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CUE_AEDAE
ID   CUE_AEDAE               Reviewed;         664 AA.
AC   Q16YE7;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE   Flags: Precursor;
GN   Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=AAEL008564;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1] {ECO:0000312|EMBL:EAT39657.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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; CH477517; EAT39657.1; -; Genomic_DNA.
DR   RefSeq; XP_001653297.1; XM_001653247.1.
DR   AlphaFoldDB; Q16YE7; -.
DR   SMR; Q16YE7; -.
DR   STRING; 7159.AAEL008564-PA; -.
DR   GeneID; 5570793; -.
DR   KEGG; aag:5570793; -.
DR   VEuPathDB; VectorBase:AAEL008564; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   HOGENOM; CLU_026602_0_0_1; -.
DR   InParanoid; Q16YE7; -.
DR   OMA; KLYWTNS; -.
DR   OrthoDB; 520442at2759; -.
DR   PhylomeDB; Q16YE7; -.
DR   Proteomes; UP000008820; Chromosome 2.
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; -; 1.
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; 4.
DR   SMART; SM00135; LY; 5.
DR   PROSITE; PS00022; EGF_1; 5.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..664
FT                   /note="Protein cueball"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000386566"
FT   TOPO_DOM        22..552
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..664
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          115..157
FT                   /note="LDL-receptor class B 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          168..211
FT                   /note="LDL-receptor class B 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          212..257
FT                   /note="LDL-receptor class B 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          367..399
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          402..438
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          473..510
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        371..380
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        375..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        406..416
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        410..426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        428..437
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        477..487
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        481..498
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        500..509
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   664 AA;  75077 MW;  F0169CE54C27EB20 CRC64;
     MRNLGIAVTF AVLLVIGYVT ALEWDAVVTT DSGILFFDKN WTQISSGGHQ FHHISAFAYD
     EVKRKLYFSD LKDPSFRIFS LDTKPEEEYH KVAKLLPKSD QTGYITGLAF DHLERKLYWT
     EKGTHSVYSV EVDKLGAPAN ATDGLINLVA QVEENHDLAA LTIDECRRHL YWTNSYLQTS
     SIVRAAMNGT VLDDHKEDVY EPRGISVDHY NNRIYWVEKK YGRAFTVESA NLEVQDRQTF
     LRGEDKIPTH VSPNSQYLYW IDQEDGEVHE TMKSDSKVTR VVYKGSRPSA LIIRSGLLVE
     YQKNNPSCKA VVSEIIDNVR KESSEVKDVA QAVTSKPEMI TCLNKGILNH NTNSCICLPE
     YQGTFCEIPI CNNFCVHGEC VVGADSRPMC KCHAEFEGER CDRNICDGYC LNNGRCALSA
     TGQRSCTCSK NFSGARCETA ICTSDYCYNG ECFVENEVPE CKCNVGYRGD RCEEYTCNNY
     CLHDGTCILN NDTMLVECRC GSEYTGKRCE IPKRFCSLDN GNPEMQQYCE GVAIAKNLVE
     PQVTYCKNSF NRTVVYVSLA FTASLVTLVT ILCTVRRMYE RNRPRITKRF KVTNNTQMTS
     RPATQCEITI ENCCNMNVCE TPCFDTKILQ KSATKAEDKQ FLLDDIESIA GSYRKLPSCV
     AEKN
 
 
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