EBPR_ANOGA
ID EBPR_ANOGA Reviewed; 407 AA.
AC Q7QDY3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Enolase-binding protein {ECO:0000303|PubMed:24474798};
DE Short=AgEBP {ECO:0000303|PubMed:24474798};
DE Flags: Precursor;
GN Name=EBP {ECO:0000303|PubMed:24474798};
GN ORFNames=AgaP_AGAP010479 {ECO:0000312|EMBL:EAA07224.3};
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 {ECO:0000312|Proteomes:UP000007062};
RN [1] {ECO:0000312|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|Proteomes:UP000007062};
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).
RN [2] {ECO:0000305}
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH P.FALCIPARUM AND P.BERGHEI
RP ENO, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24474798; DOI=10.1073/pnas.1315517111;
RA Vega-Rodriguez J., Ghosh A.K., Kanzok S.M., Dinglasan R.R., Wang S.,
RA Bongio N.J., Kalume D.E., Miura K., Long C.A., Pandey A., Jacobs-Lorena M.;
RT "Multiple pathways for Plasmodium ookinete invasion of the mosquito
RT midgut.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E492-E500(2014).
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for ENO/enolase from
CC parasites P.berghei and P.falciparum (PubMed:24474798). The interaction
CC is involved in the invasion of the mosquito midgut by P.berghei
CC ookinete, but is dispensable for P.falciparum ookinete invasion
CC (PubMed:24474798). {ECO:0000269|PubMed:24474798}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ENO/enolase from
CC parasites P.berghei and P.falciparum. {ECO:0000269|PubMed:24474798}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24474798};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Localizes to
CC the luminal side of the midgut epithelium.
CC {ECO:0000269|PubMed:24474798}.
CC -!- TISSUE SPECIFICITY: Expressed in the female midgut epithelium.
CC {ECO:0000269|PubMed:24474798}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces oocyst formation
CC by 50% following infection with P.berghei but not with P.falciparum.
CC {ECO:0000269|PubMed:24474798}.
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DR EMBL; AAAB01008849; EAA07224.3; -; Genomic_DNA.
DR RefSeq; XP_311465.3; XM_311465.4.
DR EnsemblMetazoa; AGAP010479-RA; AGAP010479-PA; AGAP010479.
DR GeneID; 1272604; -.
DR KEGG; aga:AgaP_AGAP010479; -.
DR VEuPathDB; VectorBase:AGAP010479; -.
DR eggNOG; ENOG502T85J; Eukaryota.
DR InParanoid; Q7QDY3; -.
DR OMA; AKPENIH; -.
DR OrthoDB; 746769at2759; -.
DR Proteomes; UP000007062; Chromosome 3L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..407
FT /note="Enolase-binding protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5014588429"
FT TOPO_DOM 25..366
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 407 AA; 45076 MW; 3480EA30329A7FD5 CRC64;
MALGNALYPL TATVFLCVVG FATSSNENSR FLINSRLEVN VKSLLGEICG TNSSLLSIGV
KSLSNEYSDR TVENLCGNET TEVLLWIPVG NFGNLAELGL SSRYLGKGAG DEDFAEYCSY
DVTTKSCTTD NGAVEGSILL LAEKFPERYE LRDLVYKKWR NSTHLGAPIL AYGTLKNREP
AYKYVDQDIS YLADTRIEYV LPATVTHGIP LSVYRGKTES YKLVAGETYY SRIFKTINAI
RYMSPYSTIN VTVIGSEGRD YREFRAKLVT VYTDEEGYGW SKSLSSIEAA MIETKLTETH
VEYALPVNLY DTQPPVLSPL LPALNEGNSI VDKGQQPAKG IVAKPENIHI HISELDFGQA
YPGFRNVAIG AAILFFSVLG VAIIDMIRRT IANRRAKRLH LGKYSRT
