MGP Database

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MGP005247

UniProt Annotations

Entry Information
Gene Nameendoplasmic reticulum aminopeptidase 1
Protein EntryERAP1_HUMAN
UniProt IDQ9NZ08
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9NZ08-1; Sequence=Displayed; Name=2; IsoId=Q9NZ08-2; Sequence=VSP_005450;
Catalytic ActivityRelease of an N-terminal amino acid, Xaa-|- Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe. {ECO:0000269|PubMed:21478864}.
CautionIt is uncertain whether Met-1 or Met-13 is the initiator. {ECO:0000305}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
FunctionAminopeptidase 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. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:16286653, ECO:0000269|PubMed:21478864}.
InductionBy IFNG/IFN-gamma. {ECO:0000269|PubMed:15908954}.
PtmN-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:21478864, ECO:0000269|Ref.15}.
Sequence CautionSequence=BAA25451.2; Type=Erroneous initiation; Evidence={ECO:0000305};
SimilarityBelongs to the peptidase M1 family. {ECO:0000305}.
Subcellular LocationEndoplasmic reticulum membrane {ECO:0000305|PubMed:15908954}; Single-pass type II membrane protein {ECO:0000305|PubMed:15908954}.
SubunitMonomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX. {ECO:0000269|PubMed:15908954, ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:21478864, ECO:0000269|Ref.15}.
Tissue SpecificityUbiquitous.
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