGGAGCAGTGACCCTTTCTCCTTC
CTGCAAAGTGTGTGCCATACCGTGGTGGTGCAAGGGGTGTCGGCGCTGCTCGCCTTCCCC
CAGAGCCAGGGCGAAATGATGGAGCTCGACTTGGTCAGCTTAGTCCTGCACATTCCAGTG
ATCAGCATCGTGCGCCACGAGTTTCCGCGGGAGAGTCAGAATCCCCTTCACCTACAACTG
AGTTTAGAAAATTCATTAAGTTCTGATGCTGATGTCACTGTCTCAATCCTGACCATGAAC
AACTGGTACAATTTTAGCTTGTTGCTGTGCCAGGAAGACTGGAACATCACCGACTTCCTC
CTCCTTACCCAGAATAATTCCAAGTTCCACCTTGGTTCTATCATCAACATCACCGCTAAC
CTCCCCTCCACCCAGGACCTCTTGAGCTTCCTACAGATCCAGCTTGAGAGTATTAAGAAC
AGCACACCCACAGTGGTGATGTTTGGCTGCGACATGGAAAGTATCCGGCGGATTTTCGAA
ATTACAACCCAGTTTGGGGTCATGCCCCCTGAACTTCGTTGGGTGCTGGGAGATTCCCAG
AATATGGAGGAACTGAGGACAGAGGGTCTGCCCTTAGGACTCATTGCTCATGGAAAAACA
ACACAGTCTGTCTTTGAGCACTACGTACAAGATGCTATGGAGCTGGTCGCAAGAGCTGTA
GCCACAGCCACCATGATCCAACCAGAACTTGCTCTCATTCCCAGCACGATGAACTGCATG
GAGGTGGAAACTACAAATCTCACTTCAGGACAATATTTATCAAGGTTTCTAGCCAATACC
ACTTTCAGAGGCCTCAGTGGTTCCATCAGAGTAAAAGGTTCCACCATCGTCAGCTCAGAA
AACAACTTTTTCATCTGGAATCTTCAACATGACCCCATGGGAAAGCCAATGTGGACCCGC
TTGGGCAGCTGGCAGGGGAGAAAGATTGTCATGGACTATGGAATATGGCCAGAGCAGGCC
CAGAGACACAAAACCCACTTCCAACATCCAAGTAAGCTACACTTGAGAGTGGTTACCCTG
ATTGAGCATCCTTTTGTCTTCACAAGGGAGGTAGATGATGAAGGCTTGTGCCCTGCTGGC
CAACTCTGTCTAGACCCCATGACTAATGACTCTTCCACACTGGACAGCCTTTTTAGCAGC
CTCCATAGCAGTAATGATACAGTGCCCATTAAATTCAAGAAGTGCTGCTATGGATATTGC
ATTGATCTGCTGGAAAAGATAGCAGAAGACATGAACTTTGACTTCGACCTCTATATTGTA
GGGGATGGAAAGTATGGAGCCTGGAAAAATGGGCACTGGACTGGGCTAGTGGGTGATCTC
CTGAGAGGGACTGCCCACATGGCAGTCACTTCCTTTAGCATCAATACTGCACGGAGCCAG
GTGATAGATTTCACCAGCCCTTTCTTCTCCACCAGCTTGGGCATCTTAGTGAGGACCCGA
GATACAGCAGCTCCCATTGGAGCCTTCATGTGGCCACTCCACTGGACAATGTGGCTGGGG
ATTTTTGTGGCTCTGCACATCACTGCCGTCTTCCTCACTCTGTATGAATGGAAGAGTCCA
TTTGGTTTGACTCCCAAGGGGCGAAATAGAAGTAAAGTCTTCTCCTTTTCTTCAGCCTTG
AACATCTGTTATGCCCTCTTGTTTGGCAGAACAGTGGCCATCAAACCTCCAAAATGTTGG
ACTGGAAGGTTTCTAATGAACCTTTGGGCCATTTTCTGTATGTTTTGCCTTTCCACATAC
ACGGCAAACTTGGCTGCTGTCATGGTAGGTGAGAAGATCTATGAAGAGCTTTCTGGAATA
CATGACCCCAAGTTACATCATCCTTCCCAAGGATTCCGCTTTGGAACTGTCCGAGAAAGC
AGTGCTGAAGATTATGTGAGACAAAGTTTCCCAGAGATGCATGAATATATGAGAAGGTAC
AATGTTCCAGCCACCCCTGATGGAGTGGAGTATCTGAAGAACAATCCAGAGAAACTAGAC
GCCTTCATCATGGACAAAGCCCTTCTGGATTATGAAGTGTCAATAGATGCTGACTGCAAA
CTTCTCACTGTGGGGAAGCCATTTGCCATAGAAGGATACGGCATTGGCCTCCCACCCAAC
TCTCCATTGACCGCCAACATATCCGAGCTAATCAGTCAATACAAGTCACATGGGTTTATG
GATATGCTCCATGACAAGTGGTACAGGGTGGTTCCCTGTGGCAAGAGAAGTTTTGCTGTC
ACGGAGACTTTGCAAATGGGCATCAAACACTTCTCTGGGCTCTTTGTGCTGCTGTGCATT
GGATTTGGTCTGTCCATTTTGACCACCATTGGTGAGCACATAGTATACAGGCTGCTGCTA
CCACGAATCAAAAACAAATCCAAGCTGCAATACTGGCTCCACACCAGCCAGAGATTACAC
AGAGCAATAAATACATCATTTATAGAGGAAAAGCAGCAGCATTTCAAGACCAAACGTGTG
GAAAAGAGGTCTAATGTGGGACCCCGTCAGCTTACCGTATGGAATACTTCCAATCTGAGT
CATGACAACCGACGGAAATACATCTTTAGTGATGAGGAAGGACAAAACCAGCTGGGCATC
CGGATCCACCAGGACATCCCCCTCCCTCCAAGGAGAAGAGAGCTCCCTGCCTTGCGGACC
ACCAATGGGAAAGCAGACTCCCTAAATGTATCTCGGAACTCAGTGATGCAGGAACTCTCA
GAGCTCGAGAAGCAGATTCAGGTGATCCGTCAGGAGCTGCAGCTGGCTGTGAGCAGGAAA
ACGGAGCTGGAGGAGTATCAAAGGACAAGTCGGACTTGTGAGTCCTAG

1. Andersson O, Stenqvist A, Attersand A, von Euler G: Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B. Genomics. 2001 Dec;78(3):178-84. [PubMed ]
2. Eriksson M, Nilsson A, Froelich-Fabre S, Akesson E, Dunker J, Seiger A, Folkesson R, Benedikz E, Sundstrom E: Cloning and expression of the human N-methyl-D-aspartate receptor subunit NR3A. Neurosci Lett. 2002 Mar 22;321(3):177-81. [PubMed ]
3. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed ]

1. GABA(Areceptor subunit alpha-1