CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010650
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Peptidyl-glycine alpha-amidating monooxygenase 
Protein Synonyms/Alias
 PAM; Peptidylglycine alpha-hydroxylating monooxygenase; PHM; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidylamidoglycolate lyase; PAL 
Gene Name
 Pam 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
922VLGRLRGKGSSGLNLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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 (By similarity). 
Sequence Annotation
 REPEAT 501 544 NHL 1.
 REPEAT 570 611 NHL 2.
 REPEAT 620 665 NHL 3.
 REPEAT 673 717 NHL 4.
 REPEAT 769 812 NHL 5.
 REGION 1 497 Peptidylglycine alpha-hydroxylating
 REGION 498 823 Peptidyl-alpha-hydroxyglycine alpha-
 REGION 931 948 Interaction with RASSF9 (By similarity).
 METAL 106 106 Copper A (By similarity).
 METAL 107 107 Copper A (By similarity).
 METAL 171 171 Copper A (By similarity).
 METAL 241 241 Copper B (By similarity).
 METAL 243 243 Copper B (By similarity).
 METAL 313 313 Copper B (By similarity).
 MOD_RES 924 924 Phosphoserine.
 MOD_RES 925 925 Phosphoserine.
 MOD_RES 935 935 Phosphoserine (By similarity).
 MOD_RES 948 948 Phosphoserine.
 MOD_RES 949 949 Phosphothreonine (By similarity).
 MOD_RES 952 952 Phosphoserine; by UHMK1.
 CARBOHYD 765 765 N-linked (GlcNAc...) (Potential).
 DISULFID 46 185 By similarity.
 DISULFID 80 125 By similarity.
 DISULFID 113 130 By similarity.
 DISULFID 226 333 By similarity.
 DISULFID 292 314 By similarity.
 DISULFID 634 655 By similarity.
 DISULFID 702 713 By similarity.  
Keyword
 Cleavage on pair of basic residues; Complete proteome; Copper; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Vitamin C; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 979 AA 
Protein Sequence
MAGRARSRLL LLLGLLALQS SCLAFRSPLS VFKRFKETTR SFSNECLGTT RPITPIDSSD 60
FTLDIRMPGV TPKESDTYFC MSMRLPVDEE AFVIDFKPRA SMDTVHHMLL FGCNMPSSTG 120
SYWFCDEGTC TDKANILYAW ARNAPPTRLP KGVGFRVGGE TGSKYFVLQV HYGDISAFRD 180
NHKDCSGVSL HLTRVPQPLI AGMYLMMSVN TVIPPGEKVV NSDISCHYKM YPMHVFAYRV 240
HTHHLGKVVS GYRVRNGQWT LIGRQSPQLP QAFYPVEHPV DVAFGDILAA RCVFTGEGRT 300
EATHIGGTSS DEMCNLYIMY YMEAKHAVSF MTCTQNVAPD MFRTIPEEAN IPIPVKSDMV 360
MIHGHHKETE NKEKSALIQQ PKQGEEEAFE QGDFYSLLSK LLGEREDVVH VHKYNPTEKT 420
ESGSDLVAEI ANVVQKKDLG RSDAREGAEH EEGGNAILVR DRIHKFHRLE STLRPAESRA 480
LSFQQPGEGP WEPELAGDFH VEEALEWPGV YLLPGQVSGV ALDSKNNLVI FHRGDHVWDG 540
NSFDSKFVYQ QRGLGPIEED TILVIDPNKA EILQSSGKNL FYLPHGLSID TDGNYWVTDV 600
ALHQVFKLEP RSKEGPLLVL GRSMQPGSDQ NHFCQPTDVA VEPSTGAVFV SDGYCNSRIV 660
QFSPSGKFIT QWGEESSGSS PKPGQFSVPH SLALVPHLNQ LCVADRENGR IQCFKTDTKE 720
FVREIKHASF GRNVFAISYI PGFLFAVNGK PYFGDQEPVQ GFVMNFSSGE IIDVFKPVRK 780
HFDMPHDIVA SEDGTVYIGD AHTNTVWKFT LTESRLEVEH RSVKKAGIEV PEIKEAEAVV 840
EPKVKNKPTS SELQKMQEKK KLIKDPGSGV PVVLITTLLV IPVVVLLAIA MFIRWKKSRA 900
FGDHDRKLES SSGRVLGRLR GKGSSGLNLG NFFASRKGYS RKGFDRVSTE GSDQEKDEDD 960
GSESEEEYSA PLPTPAPSS 979 
Gene Ontology
 GO:0005829; C:cytosol; TAS:MGI.
 GO:0005887; C:integral to plasma membrane; TAS:MGI.
 GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005507; F:copper ion binding; IEA:InterPro.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:EC.
 GO:0004504; F:peptidylglycine monooxygenase activity; TAS:MGI.
 GO:0006518; P:peptide metabolic process; TAS:MGI. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR014784; Cu2_ascorb_mOase-like_C.
 IPR020611; Cu2_ascorb_mOase_CS-1.
 IPR014783; Cu2_ascorb_mOase_CS-2.
 IPR000323; Cu2_ascorb_mOase_N.
 IPR001258; NHL_repeat.
 IPR013017; NHL_repeat_subgr.
 IPR000720; Pep_amidat_mOase.
 IPR008977; PHM/PNGase_F_dom. 
Pfam
 PF01082; Cu2_monooxygen
 PF01436; NHL 
SMART
  
PROSITE
 PS00084; CU2_MONOOXYGENASE_1
 PS00085; CU2_MONOOXYGENASE_2
 PS51125; NHL 
PRINTS
 PR00790; PAMONOXGNASE.