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UniProtKB/Swiss-Prot entry P19021


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AMD_HUMAN
Primary accession number P19021
Secondary accession numbers A8K293 O95080 Q16252 Q16253 Q54A45 Q86U53 Q8WVC7 Q9UCG0
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on September 19, 2002 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 107)
Name and origin of the protein
Protein name Peptidyl-glycine alpha-amidating monooxygenase [Precursor]
Synonym PAM
Includes Peptidylglycine alpha-hydroxylating monooxygenase
     (PHM)
     (EC 1.14.17.3)
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
     (EC 4.3.2.5)
     (Peptidylamidoglycolate lyase)
     (PAL)
Gene name
Name: PAM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thyroid carcinoma;
DOI=10.1016/0006-291X(90)90366-U; PubMed=2357221 [NCBI, ExPASy, EBI, Israel, Japan]
Glauder J., Ragg H., Rauch J., Engels J.W.;
"Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells.";
Biochem. Biophys. Res. Commun. 169:551-558(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
DOI=10.1006/bbrc.1994.2662; PubMed=7999037 [NCBI, ExPASy, EBI, Israel, Japan]
Tateishi K., Arakawa F., Misumi Y., Treston A.M., Vos M., Matsuoka Y.;
"Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase.";
Biochem. Biophys. Res. Commun. 205:282-290(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), COFACTOR, AND ENZYME REGULATION.
TISSUE=Heart;
DOI=10.1016/S1046-5928(02)00684-8; PubMed=12699694 [NCBI, ExPASy, EBI, Israel, Japan]
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. 28:293-302(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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 T.-O., 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. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-973 (ISOFORM 4).
TISSUE=Kidney;
Chung B.H., Oh G.H., Choi E.S.;
"The alpha-amidating monooxygenase gene of human kidney.";
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[9]
SULFATION AT TYR-961.
PubMed=8144680 [NCBI, ExPASy, EBI, Israel, Japan]
Yun H.Y., Keutmann H.T., Eipper B.A.;
"Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase.";
J. Biol. Chem. 269:10946-10955(1994).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-955 AND SER-957, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-929, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M37721; AAA36414.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S75037; AAB32775.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S75038; AAB32776.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB095007; BAC22594.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290158; BAF82847.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007419; AAP36087.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471086; EAW49085.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018127; AAH18127.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF010472; AAD01439.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A35477; URHUAP.
RefSeq NP_000910.2; -.
NP_620121.1; -.
NP_620176.1; -.
NP_620177.1; -.
UniGene Hs.369430
3D structure databases
HSSP P14925; 1PHM. [HSSP ENTRY / PDB]
SMR P19021; 40-351.
ModBase P19021.
PTM databases
PhosphoSite P19021; -.
Organism-specific databases
GeneCards GC05P102229; -.
H-InvDB HIX0021107; -.
HGNC HGNC:8596; PAM.
GenAtlas PAM.
MIM 170270; gene. [NCBI / EBI]
PharmGKB PA134983031; -.
GeneCards P19021.
Gene expression databases
ArrayExpress P19021; -.
CleanEx HS_PAM; -.
GermOnline ENSG00000145730; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030141; Cellular component: secretory granule (non-traceable author statement from UniProtKB).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0031418; Molecular function: L-ascorbic acid binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004598; Molecular function: peptidylamidoglycolate lyase activity (inferred from electronic annotation from EC).
GO:0004504; Molecular function: peptidylglycine monooxygenase activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006518; Biological process: peptide metabolic process (non-traceable author statement from UniProtKB).
GO:0006464; Biological process: protein modification process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR011042; 6-blade_b-propeller_TolB-like.
IPR014783; Cu2_ascorb_mOase_C.
IPR000323; Cu2_ascorb_mOase_N.
IPR001258; NHL_repeat.
IPR013017; NHL_repeat_subgr.
IPR000720; Pep_amidat_mOase.
Graphical view of domain structure.
Gene3D G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
Pfam PF03712; Cu2_monoox_C; 1.
PF01082; Cu2_monooxygen; 1.
PF01436; NHL; 4.
Pfam graphical view of domain structure.
PRINTS PR00790; PAMONOXGNASE.
PROSITE PS00084; CU2_MONOOXYGENASE_1; 1.
PS00085; CU2_MONOOXYGENASE_2; 1.
PS51125; NHL; 5.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000145730; Homo sapiens. [Contig view]
GeneID 5066; -.
KEGG hsa:5066; -.
Phylogenomic databases
HOVERGEN P19021; -.
Other
DrugBank DB00126; Vitamin C.
LinkHub P19021; -.
NextBio 19512; -.
SOURCE PAM; Homo sapiens.
ProtoNet P19021.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cleavage on pair of basic residues; Copper; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Phosphoprotein; Repeat; Secreted; Signal; Sulfation; Transmembrane; Vitamin C; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Probable. 
PROPEP   21    30  10     Probable. PRO_0000006361
CHAIN   31   973  943     Peptidyl-glycine alpha-amidating monooxygenase. PRO_0000006362
TOPO_DOM   31   863  833     Intragranular (Potential). 
TRANSMEM   864   887  24     Potential. 
TOPO_DOM   888   973  86     Cytoplasmic (Potential). 
REPEAT   498   541  44     NHL 1. 
REPEAT   567   608  42     NHL 2. 
REPEAT   617   662  46     NHL 3. 
REPEAT   670   714  45     NHL 4. 
REPEAT   766   809  44     NHL 5. 
REGION   1   494  494     Peptidylglycine alpha-hydroxylating monooxygenase (By similarity). 
REGION   495   817  323     Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (By similarity). 
REGION   925   942  18     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   955   955        Phosphoserine. 
MOD_RES   957   957        Phosphoserine. 
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. 
VAR_SEQ   388   494        Missing (in isoform 2). VSP_001227
VAR_SEQ   829   914        Missing (in isoform 4). VSP_001229
VAR_SEQ   829   896        Missing (in isoform 3). VSP_001228
CONFLICT   26    26        S -> P (in Ref. 4; BAF82847). 
CONFLICT   574   574        G -> E (in Ref. 1; AAA36414). 
CONFLICT   774   774        P -> L (in Ref. 4; BAF82847). 
CONFLICT   830   831        Missing (in Ref. 2; AAB32775). 
CONFLICT   896   896        G -> GA (in Ref. 1; AAA36414). 
Sequence information
Length: 973 AA [This is the length of the unprocessed precursor] Molecular weight: 108332 Da [This is the MW of the unprocessed precursor] CRC64: 8A089B657F56EE39 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGRVPSLLV LLVFPSSCLA FRSPLSVFKR FKETTRPFSN ECLGTTRPVV PIDSSDFALD 

        70         80         90        100        110        120 
IRMPGVTPKQ SDTYFCMSMR IPVDEEAFVI DFKPRASMDT VHHMLLFGCN MPSSTGSYWF 

       130        140        150        160        170        180 
CDEGTCTDKA NILYAWARNA PPTRLPKGVG FRVGGETGSK YFVLQVHYGD ISAFRDNNKD 

       190        200        210        220        230        240 
CSGVSLHLTR LPQPLIAGMY LMMSVDTVIP AGEKVVNSDI SCHYKNYPMH VFAYRVHTHH 

       250        260        270        280        290        300 
LGKVVSGYRV RNGQWTLIGR QSPQLPQAFY PVGHPVDVSF GDLLAARCVF TGEGRTEATH 

       310        320        330        340        350        360 
IGGTSSDEMC NLYIMYYMEA KHAVSFMTCT QNVAPDMFRT IPPEANIPIP VKSDMVMMHE 

       370        380        390        400        410        420 
HHKETEYKDK IPLLQQPKRE EEEVLDQGDF YSLLSKLLGE REDVVHVHKY NPTEKAESES 

       430        440        450        460        470        480 
DLVAEIANVV QKKDLGRSDA REGAEHERGN AILVRDRIHK FHRLVSTLRP PESRVFSLQQ 

       490        500        510        520        530        540 
PPPGEGTWEP EHTGDFHMEE ALDWPGVYLL PGQVSGVALD PKNNLVIFHR GDHVWDGNSF 

       550        560        570        580        590        600 
DSKFVYQQIG LGPIEEDTIL VIDPNNAAVL QSSGKNLFYL PHGLSIDKDG NYWVTDVALH 

       610        620        630        640        650        660 
QVFKLDPNNK EGPVLILGRS MQPGSDQNHF CQPTDVAVDP GTGAIYVSDG YCNSRIVQFS 

       670        680        690        700        710        720 
PSGKFITQWG EESSGSSPLP GQFTVPHSLA LVPLLGQLCV ADRENGRIQC FKTDTKEFVR 

       730        740        750        760        770        780 
EIKHSSFGRN VFAISYIPGL LFAVNGKPHF GDQEPVQGFV MNFSNGEIID IFKPVRKHFD 

       790        800        810        820        830        840 
MPHDIVASED GTVYIGDAHT NTVWKFTLTE KLEHRSVKKA GIEVQEIKEA EAVVETKMEN 

       850        860        870        880        890        900 
KPTSSELQKM QEKQKLIKEP GSGVPVVLIT TLLVIPVVVL LAIAIFIRWK KSRAFGDSEH 

       910        920        930        940        950        960 
KLETSSGRVL GRFRGKGSGG LNLGNFFASR KGYSRKGFDR LSTEGSDQEK EDDGSESEEE 

       970 
YSAPLPALAP SSS 

P19021 in FASTA format

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