Tag | Content |
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CPLM ID | CPLM-004363 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aminopeptidase N |
Protein Synonyms/Alias | AP-N; rAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Kidney Zn peptidase; KZP; Microsomal aminopeptidase; CD13 |
Gene Name | Anpep |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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826 | TLVNEADKLRSALAC | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). |
Sequence Annotation | REGION 33 68 Cytosolic Ser/Thr-rich junction. REGION 69 965 Metalloprotease. REGION 351 355 Substrate binding (By similarity). ACT_SITE 388 388 Proton acceptor (By similarity). METAL 387 387 Zinc; catalytic (By similarity). METAL 391 391 Zinc; catalytic (By similarity). METAL 410 410 Zinc; catalytic (By similarity). MOD_RES 176 176 Sulfotyrosine (Potential). MOD_RES 852 852 Phosphotyrosine (By similarity). CARBOHYD 114 114 N-linked (GlcNAc...) (Potential). CARBOHYD 128 128 N-linked (GlcNAc...) (Potential). CARBOHYD 234 234 N-linked (GlcNAc...) (Potential). CARBOHYD 242 242 N-linked (GlcNAc...) (Potential). CARBOHYD 264 264 N-linked (GlcNAc...) (Potential). CARBOHYD 555 555 N-linked (GlcNAc...) (Potential). CARBOHYD 606 606 N-linked (GlcNAc...) (Potential). CARBOHYD 624 624 N-linked (GlcNAc...) (Potential). CARBOHYD 780 780 N-linked (GlcNAc...) (Potential). DISULFID 760 767 By similarity. DISULFID 797 833 By similarity. |
Keyword | Aminopeptidase; Angiogenesis; Complete proteome; Developmental protein; Differentiation; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; Signal-anchor; Sulfation; Transmembrane; Transmembrane helix; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 965 AA |
Protein Sequence | MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSAIAPTL PGSTSATTST 60 TNPAIDESKP WNQYRLPKTL IPDSYQVTLR PYLTPNEQGL YIFKGSSTVR FTCNETTNVI 120 IIHSKKLNYT NKGNHRVALR ALGDTPAPNI DTTELVERTE YLVVHLQGSL VKGHQYEMDS 180 EFQGELADDL AGFYRSEYME GGNKKVVATT QMQAADARKS FPCFDEPAMK ASFNITLIHP 240 NNLTALSNML PKDSRTLQED PSWNVTEFHP TPKMSTYLLA YIVSEFKYVE AVSPNRVQIR 300 IWARPSAIDE GHGDYALQVT GPILNFFAQH YNTAYPLEKS DQIALPDFNA GAMENWGLVT 360 YRESALVFDP QSSSISNKER VVTVIAHELA HQWFGNLVTV DWWNDLWLNE GFASYVEFLG 420 ADYAEPTWNL KDLIVLNDVY RVMAVDALAS SHPLSSPANE VNTPAQISEL FDSITYSKGA 480 SVLRMLSSFL TEDLFKKGLS SYLHTFQYSN TIYLDLWEHL QQAVDSQTAI KLPASVSTIM 540 DRWILQMGFP VITVNTSTGE IYQEHFLLDP TSKPTRPSDF NYLWIVPIPY LKNGKEDHYW 600 LETEKNQSAE FQTSSNEWLL LNINVTGYYQ VNYDENNWRK IQNQLQTDLS VIPVINRAQI 660 IHDSFNLASA GKLSITLPLS NTLFLASETE YMPWEAALSS LNYFKLMFDR SEVYGPMKRY 720 LKKQVTPLFA YFKIKTNNWL DRPPTLMEQY NEINAISTAC SSGLEECRDL VVGLYSQWMN 780 NSDNNPIHPN LRSTVYCNAI AFGGEEEWNF AWEQFRKATL VNEADKLRSA LACSNEVWIL 840 NRYLSYTLNP DYIRKQDATS TIVSIANNVV GQTLVWDFVR SNWKKLFEDY GGGSFSFANL 900 IQGVTRRFSS EFELQQLEQF KEDNSATGFG SGTRALEQAL EKTKANIKWV KENKDVVLKW 960 FTENS 965 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0031983; C:vesicle lumen; IDA:RGD. GO:0012506; C:vesicle membrane; IDA:RGD. GO:0004177; F:aminopeptidase activity; IDA:RGD. GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. GO:0042277; F:peptide binding; IDA:RGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. GO:0006725; P:cellular aromatic compound metabolic process; IDA:RGD. GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD. GO:0006508; P:proteolysis; IDA:RGD. |
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PROSITE | |
PRINTS | |