ERAP2_PONAB
ID ERAP2_PONAB Reviewed; 960 AA.
AC Q5RFP3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Endoplasmic reticulum aminopeptidase 2;
DE EC=3.4.11.-;
GN Name=ERAP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Aminopeptidase that plays a central role in peptide trimming,
CC a step required for the generation of most HLA class I-binding
CC peptides. Peptide trimming is essential to customize longer precursor
CC peptides to fit them to the correct length required for presentation on
CC MHC class I molecules. Preferentially hydrolyzes the basic residues Arg
CC and Lys (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer with ERAP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857110; CAH89414.1; -; mRNA.
DR RefSeq; NP_001124597.1; NM_001131125.1.
DR AlphaFoldDB; Q5RFP3; -.
DR SMR; Q5RFP3; -.
DR STRING; 9601.ENSPPYP00000017500; -.
DR MEROPS; M01.024; -.
DR GeneID; 100171433; -.
DR KEGG; pon:100171433; -.
DR CTD; 64167; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; Q5RFP3; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR033528; ERAP2.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF239; PTHR11533:SF239; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Aminopeptidase; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Immunity; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..960
FT /note="Endoplasmic reticulum aminopeptidase 2"
FT /id="PRO_0000315720"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..960
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334..338
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 455
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 421..460
FT /evidence="ECO:0000250"
FT DISULFID 759..766
FT /evidence="ECO:0000250"
SQ SEQUENCE 960 AA; 110256 MW; 09B2CDCBCEA872B6 CRC64;
MLHSSAMVNS HRKSMFNIHK GFYCLAAILP QICICSQFSV PSSYHFSEDP GAFPVATNGE
RFPWQELRLP SVVIPLHYDL FVHPNLTSLD FVASEKIEVL VSNATQFIIL HSKDLEITNA
TLQSEEDSRY MKPGKELKVL SYPAHQQIAL LVPEKLMPHL KYYVAIDFQA KLGDGFEGFY
KSTYRTLGGE TRILAVTDFE PTQARMAFPC FDEPLFKANF SIKIRRESGH IALSNMPKVR
TIELEGGLLE DHFETTVKMS TYLVAYIVCD FHSVSGITSS GVKVSIYASP DKQNQTHYAL
QASLKLLDFY EKYFDIYYPL SKLDLIAIPD FASGAMENWG LITYRETSLL FDPKTSSASD
KLWVTRVIAH ELAHQWFGNL VTMEWWNDIW LKEGFAKYME LIAVNATYPE LQFDDYFLNV
CFEVITKDSL NSSRPISKPA ETPTQIQEMF DEVSYNKGAC ILNMLKDFLG EEKFQKGIIQ
YLKKFSYRNA KNDDLWSSLS NSCLESDFTS GGVCHSDPKM TSNMLTFLGE NAEVKEMMTT
WTLQKGIPLL VVKQDGCSLR LQQERFLQGV FQEDPEWRAL QERYLWHIPL TYSTSSSNVI
HRHILKSKTD TLDLPEKTSW VKFNVDSNGY YIVHYEGHGW DQLITQLNQN HTLLRPKDRV
GLIHDVFQLV GAGRLTLDKA LDMTHYLQHE TSSPALLEGL SYLELFYHMM DRRNISDISE
NLKRYLLQYF KPVIDRQSWS DEGSVWDRML RSALLKLACD LNHAPCIQKA TELFSQWMES
SGKLNIPTDV LKIVYSVGAQ TAAGWNYLLE QYELSMSSAE QNKILYALST SKHQEKLLKL
IELGMEGKVI KTQNLAALLH VIARRPKGQQ LAWDFVRENW THLLKKFDLG SFDIRMIISG
TTARFSSKDK LQEVKLFFES LEAQGSHLDI FQIVLETITK NIKWLEKNLP TLRTWLLVNT
