Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX.
Function:
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.
Subcellular Location:
Endoplasmic reticulum membrane
Single-pass type II membrane protein
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANT PRO-127
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
"Molecular characterization of human aminopeptidase PILS." Schomburg L.
Submitted (1999-09) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANTS ASP-346; ARG-528 AND GLU-730
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: FUNCTION;SUBCELLULAR LOCATION;SUBUNIT;INDUCTION BY IFNG
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Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-414
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
15.
"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1." Structural genomics consortium (SGC)
Submitted (2010-05) to the PDB data bank
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Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-940 IN COMPLEX WITH ZINC IONS;DISULFIDE BONDS;GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-414
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Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINC IONS AND BESTATIN;FUNCTION;DISULFIDE BONDS;GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-760;ACTIVE SITE;CATALYTIC ACTIVITY;SUBUNIT;MUTAGENESIS OF TYR-438
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