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CUE_ANOGA
ID   CUE_ANOGA               Reviewed;         704 AA.
AC   Q7QIQ6;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 4.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE   Flags: Precursor;
GN   Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=AGAP007023;
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] {ECO:0000312|EMBL:EAA04702.4}
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: Has a role in spermatogenesis and oogenesis.
CC       {ECO:0000250|UniProtKB:Q95RU0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cueball family. {ECO:0000305}.
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DR   EMBL; AAAB01008807; EAA04702.4; -; Genomic_DNA.
DR   RefSeq; XP_308749.4; XM_308749.4.
DR   AlphaFoldDB; Q7QIQ6; -.
DR   STRING; 7165.AGAP007023-PA; -.
DR   PaxDb; Q7QIQ6; -.
DR   GeneID; 1270082; -.
DR   KEGG; aga:AgaP_AGAP007023; -.
DR   CTD; 1270082; -.
DR   VEuPathDB; VectorBase:AGAP007023; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   HOGENOM; CLU_026602_0_0_1; -.
DR   InParanoid; Q7QIQ6; -.
DR   OMA; KLYWTNS; -.
DR   OrthoDB; 520442at2759; -.
DR   PhylomeDB; Q7QIQ6; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00135; LY; 5.
DR   PROSITE; PS00022; EGF_1; 4.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 3.
PE   3: Inferred from homology;
KW   Cell membrane; Differentiation; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Oogenesis; Reference proteome; Repeat; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..704
FT                   /note="Protein cueball"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000386567"
FT   TOPO_DOM        27..594
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        595..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        616..704
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          69..119
FT                   /note="LDL-receptor class B 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          120..166
FT                   /note="LDL-receptor class B 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          199..242
FT                   /note="LDL-receptor class B 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          243..288
FT                   /note="LDL-receptor class B 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          363..397
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          432..478
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          514..551
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        372..385
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        387..396
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        436..446
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        440..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        467..477
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        518..528
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        522..539
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        541..550
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   704 AA;  79143 MW;  4E59FE1888ED20B8 CRC64;
     MKSPCRAAAG WLVLLLSSCC LGYVIATEWA AAVTTDNGIL FFDSNWRKIS SAAHQYSRIS
     AFAYDEVLGK LYFADLDHPE YRLFALDYDD TDELHKVTKL LPKSAQTAYI SGMAFDHLER
     RLYWTEKGTR SVYYVAIDEL LSSTRSAAAA ANGTAAAAAT AVEATTSAPP PSSSSPVQLV
     ATVQPDHELA GLAIDECRRH LYWTNCYPKT SNIVRAAMNG TVLNVHEEQV YLPKGITVDH
     YRNRLYWVEK KYGRRYTIES ADLEVNDQRT LQTGLDRLPA DIAVKNDYIY WTDQENNEIY
     EMSKEPNAPS RTVYRGEHPS AVILRANLLL EHQRNNPDCR SVVDRILENM QNSKPASVLQ
     QETQQQGQLT VCLNNGTVNH HTNTCLCQPA FGGKLCEIDL CNNYCAQGSC RIGRDNRPRC
     DCDRRYEGDR CDRNRCDGFC LNGGRCQFSN GTAGRTEEEM GDRTCLCEST GYSGARCENP
     ICGTDYCYNG ECYVEEGKRP KCRCKAGYRG ERCEEYSCNN YCLNGGHCTL GNETTVPECE
     CGEEFAGQRC EIAVRLCSTY NEDPQWQQYC LGISKTLPLM EPKVTYCKES FNRTVVYTSL
     CFTVSFALLL AVVLVVSRMM KPPRPRITKK MVVTPMTSRP PTTQCEITIE NCCNMNVCET
     PCFDTKLLKK SKKEDKQFLL EDIEDVGGSY RKLPNCGDGT AERK
 
 
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