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Identification
HMDB Protein ID HMDBP00252
Secondary Accession Numbers
  • 5484
Name Peptidyl-glycine alpha-amidating monooxygenase
Synonyms
  1. PAL
  2. PAM
  3. PHM
  4. Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
  5. Peptidylamidoglycolate lyase
  6. Peptidylglycine alpha-hydroxylating monooxygenase
Gene Name PAM
Protein Type Unknown
Biological Properties
General Function Involved in monooxygenase activity
Specific Function Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
Pathways Not Available
Reactions
Peptidylglycine + Ascorbic acid + Oxygen → peptidyl(2-hydroxyglycine) + Dehydroascorbic acid + Water details
Peptidylamidoglycolate → peptidyl amide + Glyoxylic acid details
GO Classification
Biological Process
cellular protein modification process
response to drug
heart development
limb development
peptide metabolic process
response to pH
response to glucocorticoid stimulus
response to estradiol stimulus
response to hypoxia
response to copper ion
central nervous system development
Cellular Component
perikaryon
secretory granule
extracellular region
integral to membrane
Component
membrane
cell part
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
monooxygenase activity
oxidoreductase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
peptidylglycine monooxygenase activity
copper ion binding
Molecular Function
L-ascorbic acid binding
peptidylamidoglycolate lyase activity
peptidylglycine monooxygenase activity
copper ion binding
Process
metabolic process
cellular process
cellular metabolic process
peptide metabolic process
oxidation reduction
Cellular Location
  1. Isoform 4:Secreted
Gene Properties
Chromosome Location 5
Locus 5q14-q21
SNPs PAM
Gene Sequence
>2922 bp
ATGGCTGGCCGCGTCCCTAGCCTGCTAGTTCTCCTTGTTTTTCCAAGCAGCTGTTTGGCT
TTCCGAAGCCCACTTTCTGTCTTTAAGAGGTTTAAAGAAACTACCAGACCATTTTCCAAT
GAATGTCTTGGTACCACCAGACCCGTAGTTCCTATTGATTCATCAGATTTTGCATTGGAT
ATTCGCATGCCTGGGGTTACACCTAAACAGTCCGATACATACTTCTGCATGTCTATGCGA
ATACCAGTGGATGAGGAAGCCTTCGTGATTGACTTCAAGCCTCGAGCCAGCATGGATACT
GTCCATCACATGTTACTTTTTGGATGCAATATGCCTTCATCCACTGGAAGTTACTGGTTT
TGTGATGAAGGAACCTGTACAGATAAAGCCAATATTCTGTATGCCTGGGCGAGAAATGCT
CCCCCTACCCGGCTCCCCAAAGGTGTTGGATTCAGAGTTGGAGGAGAGACTGGAAGTAAA
TACTTTGTACTACAGGTACACTATGGGGATATTAGTGCTTTTAGAGATAATAACAAGGAC
TGTTCTGGTGTGTCCTTACACCTCACACGTCTGCCACAGCCTTTAATTGCTGGCATGTAC
CTTATGATGTCTGTTGACACTGTTATCCCAGCAGGAGAAAAAGTGGTGAATTCTGACATT
TCATGCCATTATAAAAATTATCCAATGCATGTCTTTGCCTATAGAGTTCACACTCACCAT
TTAGGTAAGGTAGTAAGTGGATACAGAGTAAGAAATGGACAGTGGACACTGATTGGACGG
CAGAGCCCTCAGCTGCCACAGGCTTTCTACCCTGTGGGGCATCCAGTTGATGTAAGTTTT
GGTGACCTACTGGCTGCAAGATGTGTATTCACTGGTGAAGGAAGGACAGAAGCCACACAC
ATTGGTGGCACGTCTAGTGATGAAATGTGCAACTTATACATTATGTATTACATGGAAGCC
AAGCATGCAGTTTCTTTCATGACCTGTACCCAGAATGTAGCTCCAGATATGTTCAGAACC
ATACCACCAGAGGCCAACATTCCAATTCCCGTGAAGTCTGATATGGTTATGATGCATGAA
CATCATAAAGAAACAGAATATAAAGATAAGATTCCTTTACTACAGCAGCCAAAACGAGAA
GAAGAAGAAGTGTTAGACCAGGGTGATTTCTATTCACTACTTTCCAAGCTGCTAGGAGAA
AGGGAAGATGTTGTTCATGTGCACAAATATAATCCTACAGAAAAGGCAGAATCAGAGTCA
GACCTGGTAGCTGAGATTGCAAATGTAGTCCAAAAAAAGGATCTTGGTCGATCTGATGCC
AGAGAGGGTGCAGAACATGAGAGGGGTAATGCTATTCTTGTCAGAGACAGAATTCACAAA
TTCCACAGACTAGTATCTACCTTGAGGCCACCAGAGAGCAGAGTTTTCTCATTACAGCAG
CCCCCACCTGGTGAAGGCACCTGGGAACCAGAACACACAGGAGATTTCCACATGGAAGAG
GCACTGGATTGGCCTGGAGTATACTTGTTACCAGGCCAGGTTTCTGGGGTGGCTCTAGAC
CCTAAGAATAACCTGGTGATTTTCCACAGAGGTGACCATGTCTGGGATGGAAACTCGTTT
GACAGCAAGTTTGTTTACCAGCAAATAGGACTCGGACCAATTGAAGAAGACACTATTCTT
GTCATAGATCCAAATAATGCTGCAGTACTCCAGTCCAGTGGAAAAAATCTGTTTTACTTG
CCACATGGCTTGAGTATAGATAAAGATGGGAATTATTGGGTCACAGACGTGGCTCTCCAT
CAGGTGTTCAAACTGGATCCAAACAATAAAGAAGGCCCTGTATTAATCCTGGGAAGGAGC
ATGCAACCAGGCAGTGACCAGAATCACTTCTGTCAACCCACTGATGTGGCTGTGGATCCA
GGCACTGGAGCCATTTATGTATCAGATGGTTACTGCAACAGCAGGATTGTGCAGTTTTCA
CCAAGTGGAAAGTTCATCACACAGTGGGGAGAAGAGTCTTCAGGGAGCAGTCCTCTGCCA
GGCCAGTTCACTGTTCCTCACAGCTTGGCTCTTGTGCCTCTTTTGGGCCAATTATGTGTG
GCAGACCGGGAAAATGGTCGGATCCAGTGTTTTAAAACTGACACCAAAGAATTTGTGAGA
GAGATTAAGCATTCATCATTTGGAAGAAATGTATTTGCAATTTCATATATACCAGGCTTG
CTCTTTGCAGTGAATGGGAAGCCTCATTTTGGGGACCAAGAACCTGTACAAGGATTTGTG
ATGAACTTTTCCAATGGGGAAATTATCGACATCTTCAAGCCAGTGCGCAAGCACTTTGAT
ATGCCTCATGATATTGTTGCATCTGAAGATGGGACTGTGTACATTGGAGATGCTCATACC
AACACCGTGTGGAAGTTCACCTTGACTGAGAAATTGGAACATCGATCAGTTAAAAAGGCT
GGCATTGAGGTCCAGGAAATCAAAGAAGCCGAGGCAGTTGTTGAAACCAAAATGGAGAAC
AAACCCACCTCCTCAGAATTGCAGAAGATGCAAGAGAAACAGAAACTGATCAAAGAGCCA
GGCTCGGGAGTGCCTGTTGTTCTCATTACAACCCTTCTGGTTATTCCGGTGGTTGTCCTG
CTGGCCATTGCCATATTTATTCGGTGGAAAAAATCAAGGGCCTTTGGAGATTCTGAACAC
AAACTCGAGACGAGTTCAGGAAGAGTACTGGGAAGATTTAGAGGAAAGGGAAGTGGAGGC
TTAAACCTTGGTAATTTCTTTGCAAGCCGTAAGGGCTACAGTCGAAAAGGGTTTGACCGG
CTTAGCACTGAGGGCAGTGACCAAGAGAAAGAGGATGATGGAAGTGAATCAGAAGAGGAG
TATTCAGCACCTCTGCCTGCGCTCGCACCTTCCTCCTCCTGA
Protein Properties
Number of Residues 973
Molecular Weight 108402.425
Theoretical pI 6.424
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Peptidyl-glycine alpha-amidating monooxygenase
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALD
IRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWF
CDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKD
CSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATH
IGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHE
HHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESES
DLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQ
PPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSF
DSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALH
QVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFS
PSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVR
EIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFD
MPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMEN
KPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEH
KLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEE
YSAPLPALAPSSS
GenBank ID Protein 24430388
UniProtKB/Swiss-Prot ID P19021
UniProtKB/Swiss-Prot Entry Name AMD_HUMAN
PDB IDs Not Available
GenBank Gene ID AB095007
GeneCard ID PAM
GenAtlas ID PAM
HGNC ID HGNC:8596
References
General References
  1. 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:14702039 ]
  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:15489334 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  5. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed:15372022 ]
  6. Glauder J, Ragg H, Rauch J, Engels JW: Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. Biochem Biophys Res Commun. 1990 Jun 15;169(2):551-8. [PubMed:2357221 ]
  7. Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y: Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):282-90. [PubMed:7999037 ]
  8. Satani M, Takahashi K, Sakamoto H, Harada S, Kaida Y, Noguchi M: Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase. Protein Expr Purif. 2003 Apr;28(2):293-302. [PubMed:12699694 ]
  9. Yun HY, Keutmann HT, Eipper BA: Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1994 Apr 8;269(14):10946-55. [PubMed:8144680 ]