CBPA1_ANOGA
ID CBPA1_ANOGA Reviewed; 433 AA.
AC O02350; Q7Q1X1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Zinc carboxypeptidase A 1;
DE EC=3.4.17.-;
DE AltName: Full=AgCP;
DE Flags: Precursor;
GN ORFNames=AGAP009593;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=G3;
RX PubMed=9569647; DOI=10.1016/s0965-1748(97)00093-3;
RA Edwards M.J., Lemos F.J., Donnelly-Doman M., Jacobs-Lorena M.;
RT "Rapid induction by a blood meal of a carboxypeptidase gene in the gut of
RT the mosquito Anopheles gambiae.";
RL Insect Biochem. Mol. Biol. 27:1063-1072(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Involved in the digestion of the blood meal. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9569647}.
CC -!- TISSUE SPECIFICITY: Expressed in the posterior midgut in pupae and
CC female adults. {ECO:0000269|PubMed:9569647}.
CC -!- INDUCTION: By blood meal, 10 fold increase within 10 hours.
CC {ECO:0000269|PubMed:9569647}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF000953; AAB96576.1; -; Genomic_DNA.
DR EMBL; AAAB01008980; EAA13787.2; -; Genomic_DNA.
DR RefSeq; XP_318615.2; XM_318615.2.
DR AlphaFoldDB; O02350; -.
DR SMR; O02350; -.
DR STRING; 7165.AGAP009593-PA; -.
DR MEROPS; M14.A08; -.
DR PaxDb; O02350; -.
DR GeneID; 1278958; -.
DR KEGG; aga:AgaP_AGAP009593; -.
DR CTD; 1278958; -.
DR VEuPathDB; VectorBase:AGAP029977; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_2_1_1; -.
DR InParanoid; O02350; -.
DR OMA; MYKVNSE; -.
DR OrthoDB; 524270at2759; -.
DR PhylomeDB; O02350; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007586; P:digestion; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 2: Evidence at transcript level;
KW Carboxypeptidase; Disulfide bond; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..433
FT /note="Zinc carboxypeptidase A 1"
FT /id="PRO_0000004406"
FT ACT_SITE 387
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT DISULFID 253..276
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="A -> V (in Ref. 1; AAB96576)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="H -> D (in Ref. 1; AAB96576)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..330
FT /note="EHSP -> AHCG (in Ref. 1; AAB96576)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="Y -> I (in Ref. 1; AAB96576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 49099 MW; D96729383016EFCA CRC64;
MVRLNSAAGS RWWAPAMAIL AVALSVEAAE VARYDNYRLY RVTPHSEAQL RSVAAMEQAS
DSLIFLETAR KLGDRFDIVV APHKLADFTE TLESDYIPHE LIEQNVQRAF DEERVRLTNK
RAKGPFDWND YHTLEEIHAW LDQLASEHPK EVELLDAGRS HQNRTMKGVK LSYGPGRPGV
FLEGGIHARE WISPATVTYI LNQLLTSEDA KVRALAEKFD WYVFPNANPD GYAYTFQVNR
LWRKTRKAYG PFCYGADPNR NWDFHWAEQG TSNNACSDTY HGSEAFSEVE TRSLAAFVEK
LRGKLGAYIA FHSYSQLLLF PYGHTGEHSP NHQDLNEIAE ATVKSLAKRY GTQYKYGNVY
DAIYPASGSS VDWSYGAQDV KIAYTYELRP DGDAWNGFVL PPNEIVPTGE ETLDSLITLL
EESSARGYYD EKH
