ID A0A3B4CE00_PYGNA Unreviewed; 961 AA.
AC A0A3B4CE00;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ANPEP {ECO:0000313|Ensembl:ENSPNAP00000009101.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000009101.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000009101.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR RefSeq; XP_017555006.1; XM_017699517.1.
DR AlphaFoldDB; A0A3B4CE00; -.
DR STRING; 42514.ENSPNAP00000009101; -.
DR Ensembl; ENSPNAT00000015361.1; ENSPNAP00000009101.1; ENSPNAG00000014668.1.
DR GeneID; 108428483; -.
DR CTD; 555478; -.
DR GeneTree; ENSGT00940000154876; -.
DR OMA; IQRTWLV; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF172; AMINOPEPTIDASE N; 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 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 73..271
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 309..537
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 613..938
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 44..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 470
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 961 AA; 109878 MW; 324B86F6A3B4BAD5 CRC64;
MGKGFYISKN QAIVAALLAA VAVVTIIALS IVYSKEKAKR ALPLNDEKTS PVTPTSPPSN
EPWDKYRLPD TLKPQSYNIT LWPRLTEDAQ GMYIFTGSSE VVFMCEKETD LIIIHCNKLN
LTFFDGHHAK LIGMHRTAAP AIKKTWFQVE TQYLVVQLKG TLKPGKAYSL STEFKGELAD
DLEGFYRSEY KEDGIKKVVA ITQMQATYAR KAFPCFDEPA MKAIFHITLI HEPGTIALSN
SREIGTESLQ IDRINVIRTR FEPTKKMSTY LVAFIVSDFT YITKQEDNKD LMVRIWARQK
AIKGGQGDYA LSITQPIMEF FEKYYNTDYP LSKSDQIALP DFSAGAMENW GLVTYRETAL
LYDPKTSANG NKQRIATVVS HELAHMWFGN LVTLKWWNDL WLNEGFASYV EYLGADYAEP
TWNIKDQIIL YDMYRAFAVD SLVSSHPLSC KEEEVNKPAE ISQMFNTISY SKGAAVLRML
SEFLTEPVFA KGLTTYLNQF AFGNSVYSDL WDHLQKAVDR TPQLKLPHRV HDIMNRWILQ
MGFPVVTIDT GTGNVSQKHF LLEPNSVVEK PSEFNYEWYI PINWMKKSGE QDQLWLLQKS
AVHKPMKVSR GQWVLANVNV SGYYRVNYDL ENWERLLSQL NSNHQIIPVI NRAQILDDAF
NLARASIINI TLALRTTKYL SLEKEYIPWE AALRSLNSLF LVFDRSDVYG AMQAYLRNQV
KPLFDHFTSI TGNWTTVPLG HNDQFTQIIA LSLACKTGLP GCRDIIKAWF RQWMQDPDNN
KIHPNLRSTV YCYAIAAGGV EEWDFGWRMF KKATVAAEAV KLRSALACTR EPWLLNRYLE
YTLDPEKIRK QDATSTIGSI SSNIVGQPLA WNFVRARWEY LFKVYGTGSF SFSRLINDIT
ARFCTSFELS ELKQFQKDNA DVGFGSGTQA LQQAIEKTTA KIKWLEDNKQ QVLQWFISQS
A
//