ID A0A182Y4U1_ANOST Unreviewed; 939 AA.
AC A0A182Y4U1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
OS Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI03477-PA, ECO:0000313|Proteomes:UP000076408};
RN [1] {ECO:0000313|Proteomes:UP000076408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA Sharakhov I.V., Tu Z.;
RT "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT stephensi.";
RL Genome Biol. 15:459-459(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASTEI03477-PA}
RP IDENTIFICATION.
RC STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI03477-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR AlphaFoldDB; A0A182Y4U1; -.
DR STRING; 30069.A0A182Y4U1; -.
DR EnsemblMetazoa; ASTEI03477-RA; ASTEI03477-PA; ASTEI03477.
DR VEuPathDB; VectorBase:ASTE000360; -.
DR VEuPathDB; VectorBase:ASTEI03477; -.
DR VEuPathDB; VectorBase:ASTEI20_031555; -.
DR OMA; SSYNHYR; -.
DR Proteomes; UP000076408; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of 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:SF253; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000076408};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 39..238
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 275..500
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 590..919
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 433
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 939 AA; 108008 MW; 9E27E1024D288D15 CRC64;
MTVMRSALLL VAILAAIAGT LGDSSNSYSS YRLPKSITPE HYNLRVYTHL GDERGFIFYG
RVAIRFLCHE AADSVVLHSK NLTLLEQQIT LHEVSPDVPQ KASREMDVKG VEYITEHDYA
VFHVSTALRK GARYELTIPF ESGLGTGLLG YYRSSYLDKR TKQKVWLAVT QFEPTYARQA
FPCFDEPEMK ATFDISLAHH ERYVALSNMP VNRTVPVEDM PGWVLDEFNT TVPMSTYLVA
YTVNDFEYRE ATTSEPGDVV FKIWARRDAI DQVDYARDIG PRVTRFYEDY FHQKFPLPKI
DMIAIPDFAS GAMENWGLIT YRETALLYHP NISTASNKHR VASVIAHELA HQWFGNLVTM
RWWTDLWLNE GFATYVASLG VDYLHPEWYS LEEESISNTL DIFKFDALLS SHPISVEIGH
PNQISQIFDA ISYEKGSIVI RMMHLFLSEE TFRDGVSRYL RRHAYGNAEQ DNLWEALTEE
AHANGVLPDF IDVKRVMDSW TLQTGYPIIT VTRNYDANSA EITQTRFVSS EVPADRNVTD
YCWWIPLTYT TAKSLDFNDT LPKGWMECTN GTSNGHQVKV MDDLPDSEHW VIFNVQLAGL
YKVKYDKTNY RLIIAQLNGP SYDAIGLLNR AQLIDDAMDL AWTGQQNYGI AFAMINYLRQ
ETEYIPWKSA LTNLNSLNRI LKRTPLYDIF KSYVQYILEP IYERLEVFNV TRKPTDRLDA
IKQLTLIASW ACRFEVGDCV DRSVQLFARW MNEANPDANN PVPIDLRPVV YCNAIRQGND
TQWNFLWRRY LQSNVGAEKI MIIGSLACTR QLWLVERFLQ WSLNSTSGVR KQDATILFSS
VSRNDAGFNA AKSFFLTRAD EIYEYLSPDT SRLSRYIKPL AEQMFSTQEV QELNELIRKK
TALFEKANQG VKQALETAQT NSKWAETNIN KMERLLPML
//
