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Database: UniProt
Entry: A0A3B4CE00_PYGNA
LinkDB: A0A3B4CE00_PYGNA
Original site: A0A3B4CE00_PYGNA 
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
//
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