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Database: UniProt
Entry: A0A182YDX4_ANOST
LinkDB: A0A182YDX4_ANOST
Original site: A0A182YDX4_ANOST 
ID   A0A182YDX4_ANOST        Unreviewed;      1056 AA.
AC   A0A182YDX4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EnsemblMetazoa:ASTEI06660-PA};
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:ASTEI06660-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:ASTEI06660-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI06660-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       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
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}.
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DR   AlphaFoldDB; A0A182YDX4; -.
DR   STRING; 30069.A0A182YDX4; -.
DR   EnsemblMetazoa; ASTEI06660-RA; ASTEI06660-PA; ASTEI06660.
DR   VEuPathDB; VectorBase:ASTE007236; -.
DR   VEuPathDB; VectorBase:ASTEI06660; -.
DR   VEuPathDB; VectorBase:ASTEI20_042139; -.
DR   OMA; SYLWMKE; -.
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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:SF290; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          48..248
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          285..488
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          594..909
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         378
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            441
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1056 AA;  119959 MW;  669B7D288FF8B20B CRC64;
     MKWHRCESAV RCAPVQTALR ILILSLSFIH SNGQSEPLNY RLPNETYPLR YNIELITRIH
     DDTIGDDRFR FEGKVTIQLM ATDDRNAATD TITLNYRQID ITHVKLWYLI QNEWENVILD
     DSTSFTVDPV REFLTIHSPQ PLNGSYFLEI KYNGTLREDN GGFYRSSYRT NDGKVQWLAT
     TQFSPTDARH TFPCYDEPGI RAPIALRVIH GKNYSVLSNN VPIDVRESIM EGMVITTFPE
     TPKMPSYLLG IIVSDFAEVS LPSYARQLAY ARPTALSTPA ANFILEAGFK VLAVLEDFLQ
     TPYILRKLAH VAVPDFSPGA MENYGLITYK EENFLYNPQT SPMKQKKKIA TIVAHEIGHH
     YFGNYVSPAW WSYLWMKEGF ARFFEYTAAQ MVFPEMEIGK MYTIDKTHNA FQTDSLSSSR
     PMTYYVNTQT EISNIFDDIA YDKGGAVMLM FYHAFGQEPF RNALIKYIQD NALQAGTPAK
     FAEAMQSTMF DTLPPDSLPF NASALLASWT DQAGYPILYI SRSGADCALR IEQQRYLLKS
     NETSSSSAVQ WMIPYNFATA KNPSFQDTTY SGWITERFHT IKPTDDLSWT CDDWIVFNKQ
     QTGYYRVNYD SDLWQLITTA LLQNSSAFHE NNRAQVIDDA MNNGRSGRLQ YAVPLQLLRY
     LSKETDYVPW AAVDRNLALL NVLMRGTNKY DLWHKYCLEF VEPTYTLMGM TTLDQDTLTQ
     RMTREIVVSW ACKVGSASCL NNTAFIVREI AENRLKDADP DLREPIFCNG LRNASAAVFD
     SIWQRMQASQ DQAYRSELIR SLGCVESEPL VNQYLDSTIS TNSSNYYNQE RERVFMAVYR
     NGEFGLQLAM KFLLENMDQV NQLYNKGNFG GRAISSIVRN MAQQITNEDM HTQLQDLMEK
     LLEKGFLRSA DMLQALEYSS ENLMWIQERG AQIAAWLDEQ YPDPPPTTTT ISTTTTTTTP
     ATTSTVTVTP TSTLSSAKSS TSDAISTSSI SITTISSLPT TISTKYDIIS NVSTSPMDSI
     TSTENYDDNG ASHIQHDVFY STLLVVVSVL LIMFTQ
//
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