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Database: UniProt
Entry: A0A182XMQ5_ANOQN
LinkDB: A0A182XMQ5_ANOQN
Original site: A0A182XMQ5_ANOQN 
ID   A0A182XMQ5_ANOQN        Unreviewed;      1042 AA.
AC   A0A182XMQ5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 2.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
OS   Anopheles quadriannulatus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA011151-PA, ECO:0000313|Proteomes:UP000076407};
RN   [1] {ECO:0000313|Proteomes:UP000076407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AQUA011151-PA}
RP   IDENTIFICATION.
RC   STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA011151-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; A0A182XMQ5; -.
DR   STRING; 34691.A0A182XMQ5; -.
DR   EnsemblMetazoa; AQUA011151-RA; AQUA011151-PA; AQUA011151.
DR   VEuPathDB; VectorBase:AQUA011151; -.
DR   Proteomes; UP000076407; 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; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 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|ARBA:ARBA00022438};
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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          188..372
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          407..624
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          704..1017
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        480
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         479
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         483
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         502
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            565
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   1042 AA;  117241 MW;  0D098AD76CE7D3B9 CRC64;
     MRLLYGNRRL APAVCVQYFQ HTTALAAPQA AAPRPYSAGR WNDSVATAAK QCYLFNSPSA
     VTSPASAAPA TVGLTSAWQR YRLREQRNTP PRSRVSACVQ RQQSSSGCYV HFAPKQSSGV
     WSTVVRPVVY GCDGNSARTV SCCARETQRR YSSTSATIDG SDVCETSEYK MSATTGKPKF
     QRLPTNVVPE HYRLTLKPNL TALTFEGNTA VELKVVEATD RITLNALDLK LGTATVSFGD
     QQLTAQDIQF DAGQETACFV FGAEIPPGKA TLAVEFSGEL NDKMKGFYRS KYFSPTGEER
     YAGVTQFEAT DARRCFPCWD EPAIKATFDI SLIVPTNLVA LSNMPVVEER PEPADNTVHF
     KFDRTPVMST YLVAVVVGEY DYVEDRSADG VLVRVYTPVG KREQGRFALD VATKVLPYYK
     DYFNIAYPLP KMDLIAISDF SAGAMENWGL ITYRETFVLV DPENTSLIRK QSIALTVGHE
     IAHQWFGNLV TMEWWTHLWL NEGYASFVEF LCVDHLFPDY DIWTQFVTDM YTRALELDCL
     RNSHPIEVPV GHPSEIDEIF DEISYNKGAS VIRMLHHYIG DEDFKRGMNL YLTRHQYNNT
     RTEDLWNALQ EASSKPVGAV MSTWIQRMGF PVVQVRSSKQ LEGNRRVLSI AQSKFCADGC
     EAPEQSLWMI PINVSTPSSG NAVSTVLETA TADITVEGVG EQDWVKINPG TIGYYRTQYP
     AEMLEQFLPA IKNMTLPPLD RLGLIDDLFA LVQAGKSSTV DALKVIDAYR NENNYTVWSS
     ISNCLAKLQL LLAHTPAEKQ FSEYGVRLYQ PVAEKLGWDV KPGESHLDTL LRSLVLGRLV
     SFGCPKTVAE AKRRFEEHAQ NKSVLPADLR STCYRAVLQH GDLATYDEML RLYRATDLHE
     EKDRISRALG SIGNVDILRK VIDFAMSEEV RAQDSVFVIV SVAINPKGRD MAWDYFCEHW
     QVLLNQYEGG FLLARLIKYL TENFSTEERA KEVEQFFREH DFPGTERTVS QSIETIRLNA
     DWMRRDLDAI SAYLKQQEAE GH
//
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