ID A0A3B3CE39_ORYME Unreviewed; 943 AA.
AC A0A3B3CE39;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ANPEP {ECO:0000313|Ensembl:ENSOMEP00000016085.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000016085.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000016085.1}
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 -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; A0A3B3CE39; -.
DR STRING; 30732.ENSOMEP00000016085; -.
DR PaxDb; 30732-ENSOMEP00000016085; -.
DR Ensembl; ENSOMET00000024456.1; ENSOMEP00000016085.1; ENSOMEG00000017738.1.
DR GeneTree; ENSGT00940000154876; -.
DR OMA; QVIIRIW; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000261560; 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:SF271; AMINOPEPTIDASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {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 Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {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 53..252
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 288..515
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 591..917
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 449
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 943 AA; 107402 MW; 84C49A03FAC7895C CRC64;
MGKNCKVSKL SLMCMCLVLV SVATFVVWIV VIIGDSKDVT AAWDRYRLPK TLVPEFYNVT
LWPRLQPDPD SGLYIFTGWS TVQFVCVEAT NLILIHSNKL NYTRMDTQLA SLTAEGGGSA
PRIKSTWLQL QTQYLVIQLK DKLVSGQSYQ LHTRFTGELA DDLVGFYRSE YEEDGVKRII
AISQMHPTHS RKTFPCFDEP AMKAVFHLTL IHHPGTVALS NGMETEVLHT TLDGEAVTQT
RFEPTEKMST YLLAIVVSNF TYLNTMQGDT LVRIWARRKT IEQGQGDYAL NLTGPILDFL
QSYYSIPYPL SKSDQIALPD FYYGAMENWG LVTYRETRLL YDPETSSNGN KETTATIIAH
ELAHMWFGNL VTLHWWNEVW LNEGFASYVS YLGADHAEPD WNVKDLIVLD DVHRVFAVDA
LTSSHPLTSD EDSIVLPEQI LEQFDTISYS KGAAVLRMLS DFLSEPVFKE GLSSYLKQFS
YSNTIGSDLW KHLQMAVSNN NISLPCQVDT VMNRWVLQMG FPVVKIDTTT GKISQKHFLL
DPENNVTVTS PYKYEWIVPV RWMKNGDLIG DIWWLMEKEA VNLDMRSGSS WILANINVTG
YYRVNYDLGN WERLLAQLMS DHQVLPVINR AQLVDDAFNL ARAQLVSTTL ALRTTSYLSR
DTEFMPWQFA LDNLHYYNLM LDRTEVYQPM QEYLKNQVTP LFLHYKNMTS NWTHVPEKHT
DQYNQVNAVQ TACETGLTEC QDLTSMWFKQ WMDNPQHNPI HPNLRSAVYC SAMAAGGEKE
WQFAWSQFKA ASVASEASKL MSALACTTNV ELLKMYLSYT LDPAMIRKQD ATAVITSVAD
NRASQSLAWE FVRDHWNFMF TQYGVGSFSF ASIILGVTAR FSTPAELQQL EDFVSKHEAA
GFGSASLAVD QALEKTKANI KWVQQNKQEI LDWFNSQIGL QKS
//
