CUE_DROPS
ID CUE_DROPS Reviewed; 647 AA.
AC Q29FE9;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GA11386;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL31306.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CH379067; EAL31306.2; -; Genomic_DNA.
DR RefSeq; XP_001354253.2; XM_001354217.3.
DR AlphaFoldDB; Q29FE9; -.
DR SMR; Q29FE9; -.
DR STRING; 7237.FBpp0276820; -.
DR EnsemblMetazoa; FBtr0278382; FBpp0276820; FBgn0071440.
DR GeneID; 4814131; -.
DR KEGG; dpo:Dpse_GA11386; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; Q29FE9; -.
DR OMA; KLYWTNS; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0071440; Expressed in adult organism and 3 other tissues.
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:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:EnsemblMetazoa.
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 Pfam; PF00058; Ldl_recept_b; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00135; LY; 4.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS51120; LDLRB; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..647
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386575"
FT TOPO_DOM 23..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 119..166
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 167..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 365..401
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 436..473
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 376..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 440..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 444..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 463..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 647 AA; 72928 MW; 3CAE7CBD68C9961C CRC64;
MLWCPSVLVP LIAVAACLPV LAIGTPLEWE FAITLKSKIL FVDEFWRTLA SAAHEFDELS
ALTFDETEEL IYFNDQQHRN GSIFSLRRDA LMASHIAEQA IQRTGNESVG GLAYDPLNRN
LFWSDTLQKK IFFASIDSKV TETPKVLVDL SQEGARPDGV AVDVCRRKLY WTNSNITHPT
VESIDLAGTN RQVIIDTDID MPRGIVVDQL SDRIFWIDDL KGVFFALKSA RLDGSDRQLV
LHDKHHEPLN LAVTNDAIYW TDKTTKAVWS HPKVPIVKAT TTTSPLKAEE EDATETIPDI
EPEPVAEVSA LLRVANLSEE ARGIVARTGF YQRLQKDEHC ANIVRKVKER LDLMTKKKQM
RSLVDEKTAQ LERDHCLNGG TYIADRVLCI CPTGFKGSRC EIRECHNFCV HGTCEISDRA
YPKCYCQPGF SGERCEISKC SGLCLNGGHC KLEDISEKPS CECPHNFAGE RCEQNSTEIC
ALFCRLLKHE ADIYVPFGCH DICEELAKDA SDKIAIPQYH HLEVCMTPSP WTSNVIIVLV
LGIVSCFFLV AVIVHGFRRL YKPKRPRIRK TFVVRKQART NSSGDTPLTN RPLATEQCEI
TIENCCNMNI CETPCFDPKL VEQTLAKSSN CKEDKKILIH NMDDDLY
