ID A0A3B5ARN1_9TELE Unreviewed; 923 AA.
AC A0A3B5ARN1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000024103.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000024103.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal glutamate (and to a lesser extent
CC aspartate) from a peptide.; EC=3.4.11.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001703};
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; A0A3B5ARN1; -.
DR Ensembl; ENSSPAT00000024502.1; ENSSPAP00000024103.1; ENSSPAG00000018053.1.
DR GeneTree; ENSGT00940000156946; -.
DR Proteomes; UP000261400; 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:SF242; GLUTAMYL 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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 92..280
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 315..498
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 592..902
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 45..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 351..355
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 854
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT SITE 473
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 923 AA; 104848 MW; 9DE9811B320C8CE2 CRC64;
MFNRRRGSNS TKKQYCIRGK HVFIICVTVA VCSLAVGLGV GLSRSDSVPV TPVPPTPGPT
QPPPSPGRGP CTPSTDSDGD WRNFRLPSYV TPVHYNLHLE PDLVDDTYSG TVDIQVEVSK
PTRHLWLHIR ETFVSAMPRL TMLNSQGAQR EVAVKSCFEY TPQQYVVVEA TEELPVTGPG
ELYVLSLDFQ GWLNGSVVGF YRVIYTEGGL TKKIAATDHE PTDARKSFPC FDEPNKKATY
TISITHDAAY GALSNMPPEQ LSGNKLKTTF QKSVPMSTYL VCFAVHQFKY VERTSARGIP
LRIYAQPSQL ATAEYAADIT EIIFDYFEEY FNMTYSISKL DKIAIPDFGT GAMENWGLIT
YRETNLLYDE NESSSDNKQR VASVIAHELV HQWFGNIVTM DWWDDLWLNE GFASFFEYVG
VEKARPDWGM RDIMIVNDVL PVMVDDALIS SHPIIVNVST PAEITSVFDA ISYSKGASIL
RMLEDWMGKD MFRDGCRVSQ TSSVLTHIEQ RVSGLPVADV MDTWTKQMGY PVLDLSVSET
NARLRQTRFL LDPKADANQP PSALGYKWTI PVKFQTVQNH VISDYSLSKD GLLKVNDDHM
GFYRVNHDDH MWNVISEQLQ TNHSVQLSSR SDRTSYIDDV FALARAGLID YGNAFNLTKY
LTKESDYIVW DRVASSIAYV RDMLSGKADL YPKFQVIIST QLGWSDVGAL LRETVLSIAC
QMEDPDALRQ ASHIFDQWIN GELSVAVNLR LLVYRYGMKN SGTEEKWNTM FERYKTSSLA
QEKDKLLYGL ASVENVDLLY KLLEATKDES VVKSQDLFTV VRYVSYNSLG QSMAWDWTTL
NWDYLVNRYT INDRNLGRLL TQISTTYNTE LQLWKMEHFF SRTPDAGAGE MPRQQALETV
RNNIEWLRQN EDEIRQWLEN NTV
//
