CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004726
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93EAFVIDFKPRASMDTubiquitination[1, 2]
409EDVVHVHKYNPTEKAubiquitination[1]
415HKYNPTEKAESESDLubiquitination[1]
432EIANVVQKKDLGRSDubiquitination[1]
610FKLDPNNKEGPVLILubiquitination[1]
716QCFKTDTKEFVREIKubiquitination[1]
819LEHRSVKKAGIEVQEubiquitination[1]
901AFGDSEHKLETSSGRubiquitination[1]
916VLGRFRGKGSGGLNLubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
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. 
Sequence Annotation
 REPEAT 498 541 NHL 1.
 REPEAT 567 608 NHL 2.
 REPEAT 617 662 NHL 3.
 REPEAT 670 714 NHL 4.
 REPEAT 766 809 NHL 5.
 REGION 1 494 Peptidylglycine alpha-hydroxylating
 REGION 495 817 Peptidyl-alpha-hydroxyglycine alpha-
 REGION 925 942 Interaction with RASSF9 (By similarity).
 METAL 102 102 Copper A (By similarity).
 METAL 103 103 Copper A (By similarity).
 METAL 167 167 Copper A (By similarity).
 METAL 237 237 Copper B (By similarity).
 METAL 239 239 Copper B (By similarity).
 METAL 309 309 Copper B (By similarity).
 MOD_RES 918 918 Phosphoserine (By similarity).
 MOD_RES 929 929 Phosphoserine.
 MOD_RES 942 942 Phosphoserine.
 MOD_RES 943 943 Phosphothreonine.
 MOD_RES 946 946 Phosphoserine; by UHMK1; in vitro.
 MOD_RES 961 961 Sulfotyrosine.
 CARBOHYD 762 762 N-linked (GlcNAc...) (Potential).
 DISULFID 42 181 By similarity.
 DISULFID 76 121 By similarity.
 DISULFID 109 126 By similarity.
 DISULFID 222 329 By similarity.
 DISULFID 288 310 By similarity.
 DISULFID 631 652 By similarity.
 DISULFID 699 710 By similarity.  
Keyword
 Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Copper; Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal; Sulfation; Transmembrane; Transmembrane helix; Vitamin C; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 973 AA 
Protein Sequence
MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 60
IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 120
CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 180
CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 240
LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 300
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 360
HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 420
DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 480
PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 540
DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 600
QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 660
PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 720
EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 780
MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 840
KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH 900
KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK EDDGSESEEE 960
YSAPLPALAP SSS 973 
Gene Ontology
 GO:0009986; C:cell surface; IEA:Compara.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0043204; C:perikaryon; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0030141; C:secretory granule; NAS:UniProtKB.
 GO:0030667; C:secretory granule membrane; IEA:Compara.
 GO:0005802; C:trans-Golgi network; IEA:Compara.
 GO:0005509; F:calcium ion binding; IEA:Compara.
 GO:0005507; F:copper ion binding; IEA:Compara.
 GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
 GO:0004598; F:peptidylamidoglycolate lyase activity; IEA:EC.
 GO:0004504; F:peptidylglycine monooxygenase activity; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0006464; P:cellular protein modification process; TAS:ProtInc.
 GO:0007417; P:central nervous system development; IEA:Compara.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0060173; P:limb development; IEA:Compara.
 GO:0001676; P:long-chain fatty acid metabolic process; IEA:Compara.
 GO:0060135; P:maternal process involved in female pregnancy; IEA:Compara.
 GO:0042476; P:odontogenesis; IEA:Compara.
 GO:0022602; P:ovulation cycle process; IEA:Compara.
 GO:0001519; P:peptide amidation; IEA:Compara.
 GO:0006518; P:peptide metabolic process; NAS:UniProtKB.
 GO:0018032; P:protein amidation; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Compara.
 GO:0050708; P:regulation of protein secretion; IEA:Compara.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0046688; P:response to copper ion; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0032355; P:response to estradiol stimulus; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0009268; P:response to pH; IEA:Compara.
 GO:0009404; P:toxin metabolic process; IEA:Compara. 
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.