ERAP2_BOVIN
ID ERAP2_BOVIN Reviewed; 954 AA.
AC A6QPT7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Endoplasmic reticulum aminopeptidase 2;
DE EC=3.4.11.-;
GN Name=ERAP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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}.
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DR EMBL; BC149475; AAI49476.1; -; mRNA.
DR RefSeq; NP_001069096.2; NM_001075628.2.
DR RefSeq; XP_005209817.1; XM_005209760.3.
DR AlphaFoldDB; A6QPT7; -.
DR SMR; A6QPT7; -.
DR STRING; 9913.ENSBTAP00000001164; -.
DR MEROPS; M01.024; -.
DR PaxDb; A6QPT7; -.
DR PRIDE; A6QPT7; -.
DR Ensembl; ENSBTAT00000001164; ENSBTAP00000001164; ENSBTAG00000039275.
DR GeneID; 513572; -.
DR KEGG; bta:513572; -.
DR CTD; 64167; -.
DR VEuPathDB; HostDB:ENSBTAG00000039275; -.
DR VGNC; VGNC:28561; ERAP2.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000162653; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; A6QPT7; -.
DR OrthoDB; 110058at2759; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000039275; Expressed in neutrophil and 108 other tissues.
DR ExpressionAtlas; A6QPT7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
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:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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..954
FT /note="Endoplasmic reticulum aminopeptidase 2"
FT /id="PRO_0000315718"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..954
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 365
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 328..332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 449
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 415..454
FT /evidence="ECO:0000250"
FT DISULFID 753..760
FT /evidence="ECO:0000250"
SQ SEQUENCE 954 AA; 109719 MW; CC9F28CB1EBFBE2F CRC64;
MANSCRKLIF NIYVVFYCSA VIMPQICICS QFTSSPIDQF NKDPKAFPVA TNGEIFPWHE
LRLPTVVIPL HYDLLIHPNL TSLDFVASEK IEVLVRDATQ FIILHSKDLE ILNASLQSEE
DVRYKKPGEN LTVLSYPAHQ QIALLVPEKL RAHLRYSVAI DFQAKLADGF EGFYKSTYRT
LGGETRTIAV TDFEPTEARM AFPCFDEPLF KANFSIKIRR ESRHIALSNM PKVKTIELEG
GLLEDHFETT VRMSTYLVAY IVCDFTSVSG TASSGVKVSI YASPDKWSQT HYALEASVKL
LDFYENYFDI HYPLPKLDLV AIPDFASGAM ENWGLITYRE TSLLFDPKTS STSDKLWVTK
VIAHELAHQW FGNLVTMEWW NDIWLNEGFA RYMELISLNI TYPELQFDDS FSNTCFEVIK
RDSLNSSHPI SNEAKTATQI KEMFDAVSYN KGACILNMLK DFLSEETFRK GIIHYLKKFT
YRNAKNDDLW HSLSNNCLEG DSTSGGFCYS DSRKTSNTLA FLRENVELKE MMATWTLQKG
IPLVVVKREG RSLRLQQERF LSGVFKEDPE WGTLQERYLW HIPVTYSTSS SQAIHRHILK
LKTDTVDLSE KTDWVKFNVD SSGYYIVHYE GQGWDELITL LNQNHTLLRP KDRLGLIHDA
FQLVSAGRLT LDKALDLTRY LQHETSIPAL LKGLEYLELF YRMVERRNIS DVTENLKHYL
LQYFKPVIDT QSWLDEGSVW DRMLRSTVLK LACYLNHAPC IQKATELFSQ WMESSGKLNI
PADVLTIVYS VGAQTTAGWN YLLEQYELSL SGAEKNKILY ALSTSKHQEK LMKLIELGME
GKVIKTQDLA TLLFTTARNP KGQQLAWNFV KENWTHLLKK FELGSFPIRM IISGTTSHFS
SKDELQEVKL FFESLKAQGS HLDIFQIILE TISKNIKWLE KNLPTLRKWL LTSI
