| Tag | Content |
|---|
| CPLM ID | CPLM-021072 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Endoplasmic reticulum aminopeptidase 1 |
Protein Synonyms/Alias | ARTS-1; Adipocyte-derived leucine aminopeptidase; A-LAP; Aminopeptidase PILS; Puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; VEGF-induced aminopeptidase |
Gene Name | Erap1 |
Gene Synonyms/Alias | Appils; Arts1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 888 | KGFFSSLKENGSQLR | ubiquitination | [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 | Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney (By similarity). |
Sequence Annotation | REGION 306 310 Substrate binding (By similarity).
ACT_SITE 343 343 By similarity.
METAL 342 342 Zinc; catalytic (By similarity).
METAL 346 346 Zinc; catalytic (By similarity).
METAL 365 365 Zinc; catalytic (By similarity).
BINDING 172 172 Substrate (By similarity).
CARBOHYD 59 59 N-linked (GlcNAc...) (Potential).
CARBOHYD 143 143 N-linked (GlcNAc...) (Potential).
CARBOHYD 403 403 N-linked (GlcNAc...) (Potential).
CARBOHYD 655 655 N-linked (GlcNAc...) (Potential).
CARBOHYD 749 749 N-linked (GlcNAc...) (Potential).
CARBOHYD 890 890 N-linked (GlcNAc...) (Potential).
DISULFID 393 432 By similarity.
DISULFID 725 732 By similarity. |
Keyword | Adaptive immunity; Aminopeptidase; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 930 AA |
Protein Sequence | MPSLLPLVLT FLSVSSPSWC QNSDIESLKA SNGDSFPWNN MRLPEYMTPI HYDLMIHANL 60
STLTFWGKTE VEIIASRPTS TIIMHSHHLQ ISKATLRRGA GEMLSEEPLK VLEYPAHEQV 120
ALLAAQPLLA GSLYTVIIDY AANLSESFHG FYKSTYRTQE GEMRILAATQ FEPTAARMAF 180
PCFDEPALKA SFSIKIKRDP RHLAISNMPL VKSVNVAEGL IEDHFDITVK MSTYLVAFII 240
SDFKSVSKMT KSGVKVSVYA VPDKINQADY ALDAAVTLLE FYEDYFNIPY PLPKQDLAAI 300
PDFQSGAMEN WGLTTYRESS LLYDKEKSSA SSKLGITMIV SHELAHQWFG NLVTMEWWND 360
LWLNEGFAKF MEFVSVTVTH PELKVEDYFF GKCFNAMEVD ALNSSHPVST PVENPAQIRE 420
MFDDVSYEKG ACILNMLRDY LSADTFKRGI VQYLQKYSYK NTKNEDLWNS MMHICPTDGT 480
QTMDGFCSRS QHSSSTSHWR QEVVDVKTMM NTWTLQKGFP LITITVSGRN VHMKQEHYMK 540
GSERFPETGY LWHVPLTFIT SKSDSVQRFL LKTKTDVLIL PEAVQWIKFN VGMNGYYIVH 600
YADDGWASLS GLLKEAHTTI SSNDRASLIN NAFQLVSIEK LSIEKALDLT LYLKNETEIM 660
PIFQALNELI PMYKLMEKRD MIEVETQFKD FLLKLLKDLI DKQTWTDEGS VSERMLRSQL 720
LLLACVRNYQ PCVQRAERYF REWKSSNGNM SIPIDVTLAV FAVGAQNTEG WDFLYSKYQS 780
SLSSTEKSQI EFSLCTSKDP EKLQWLLDQS FKGEIIKTQE FPHILTLIGR NPVGYPLAWK 840
FLRENWNKLV QKFELGSSSI AHMVMGTTDQ FSTRARLEEV KGFFSSLKEN GSQLRCVQQT 900
IETIEENIRW MDKNFDKIRL WLQKEKPELL 930 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:MGI. GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0005576; C:extracellular region; ISS:UniProtKB. GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0004177; F:aminopeptidase activity; ISS:UniProtKB. GO:0005138; F:interleukin-6 receptor binding; ISS:UniProtKB. GO:0008235; F:metalloexopeptidase activity; ISS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB. GO:0045766; P:positive regulation of angiogenesis; IMP:MGI. GO:0009617; P:response to bacterium; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |