ID A0A1L1RVF4_CHICK Unreviewed; 929 AA.
AC A0A1L1RVF4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ERAP1 {ECO:0000313|Ensembl:ENSGALP00010016831.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010016831.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010016831.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010016831.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR RefSeq; XP_001232418.2; XM_001232417.4.
DR AlphaFoldDB; A0A1L1RVF4; -.
DR SMR; A0A1L1RVF4; -.
DR STRING; 9031.ENSGALP00000062810; -.
DR Ensembl; ENSGALT00010029072.1; ENSGALP00010016831.1; ENSGALG00010012124.1.
DR GeneID; 427122; -.
DR KEGG; gga:427122; -.
DR CTD; 51752; -.
DR VEuPathDB; HostDB:geneid_427122; -.
DR GeneTree; ENSGT00940000159086; -.
DR InParanoid; A0A1L1RVF4; -.
DR OMA; MENWGVV; -.
DR OrthoDB; 3085317at2759; -.
DR Reactome; R-GGA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000014684; Expressed in colon and 13 other cell types or tissues.
DR ExpressionAtlas; A0A1L1RVF4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005138; F:interleukin-6 receptor binding; IEA:Ensembl.
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:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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; 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:SF156; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1L1RVF4};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 44..231
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 266..469
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 588..907
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 423
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 929 AA; 106564 MW; 6A10EBDEA3267C38 CRC64;
MAAPRWEVVV LGLASVAWCV GDAQSGGGSA QFPWDKVRLP KHVVPLHYHL LIHPNLTTLT
FTGTVAIDIA VTQPTNAVVL HSKRLRVTKA AIEAGAGSTC AVREVRVLQH PAHEQLALLA
AEPLCTGHNY TISIQYAANL SDSFHGFYKS TYRTQEGELR VLASTHFEPT SARMAFPCFD
EPAFKAMFSV KIRREPYHLA LSNMPLVKSV NIASWLVEDH FDTTVKMSTY LVAFIVSDFK
SISKVTSHGV KISIYTVPEK INQAHYALDA AVKLLDFYED YFSIPYPLPK QDLAAIPDFQ
SGAMENWGLT TYRESALLYD PEKSSVSSRL WITMVIAHEL AHQWFGNLVT MEWWNDLWLN
EGFAKFMELL SVNVTHPELT VEDYFLRRCF DAMEVDALNS SHPVSTPVED PAQILEMFDE
VSYEKGSCIL NMLRDFLTAD VFKAGLVQYL QKYSYQNTKN EDLWESLANI CPTVGTEKSE
LQSDGFCRRN QQSSSNAHWT KETLDVKAMM DTWTLQKGFP LVTVTVRGKN VHLQQEHYKK
GEDSLSPTEN GYLWHIPLTY ITSKSYTVER FLMRTKTDVI ILPEEVEWIK FNVDMNGYYI
VHYEDDGWDR LINLLRENHT VVSSNDRASL INNIFQLVRI KKLSISKAFD LTSYMKRETQ
IMPILQGMNE LVPIYKLMER RDMDDTEKQL KDYIVSLFKD LIDKQLWSDE GSVSERMLRQ
SLLMFACVRR YQPCVDKAEE YFSKWQKSNG TLRLPADVKT AVYTVGAQTS EGWDFLLSKY
QHHSFSVDKD KIASALSLTR NKEKLQWLMD EGLRGDIIKT QDFPYIIVSV ARNPSGYHLA
WTFLKENWEK LIEKFELGSS SIAGIVTGVT NQYSTRPQLA QVKEFFSSLE EKSAQLRCIQ
QAIETIEDNI QWMDRYFEEI KTWLQKNHS
//
