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Human Metabolome Database Version 2.5

 

Showing metabocard for 1-Hexadecanol (HMDB03424)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 21:33:57
Update Date 2009-05-05 20:59:46
Accession Number HMDB03424
Secondary Accession Numbers Not Available
Common Name 1-Hexadecanol
Description Cetyl alcohol, also known as 1-hexadecanol and palmityl alcohol, is a solid organic compound and a member of the alcohol class of compounds. Its chemical formula is CH3(CH2)15OH. At room temperature, cetyl alcohol takes the form of a waxy white solid or flakes. It belongs to the group of fatty alcohols. With the demise of commercial whaling, cetyl alcohol is no longer primarily produced from whale oil, but instead either as an end-product of the petroleum industry, or produced from vegetable oils such as palm oil and coconut oil. Production of cetyl alcohol from palm oil gives rise to one of its alternative names, palmityl alcohol.
Synonyms
  1. 1-Cetanol
  2. 1-Hexadecyl alc
  3. 1-Hexadecyl alcohol
  4. 1-Hexanedecanol
  5. 1-Hydroxyhexadecane
  6. 1-hexadecanol
  7. 16-Hexadecanol
  8. Adol
  9. Adol 52
  10. Adol 52 NF
  11. Adol 52NF
  12. Adol 54
  13. Alcohol C-16
  14. Aldol 54
  15. Alfol 16
  16. Atalco C
  17. C16 alcohol
  18. Cachalot C-50
  19. Cachalot C-50 NF
  20. Cachalot C-51
  21. Cachalot C-52
  22. Ceraphyl ICA
  23. Cetaffine
  24. Cetal
  25. Cetalol CA
  26. Cetanol
  27. Cetostearyl alcohol
  28. Cetyl alcohol
  29. Cetyl alcohol NF
  30. Cetylic alcohol
  31. Cetylol
  32. Crodacol C
  33. Crodacol C70
  34. Crodacol C95NF
  35. Crodacol-CAS
  36. Crodacol-CAT
  37. Cyclal cetyl alcohol
  38. Dehydag wax 16
  39. Dytol F-11
  40. Elfacos C
  41. Epal 16NF
  42. Ethal
  43. Ethol
  44. Eutanol G16
  45. Exxal 16
  46. Fancol CA
  47. Fatty alcohol
  48. Hexadecan-1-ol
  49. Hexadecanol
  50. Hexadecanol NF
  51. Hexadecyl alcohol
  52. Hyfatol
  53. Hyfatol 16
  54. Isocetyl alcohol
  55. Isohexadecanol
  56. Isohexadecyl alcohol
  57. Lanette 16
  58. Lanol C
  59. Lipocol C
  60. Lorol 24
  61. Lorol C16
  62. LorolL 24
  63. Loxanol K
  64. Loxanol K extra
  65. Loxanwachs SK
  66. Loxiol VPG 1743
  67. Michel XO-150-16
  68. Myristyl alcohol
  69. N-Hexadecyl alcohol
  70. Normal primary hexadecyl alcohol
  71. Palmityl alcohol
  72. Philcohol 1600
  73. Product 308
  74. Rita CA
  75. SSD
  76. SSD RP
  77. Siponol CC
  78. Siponol wax-A
  79. n-1-Hexadecanol
  80. n-Cetyl alcohol
  81. n-Hexadecan-1-ol
  82. n-Hexadecanol
Chemical IUPAC Name hexadecan-1-ol
Chemical Formula C16H34O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
Sub Class
  • Simple alcohols
Family
  • Mammalian Metabolite
Species
  • primary alcohol
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 242.441
Monoisotopic Molecular Weight 242.260971
Isomeric SMILES CCCCCCCCCCCCCCCCO
Canonical SMILES CCCCCCCCCCCCCCCCO
KEGG Compound ID C00823 Link Image
BioCyc ID CPD-348 Link Image
BiGG ID Not Available
Wikipedia Link 1-Hexadecanol Link Image
NuGOwiki Link HMDB03424 Link Image
Metagene Link HMDB03424 Link Image
METLIN ID 6927 Link Image
PubChem Compound 2682 Link Image
PubChem Substance 588000 Link Image
ChEBI ID 16125 Link Image
CAS Registry Number 36653-82-4
InChI Identifier InChI=1/C16H34O/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17/h17H,2-16H2,1H3
Synthesis Reference Mihalovici, Ar.; Bors, G. Preparation of cetyl alcohol. Curierul Farmaceutic (1938), 8(No. 6), 1-9.
Melting Point (Experimental) 49.3 oC
Experimental Water Solubility 1.34e-05 mg/mL at 25 oC [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 1.81e-04 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 7.17 [Predicted by ALOGPS]; 6.2 [Predicted by PubChem via XLOGP]; 6.73 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
Biofluid Location Not Available
Tissue Location
Tissue References
Fibroblasts
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Plasmalogen Synthesis SMP00479 Link Image
General References
  1. Rizzo WB, Craft DA: Sjogren-Larsson syndrome: accumulation of free fatty alcohols in cultured fibroblasts and plasma. J Lipid Res. 2000 Jul;41(7):1077-81. [PubMed Link Image]
  2. Hargrove JL, Greenspan P, Hartle DK: Nutritional significance and metabolism of very long chain fatty alcohols and acids from dietary waxes. Exp Biol Med (Maywood). 2004 Mar;229(3):215-26. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Alkyldihydroxyacetonephosphate synthase, peroxisomal
  2. Fatty acyl-CoA reductase 1
  3. Fatty acyl-CoA reductase 2
  4. Acyl-CoA wax alcohol acyltransferase 1
  5. Acyl-CoA wax alcohol acyltransferase 2
Enzyme 1 [top]
Enzyme 1 ID 6838
Enzyme 1 Name Alkyldihydroxyacetonephosphate synthase, peroxisomal
Enzyme 1 Synonyms
  1. Alkyl-DHAP synthase
  2. Aging-associated gene 5 protein
  3. Alkylglycerone-phosphate synthase
Enzyme 1 Gene Name AGPS
Enzyme 1 Protein Sequence >Alkyldihydroxyacetonephosphate synthase, peroxisomal
MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKA
RRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPL
SGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEAD
DRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTS
VSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGH
EPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDI
HHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRL
MDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQH
EKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDL
CRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEA
AAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL
Enzyme 1 Number of Residues 658
Enzyme 1 Molecular Weight 72911.2
Enzyme 1 Theoretical pI 7.37
Enzyme 1 GO Classification
Function
  • FAD or FADH2 binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • purine nucleoside binding
Process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion [RN:R04311]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 189054871 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID O00116 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ADAS_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1977 bp
ATGGCGGAGGCGGCGGCTGCAGCGGGTGGGACTGGCTTGGGCGCGGGCGCGAGCTACGGG
TCTGCAGCGGACCGGGACCGGGACCCGGACCCGGACCGCGCCGGGCGGAGGCTGCGGGTT
CTCTCTGGCCATCTGCTGGGCCGGCCCCGGGAGGCTCTGAGTACCAATGAGTGCAAAGCG
CGGAGAGCCGCGTCGGCGGCCACGGCAGCGCCCACGGCCACTCCCGCCGCGCAGGAGTCG
GGCACCATCCCAAAGAAGCGGCAAGAAGTTATGAAATGGAATGGATGGGGATATAATGAT
TCTAAATTCATCTTCAATAAGAAGGGCCAAATTGAATTGACTGGGAAAAGGTACCCTCTT
AGTGGCATGGGTTTACCAACATTTAAAGAATGGATCCAAAATACCCTTGGAGTAAATGTG
GAGCATAAAACTACCTCTAAAGCATCCTTAAATCCTAGTGATACACCTCCTTCTGTTGTA
AATGAAGATTTTCTTCATGACCTTAAAGAAACTAATATTTCATATTCACAAGAGGCAGAT
GATCGAGTATTTAGAGCTCATGGTCATTGTCTTCATGAGATATTTTTGCTCAGGGAAGGA
ATGTTTGAGCGAATTCCTGATATAGTTTTATGGCCAACATGCCATGATGATGTAGTTAAG
ATTGTGAATCTAGCTTGCAAATATAATCTTTGTATCATACCAATTGGTGGAGGAACAAGT
GTTTCATATGGCCTGATGTGTCCTGCAGATGAGACAAGAACAATTATTTCTTTGGACACT
TCACAAATGAATCGAATTCTCTGGGTTGATGAGAACAATTTGACAGCTCATGTAGAGGCT
GGCATAACAGGACAAGAGTTGGAAAGACAGCTTAAAGAAAGTGGTTATTGTACAGGTCAT
GAACCAGATTCCCTGGAGTTCAGTACTGTAGGAGGATGGGTATCTACTCGCGCATCAGGC
ATGAAGAAGAATATCTATGGCAATATCGAGGACCTGGTGGTTCATATAAAAATGGTAACA
CCTAGAGGTATAATAGAAAAAAGCTGTCAAGGACCTCGTATGTCAACAGGCCCTGATATC
CATCACTTCATCATGGGATCTGAAGGAACTCTTGGTGTAATAACAGAAGCTACAATAAAA
ATCAGACCAGTCCCTGAATACCAAAAGTATGGCTCAGTAGCTTTCCCTAATTTTGAACAA
GGAGTAGCCTGTTTAAGAGAAATTGCAAAACAGAGATGTGCTCCGGCATCTATTCGCCTC
ATGGACAACAAGCAGTTTCAGTTTGGTCATGCTCTTAAACCTCAGGTTTCCTCTATTTTT
ACATCATTTTTGGACGGATTAAAAAAGTTTTATATTACAAAGTTTAAAGGATTTGACCCA
AATCAGCTAAGTGTAGCCACATTACTGTTTGAGGGGGATCGTGAGAAGGTTCTTCAACAT
GAAAAACAAGTGTATGATATTGCTGCAAAATTTGGTGGGTTGGCAGCTGGAGAAGATAAT
GGACAGAGAGGTTATTTGCTGACCTATGTTATTGCATACATTCGAGACTTGGCTTTGGAA
TACTATGTATTAGGAGAATCTTTTGAGACTTCTGCTCCTTGGGACAGGGTGGTAGATCTC
TGTAGAAATGTAAAAGAAAGAATAACAAGGGAATGCAAAGAGAAGGGTGTTCAGTTTGCT
CCTTTTTCTACATGCAGGGTGACGCAGACTTACGATGCAGGTGCTTGTATCTACTTCTAT
TTTGCCTTTAACTACAGGGGAATTAGTGACCCACTGACCGTATTTGAACAAACTGAGGCA
GCTGCTAGAGAAGAAATCCTTGCTAATGGAGGGAGCCTGTCACATCACCATGGAGTGGGC
AAGTTACGGAAGCAATGGCTAAAGGAAAGTATCTCTGATGTCGGCTTTGGGATGCTGAAG
TCTGTCAAGGAATATGTGGACCCCAATAACATCTTTGGAAACAGAAACCTTTTATAA
Enzyme 1 GenBank Gene ID AK314259 Link Image
Enzyme 1 GeneCard ID AGPS Link Image
Enzyme 1 GenAtlas ID AGPS Link Image
Enzyme 1 HGNC ID HGNC:327 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2q31.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. de Vet EC, van den Broek BT, van den Bosch H: Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2. Biochim Biophys Acta. 1997 May 17;1346(1):25-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  5. de Vet EC, Ijlst L, Oostheim W, Wanders RJ, van den Bosch H: Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency. J Biol Chem. 1998 Apr 24;273(17):10296-301. [PubMed Link Image]
  6. Thai TP, Rodemer C, Jauch A, Hunziker A, Moser A, Gorgas K, Just WW: Impaired membrane traffic in defective ether lipid biosynthesis. Hum Mol Genet. 2001 Jan 15;10(2):127-36. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 12889
Enzyme 2 Name Fatty acyl-CoA reductase 1
Enzyme 2 Synonyms
  1. Male sterility domain-containing protein 2
Enzyme 2 Gene Name FAR1
Enzyme 2 Protein Sequence >Fatty acyl-CoA reductase 1
MVSIPEYYEGKNVLLTGATGFLGKVLLEKLLRSCPKVNSVYVLVRQKAGQTPQERVEEVL
SGKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEVIIDSTNIIFHCAATVRFNEN
LRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDS
LEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPF
PGWIDNFNGPSGLFIAAGKGILRTIRASNNALADLVPVDVVVNMSLAAAWYSGVNRPRNI
MVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAP
AFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTENVNMLMNQLNPEDKKT
FNIDVRQLHWAEYIENYCLGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWR
IFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY
Enzyme 2 Number of Residues 515
Enzyme 2 Molecular Weight 59356.3
Enzyme 2 Theoretical pI 9.52
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 466-483
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 37182687 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8WVX9 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name FACR1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1548 bp
ATGGTTTCAATCCCAGAATACTATGAAGGCAAGAACGTCCTCCTCACAGGAGCTACCGGT
TTTCTAGGGAAGGTGCTTCTGGAAAAGTTGCTGAGGTCTTGTCCTAAGGTGAATTCAGTA
TATGTTTTGGTGAGGCAGAAAGCTGGACAGACACCACAAGAGCGAGTGGAAGAAGTCCTT
AGTGGCAAGCTTTTTGACAGATTGAGAGATGAAAATCCAGATTTTAGAGAGAAAATTATA
GCAATCAACAGCGAACTCACCCAACCTAAACTGGCTCTCAGTGAAGAAGATAAAGAGGTG
ATCATAGATTCTACCAATATTATATTCCACTGTGCAGCTACAGTAAGGTTTAATGAAAAT
TTAAGAGATGCTGTTCAGTTAAATGTGATTGCAACGCGACAGCTTATTCTCCTTGCACAA
CAAATGAAGAATCTGGAAGTGTTCATGCATGTATCAACAGCATATGCCTACTGTAATCGC
AAGCATATTGATGAAGTAGTCTATCCACCACCTGTGGATCCCAAGAAGCTGATTGATTCT
TTAGAGTGGATGGATGATGGCCTAGTAAATGATATCACGCCAAAATTGATAGGAGACAGA
CCTAATACATACATATACACAAAAGCATTGGCAGAATATGTTGTACAACAAGAAGGAGCA
AAACTAAATGTGGCAATTGTAAGGCCATCGATTGTTGGTGCCAGTTGGAAAGAACCTTTT
CCAGGATGGATTGATAACTTTAATGGACCAAGTGGTCTCTTTATTGCGGCAGGGAAAGGA
ATTCTTCGAACAATACGTGCCTCCAACAATGCCCTTGCAGATCTTGTTCCTGTAGATGTA
GTTGTCAACATGAGTCTTGCGGCAGCCTGGTATTCCGGAGTTAATAGACCAAGAAACATC
ATGGTGTATAATTGTACAACAGGCAGCACTAATCCTTTCCACTGGGGTGAAGTTGAGTAC
CATGTAATTTCCACTTTCAAGAGGAATCCTCTCGAACAGGCCTTCAGACGGCCCAATGTA
AATCTAACCTCCAATCATCTTTTATATCATTACTGGATTGCTGTAAGCCATAAGGCCCCA
GCATTCCTGTATGATATCTACCTCAGGATGACTGGAAGAAGCCCAAGGATGATGAAAACA
ATAACTCGTCTTCACAAAGCTATGGTGTTTCTTGAATATTTCACAAGTAATTCTTGGGTT
TGGAATACTGAGAATGTCAATATGTTAATGAATCAACTAAACCCTGAAGATAAAAAGACC
TTCAATATTGATGTACGGCAGTTACATTGGGCAGAATATATAGAGAACTACTGCTTGGGA
ACTAAGAAGTACGTATTGAATGAAGAAATGTCTGGCCTCCCTGCAGCCAGAAAACATCTG
AACAAGTTGCGGAATATACGTTATGGTTTTAATACTATCCTTGTGATCCTCATCTGGCGC
ATTTTTATTGCAAGATCACAAATGGCAAGAAATATCTGGTACTTTGTGGTTAGTCTGTGT
TACAAGTTTTTGTCATACTTCCGAGCATCCAGCACTATGAGATACTGA
Enzyme 2 GenBank Gene ID AY358784 Link Image
Enzyme 2 GeneCard ID FAR1 Link Image
Enzyme 2 GenAtlas ID FAR1 Link Image
Enzyme 2 HGNC ID HGNC:26222 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 11p15.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed Link Image]
  2. 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 Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 12890
Enzyme 3 Name Fatty acyl-CoA reductase 2
Enzyme 3 Synonyms
  1. Male sterility domain-containing protein 1
Enzyme 3 Gene Name FAR2
Enzyme 3 Protein Sequence >Fatty acyl-CoA reductase 2
MSTIAAFYGGKSILITGATGFLGKVLMEKLFRTSPDLKVIYILVRPKAGQTLQQRVFQIL
DSKLFEKVKEVCPNVHEKIRAIYADLNQNDFAISKEDMQELLSCTNIIFHCAATVRFDDT
LRHAVQLNVTATRQLLLMASQMPKLEAFIHISTAYSNCNLKHIDEVIYPCPVEPKKIIDS
LEWLDDAIIDEITPKLIRDWPNIYTYTKALGEMVVQQESRNLNIAIIRPSIVGATWQEPF
PGWVDNINGPNGIIIATGKGFLRAIKATPMAVADVIPVDTVVNLMLAVGWYTAVHRPKST
LVYHITSGNMNPCNWHKMGVQVLATFEKIPFERPFRRPNANFTSNSFTSQYWNAVSHRAP
AIIYDCYLRLTGRKPRMTKLMNRLLRTVSMLEYFINRSWEWSTYNTEMLMSELSPEDQRV
FNFDVRQLNWLEYIENYVLGVKKYLLKEDMAGIPKAKQRLKRLRNIHYLFNTALFLIAWR
LLIARSQMARNVWFFIVSFCYKFLSYFRASSTLKV
Enzyme 3 Number of Residues 515
Enzyme 3 Molecular Weight 59437.9
Enzyme 3 Theoretical pI 9.79
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 3 General Function Involved in catalytic activity
Enzyme 3 Specific Function Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. The preferred substrates are C16, C18, C18:1 and C18:2 but low activity can be observed with C10-C14 substrates
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 465-484 491-510
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7022510 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96K12 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name FACR2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1548 bp
ATGTCCACAATTGCAGCTTTCTATGGCGGCAAGTCCATCCTCATCACGGGGGCCACAGGC
TTTCTGGGCAAAGTGCTAATGGAGAAGCTGTTTCGCACCAGCCCAGACCTGAAAGTCATT
TACATCCTTGTGAGGCCCAAGGCTGGCCAGACACTGCAGCAGAGGGTTTTCCAGATCCTA
GACAGTAAGCTATTTGAGAAAGTCAAAGAAGTTTGTCCAAATGTGCATGAGAAGATCAGA
GCTATTTATGCAGATCTCAATCAGAATGACTTTGCCATCAGCAAAGAGGACATGCAGGAG
CTTCTCTCCTGTACAAACATAATATTTCACTGTGCAGCCACTGTACGCTTTGACGACACT
CTCAGACATGCTGTGCAACTTAACGTCACTGCCACCCGGCAGCTCTTGCTTATGGCTAGT
CAGATGCCAAAGCTGGAAGCCTTTATACATATCTCTACTGCCTATTCAAATTGTAACCTG
AAGCACATCGATGAAGTTACCTATCCGTGCCCTGTGGAGCCAAAAAAAATCATTGATTCC
CTTGAGTGGTTAGACGATGCTATTATTGACGAGATTACACCCAAGCTGATCAGAGATTGG
CCCAATATTTATACCTACACCAAGGCCTTGGGAGAAATGGTGGTGCAGCAAGAGAGCAGG
AACCTGAACATTGCCATCATAAGGCCCTCCATTGTGGGAGCAACTTGGCAGGAGCCTTTC
CCAGGTTGGGTTGATAATATAAATGGACCTAATGGAATCATTATTGCGACTGGGAAAGGG
TTTCTTCGGGCCATAAAAGCTACTCCAATGGCTGTGGCAGACGTAATTCCAGTTGATACA
GTCGTCAATCTCATGCTAGCTGTAGGATGGTATACTGCAGTTCACAGACCTAAGTCAACA
TTAGTCTACCACATTACATCTGGTAACATGAATCCCTGCAATTGGCACAAAATGGGAGTC
CAAGTCTTGGCAACCTTTGAAAAAATCCCATTTGAGAGACCTTTCAGGAGGCCAAATGCT
AATTTTACCAGCAACAGCTTCACATCACAGTACTGGAATGCGGTCAGCCACCGGGCCCCT
GCCATTATCTATGACTGCTATCTGCGGCTCACTGGAAGGAAGCCCAGGATGACAAAGCTC
ATGAATCGGCTTTTAAGAACTGTTTCCATGTTGGAGTATTTCATCAACCGGAGTTGGGAA
TGGAGCACGTACAATACAGAAATGCTGATGTCTGAGCTGAGTCCTGAAGACCAGAGGGTA
TTCAACTTTGACGTGCGCCAGTTGAACTGGTTGGAATACATTGAAAATTATGTTTTGGGA
GTTAAAAAATACTTATTGAAAGAGGATATGGCTGGGATCCCAAAGGCAAAGCAACGCTTA
AAAAGGCTCCGAAATATTCACTACCTCTTTAATACTGCCCTCTTCCTTATCGCCTGGCGC
CTTCTCATTGCAAGATCTCAGATGGCTCGGAATGTCTGGTTCTTCATTGTAAGCTTCTGT
TATAAATTCCTCTCCTACTTTAGAGCATCCAGCACGCTCAAAGTTTAA
Enzyme 3 GenBank Gene ID AK001324 Link Image
Enzyme 3 GeneCard ID FAR2 Link Image
Enzyme 3 GenAtlas ID FAR2 Link Image
Enzyme 3 HGNC ID HGNC:25531 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 12p11.22
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  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 Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cheng JB, Russell DW: Mammalian wax biosynthesis. I. Identification of two fatty acyl-Coenzyme A reductases with different substrate specificities and tissue distributions. J Biol Chem. 2004 Sep 3;279(36):37789-97. Epub 2004 Jun 27. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 12897
Enzyme 4 Name Acyl-CoA wax alcohol acyltransferase 1
Enzyme 4 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 3
  2. Diacylglycerol acyltransferase 2
  3. Long-chain-alcohol O-fatty-acyltransferase 1
Enzyme 4 Gene Name AWAT1
Enzyme 4 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 1
MAHSKQPSHFQSLMLLQWPLSYLAIFWILQPLFVYLLFTSLWPLPVLYFAWLFLDWKTPE
RGGRRSAWVRNWCVWTHIRDYFPITILKTKDLSPEHNYLMGVHPHGLLTFGAFCNFCTEA
TGFSKTFPGITPHLATLSWFFKIPFVREYLMAKGVCSVSQPAINYLLSHGTGNLVGIVVG
GVGEALQSVPNTTTLILQKRKGFVRTALQHGAHLVPTFTFGETEVYDQVLFHKDSRMYKF
QSCFRRIFGFYCCVFYGQSFCQGSTGLLPYSRPIVTVVGEPLPLPQIEKPSQEMVDKYHA
LYMDALHKLFDQHKTHYGCSETQKLFFL
Enzyme 4 Number of Residues 328
Enzyme 4 Molecular Weight 37758.8
Enzyme 4 Theoretical pI 9.02
Enzyme 4 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 4 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 4 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has a preference for arachidyl alcohol as well as decyl alcohol, demonstrating its relatively poor activity using saturated long chain alcohols (C16, C18, and C20)
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 12-32 34-53
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 123227401 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q58HT5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name AWAT1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >987 bp
ATGGCTCATTCCAAGCAGCCTAGTCACTTCCAGAGTCTGATGCTTCTGCAGTGGCCTTTG
AGCTACCTTGCCATCTTTTGGATCTTGCAGCCATTGTTCGTCTACCTGCTGTTTACATCC
TTGTGGCCGCTACCAGTGCTTTACTTTGCCTGGTTGTTCCTGGACTGGAAGACCCCAGAG
CGAGGTGGCAGGCGTTCGGCCTGGGTAAGGAACTGGTGTGTCTGGACCCACATCAGGGAC
TATTTCCCCATTACGATCCTGAAGACAAAGGACCTATCACCTGAGCACAACTACCTCATG
GGGGTTCACCCCCATGGCCTCCTGACCTTTGGCGCCTTCTGCAACTTCTGCACTGAGGCC
ACAGGCTTCTCGAAGACCTTCCCAGGCATCACTCCTCACTTGGCCACGCTGTCCTGGTTC
TTCAAGATCCCCTTTGTTAGGGAGTACCTCATGGCCAAAGGTGTGTGCTCTGTGAGCCAG
CCAGCCATCAACTATCTGCTGAGCCATGGCACTGGCAACCTCGTGGGCATTGTAGTGGGA
GGTGTGGGTGAGGCCCTGCAAAGTGTGCCCAACACCACCACCCTCATCCTCCAGAAGCGC
AAGGGGTTCGTGCGCACAGCCCTCCAGCATGGGGCTCATCTGGTCCCCACCTTCACTTTT
GGGGAAACTGAGGTGTATGATCAGGTGCTGTTCCATAAGGATAGCAGGATGTACAAGTTC
CAGAGCTGCTTCCGCCGTATCTTTGGTTTCTACTGTTGTGTCTTCTATGGACAAAGCTTC
TGTCAAGGCTCCACTGGGCTCCTGCCATACTCCAGGCCTATTGTCACTGTGGTTGGGGAG
CCTCTGCCACTGCCCCAAATTGAAAAGCCAAGCCAGGAGATGGTGGACAAATACCATGCA
CTTTATATGGATGCTCTGCACAAACTGTTCGACCAGCATAAGACCCACTATGGCTGCTCA
GAGACCCAAAAGCTGTTTTTCCTGTGA
Enzyme 4 GenBank Gene ID AL357752 Link Image
Enzyme 4 GeneCard ID AWAT1 Link Image
Enzyme 4 GenAtlas ID AWAT1 Link Image
Enzyme 4 HGNC ID HGNC:23252 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 12898
Enzyme 5 Name Acyl-CoA wax alcohol acyltransferase 2
Enzyme 5 Synonyms
  1. Diacylglycerol O-acyltransferase 2-like protein 4
  2. Diacylglycerol O-acyltransferase candidate 4
  3. hDC4
  4. Long-chain-alcohol O-fatty-acyltransferase 2
  5. Multifunctional O-acyltransferase
  6. Wax synthase
  7. hWS
Enzyme 5 Gene Name AWAT2
Enzyme 5 Protein Sequence >Acyl-CoA wax alcohol acyltransferase 2
MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW
KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF
ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV
IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG
FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV
AKYHTLYIDALRKLFDQHKTKFGISETQELEII
Enzyme 5 Number of Residues 333
Enzyme 5 Molecular Weight 38093.2
Enzyme 5 Theoretical pI 9.69
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
Component
Enzyme 5 General Function Involved in transferase activity, transferring acyl groups other than amino-acyl groups
Enzyme 5 Specific Function Acyltransferase that predominantly esterify long chain (wax) alcohols with acyl-CoA-derived fatty acids to produce wax esters. Wax esters are enriched in sebum, suggesting that it plays a central role in lipid metabolism in skin. Has no activity using decyl alcohol and significantly prefers the C16 and C18 alcohols. May also have 2-acylglycerol O-acyltransferase (MGAT) and acyl- CoA:retinol acyltransferase (ARAT) activities, to catalyze the synthesis of diacylglycerols and retinyl esters; however this activity is unclear in vivo
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • acyl-CoA + a long-chain alcohol = CoA + a long-chain ester [RN:R01999]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 15-35 38-58 130-150
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 49854214 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q6E213 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name AWAT2_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1002 bp
ATGCTCTTGCCCTCTAAGAAGGACCTCAAGACTGCCCTGGATGTCTTTGCTGTTTTCCAG
TGGTCCTTCAGTGCCTTGCTTATCACAACCACTGTGATTGCTGTCAACCTCTACCTGGTG
GTGTTCACACCATACTGGCCTGTCACTGTGCTTATTCTTACCTGGCTGGCTTTTGACTGG
AAGACCCCTCAGCGAGGCGGCCGCCGGTTTACCTGTGTGAGGCACTGGCGCCTGTGGAAA
CACTACAGCGATTATTTCCCTCTCAAGCTTCTGAAGACTCATGACATCTGCCCCAGCCGC
AACTACATCCTCGTCTGCCACCCTCATGGGCTCTTTGCCCATGGATGGTTTGGCCACTTT
GCCACAGAGGCCTCAGGCTTCTCCAAGATATTTCCTGGCATCACCCCTTACATACTCACA
CTGGGAGCCTTTTTCTGGATGCCTTTCCTCAGAGAATATGTAATGTCTACAGGGGCCTGC
TCTGTGAGTCGATCCTCCATTGACTTTCTGCTGACTCATAAAGGCACAGGCAACATGGTC
ATTGTGGTGATTGGTGGACTGGCTGAGTGCAGATACAGCCTGCCAGGTTCTTCTACCCTG
GTGTTGAAGAACCGGTCTGGCTTTGTGCGCATGGCCCTTCAGCATGGGGTGCCTCTAATA
CCTGCCTATGCCTTTGGGGAGACGGACCTCTATGATCAGCACATTTTCACTCCTGGTGGC
TTTGTCAACCGCTTCCAGAAGTGGTTCCAGAGCATGGTACACATCTACCCTTGTGCTTTC
TATGGACGTGGCTTCACCAAGAACTCCTGGGGCCTTCTGCCCTATAGTCGGCCTGTAACC
ACCATCGTCGGGGAGCCTCTACCAATGCCCAAGATTGAGAATCCAAGCCAGGAGATCGTG
GCTAAATATCACACACTCTATATTGATGCCCTACGTAAACTGTTTGACCAGCATAAGACC
AAGTTTGGTATCTCAGAGACCCAGGAGCTGGAGATAATTTGA
Enzyme 5 GenBank Gene ID AY605053 Link Image
Enzyme 5 GeneCard ID AWAT2 Link Image
Enzyme 5 GenAtlas ID AWAT2 Link Image
Enzyme 5 HGNC ID HGNC:23251 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Cheng JB, Russell DW: Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. J Biol Chem. 2004 Sep 3;279(36):37798-807. Epub 2004 Jun 27. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Winter A, van Eckeveld M, Bininda-Emonds OR, Habermann FA, Fries R: Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet Genome Res. 2003;102(1-4):42-7. [PubMed Link Image]
  4. Turkish AR, Henneberry AL, Cromley D, Padamsee M, Oelkers P, Bazzi H, Christiano AM, Billheimer JT, Sturley SL: Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. J Biol Chem. 2005 Apr 15;280(15):14755-64. Epub 2005 Jan 25. [PubMed Link Image]
  5. Yen CL, Brown CH 4th, Monetti M, Farese RV Jr: A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. J Lipid Res. 2005 Nov;46(11):2388-97. Epub 2005 Aug 16. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available