ID A0A3B4GJN9_9CICH Unreviewed; 961 AA.
AC A0A3B4GJN9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LOC102205484 {ECO:0000313|RefSeq:XP_005747990.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000023242.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000023242.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005747990.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- 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_005747990.1; XM_005747933.1.
DR AlphaFoldDB; A0A3B4GJN9; -.
DR STRING; 303518.ENSPNYP00000023242; -.
DR Ensembl; ENSPNYT00000023811.1; ENSPNYP00000023242.1; ENSPNYG00000017288.1.
DR GeneID; 102205484; -.
DR GeneTree; ENSGT00940000154876; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; 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 ECO:0000313|RefSeq:XP_005747990.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000695023};
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 74..273
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 309..536
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 612..935
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 38..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
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; 109200 MW; E1460E43AB7D8CDB CRC64;
MGKGFFISKT VGILGIIAGV GALATIIALS VVYSQEKGKN NNQNEEQTTS KPPTTTPIPS
NKPWDKYRLP KNLVPETYNV TLWPRLTPDP TTGLYTFLGS SVVDFECVED TDLILIHSNK
LNYTKFENQL ARLMSVSSVE APAIKSSWLQ GVTQYLVLEL DGTLKKGHKY RLYTEFIGEL
ADDLGGFYRS EYMEDGEKRV MATTQMQPTD ARKSFPCFDE PAMKAYFFIT LIHDRGTTAL
SNGKDIETTE INHDGQDLLK TVFERTEKMS TYLLAFIVSD YDSIVNSIDG VEIRIFARRS
AIAAGQGQYA LNKTGPILKF FEQYYNATYP LPKSDQIAIP DFNAGAMENW GLITYRETAL
LYDEAFSSNS NKERIATIIA HELAHMWFGN LVTLRWWNDL WLNEGFASYV EYLGANNAEP
EWNVTDLIVL GDIHRVFAID ALASSHPLSS KEEDIQTPAQ ISELFDAISY SKGASVLRML
SDFLTEDVFQ LGLRSYLSAF SFGNAVYTDL WYHLQKAADS SKLKLPDTLD NIMNTWVLQM
GFPVVTINTG TGSVSQQHFL LDPEAVVTTP SPFNYQWIIP IKWMMTGNMQ NPLWLTSKSE
TSEAMKATQD QWVLANVNMV GYYRVNYDDD NWAKLLDVLQ SNHQLIPLIN RAQILDDAFN
LARAKIISTV QALNTTKYLN NERDYIPWKA ALNNLDFFYL MFDRSEVYGP MQDYLVKKVS
PLFEYYKQMT DNWSKVPDGH MDQYNQVNAI SLACRTGLEE CQNLVMTWFQ EWMDTDTNRI
HPNLRSTVYC NAIAAGGKKE WDFAWSQFKN GSTAIESDKL RYALSCTKQP WLLNRYLEYT
LDPDMIRKQD ATATIVDIAS NVVGQSLAWD FVRARWSYIF SQYGGGSFSF SNLVNGVTKR
FSTEFELQQL KQFKADNSDV GFGSGTLALD QSIERTIANI KWVEENKKNV LDWFTTEANA
Q
//
