Tag | Content |
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CPLM ID | CPLM-010645 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aminopeptidase N |
Protein Synonyms/Alias | AP-N; mAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Membrane protein p161; Microsomal aminopeptidase; CD13 |
Gene Name | Anpep |
Gene Synonyms/Alias | Lap-1; Lap1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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496 | FLTEDLFKKGLSSYL | acetylation | [1] |
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Reference | [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching. Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE. J Proteome Res. 2011 Sep 2;10(9):4134-49. [ PMID: 21728379] |
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. May have a role in angiogenesis (By similarity). Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells. |
Sequence Annotation | REGION 33 68 Cytosolic Ser/Thr-rich junction. REGION 69 966 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 418 418 Sulfotyrosine (Potential). MOD_RES 423 423 Sulfotyrosine (Potential). MOD_RES 852 852 Phosphotyrosine. CARBOHYD 106 106 N-linked (GlcNAc...). CARBOHYD 114 114 N-linked (GlcNAc...). CARBOHYD 128 128 N-linked (GlcNAc...). CARBOHYD 234 234 N-linked (GlcNAc...) (Potential). CARBOHYD 288 288 N-linked (GlcNAc...) (Potential). CARBOHYD 318 318 N-linked (GlcNAc...) (Potential). CARBOHYD 332 332 N-linked (GlcNAc...). CARBOHYD 573 573 N-linked (GlcNAc...) (Potential). CARBOHYD 606 606 N-linked (GlcNAc...). CARBOHYD 624 624 N-linked (GlcNAc...) (Potential). CARBOHYD 666 666 N-linked (GlcNAc...); atypical. CARBOHYD 734 734 N-linked (GlcNAc...) (Potential). CARBOHYD 783 783 N-linked (GlcNAc...); atypical. CARBOHYD 784 784 N-linked (GlcNAc...). CARBOHYD 785 785 N-linked (GlcNAc...); atypical. CARBOHYD 790 790 N-linked (GlcNAc...); atypical. CARBOHYD 817 817 N-linked (GlcNAc...). 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 | 966 AA |
Protein Sequence | MAKGFYISKT LGILGILLGV AAVCTIIALS VVYAQEKNRN AENSATAPTL PGSTSATTAT 60 TTPAVDESKP WNQYRLPKTL IPDSYRVILR PYLTPNNQGL YIFQGNSTVR FTCNQTTDVI 120 IIHSKKLNYT LKGNHRVVLR TLDGTPAPNI DKTELVERTE YLVVHLQGSL VEGRQYEMDS 180 QFQGELADDL AGFYRSEYME GDVKKVVATT QMQAADARKS FPCFDEPAMK AMFNITLIYP 240 NNLIALSNML PKESKPYPED PSCTMTEFHS TPKMSTYLLA YIVSEFKNIS SVSANGVQIG 300 IWARPSAIDE GQGDYALNVT GPILNFFAQH YNTSYPLPKS DQIALPDFNA GAMENWGLVT 360 YRESSLVFDS QSSSISNKER VVTVIAHELA HQWFGNLVTV AWWNDLWLNE GFASYVEYLG 420 ADYAEPTWNL KDLMVLNDVY RVMAVDALAS SHPLSSPADE IKTPDQIMEL FDSITYSKGA 480 SVIRMLSSFL TEDLFKKGLS SYLHTYQYSN TVYLDLWEHL QKAVNQQTAV QPPATVRTIM 540 DRWILQMGFP VITVNTNTGE ISQKHFLLDS KSNVTRPSEF NYIWIAPIPF LKSGQEDHYW 600 LDVEKNQSAK FQTSSNEWIL LNINVTGYYL VNYDENNWKK LQNQLQTDLS VIPVINRAQI 660 IHDSFNLASA KMIPITLALD NTLFLVKEAE YMPWQAALSS LNYFTLMFDR SEVYGPMKRY 720 LKKQVTPLFF YFQNRTNNWV NRPPTLMEQY NEINAISTAC SSGLKECRDL VVELYSQWMK 780 NPNNNTIHPN LRSTVYCNAI AFGGEEEWNF AWEQFRNATL VNEADKLRSA LACSKDVWIL 840 NRYLSYTLNP DYIRKQDTTS TIISIASNVA GHPLVWDFVR SNWKKLFENY GGGSFSFANL 900 IQGVTRRFSS EFELQQLEQF KADNSATGFG TGTRALEQAL EKTRANIDWV KENKDAVFKW 960 FTENSS 966 |
Gene Ontology | GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Compara. GO:0009897; C:external side of plasma membrane; IDA:MGI. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
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