CUE_DROME
ID CUE_DROME Reviewed; 644 AA.
AC Q95RU0; Q9W0E5;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein cueball {ECO:0000303|PubMed:8244010};
DE Flags: Precursor;
GN Name=cue {ECO:0000312|FlyBase:FBgn0011204}; ORFNames=CG12086;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF47503.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF47503.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL28687.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28687.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8244010; DOI=10.1093/genetics/135.2.489;
RA Castrillon D.H., Gonczy P., Alexander S., Rawson R., Eberhart C.G.,
RA Viswanathan S., DiNardo S., Wasserman S.A.;
RT "Toward a molecular genetic analysis of spermatogenesis in Drosophila
RT melanogaster: characterization of male-sterile mutants generated by single
RT P element mutagenesis.";
RL Genetics 135:489-505(1993).
RN [5] {ECO:0000305}
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-313, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP FUNCTION.
RX PubMed=25409104; DOI=10.5665/sleep.4680;
RA Thimgan M.S., Seugnet L., Turk J., Shaw P.J.;
RT "Identification of genes associated with resilience/vulnerability to sleep
RT deprivation and starvation in Drosophila.";
RL Sleep 38:801-814(2015).
CC -!- FUNCTION: Has a role in spermatogenesis and oogenesis (PubMed:8244010).
CC Might have a role in triglyceride homeostasis (PubMed:25409104).
CC Probably by regulating lipid storage and catabolism, plays a role in
CC neuronal function (PubMed:25409104). {ECO:0000269|PubMed:25409104,
CC ECO:0000269|PubMed:8244010}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of spermatocytes with cytoplasmic
CC abnormalities. Early spermatocytes are filled with small, refractile
CC cytoplasmic inclusions, late spermatocytes often contain up to three
CC hook-shaped structures in the cytoplasm. Testes are short with
CC incomplete coiling. The sheath of pigment cells that covers the muscle
CC layer surrounding the testis frequently peels away, particularly from
CC the region near the tip. Female fertility is also reduced, ovaries are
CC small and misshapen. {ECO:0000269|PubMed:8244010}.
CC -!- SIMILARITY: Belongs to the cueball family. {ECO:0000305}.
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DR EMBL; AE014296; AAF47503.2; -; Genomic_DNA.
DR EMBL; AY061139; AAL28687.1; -; mRNA.
DR RefSeq; NP_612113.2; NM_138269.3.
DR AlphaFoldDB; Q95RU0; -.
DR SMR; Q95RU0; -.
DR BioGRID; 63712; 1.
DR IntAct; Q95RU0; 1.
DR STRING; 7227.FBpp0072590; -.
DR GlyGen; Q95RU0; 7 sites.
DR iPTMnet; Q95RU0; -.
DR PaxDb; Q95RU0; -.
DR PRIDE; Q95RU0; -.
DR DNASU; 38174; -.
DR EnsemblMetazoa; FBtr0072706; FBpp0072590; FBgn0011204.
DR GeneID; 38174; -.
DR KEGG; dme:Dmel_CG12086; -.
DR UCSC; CG12086-RA; d. melanogaster.
DR CTD; 38174; -.
DR FlyBase; FBgn0011204; cue.
DR VEuPathDB; VectorBase:FBgn0011204; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000162544; -.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; Q95RU0; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; Q95RU0; -.
DR SignaLink; Q95RU0; -.
DR BioGRID-ORCS; 38174; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38174; -.
DR PRO; PR:Q95RU0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011204; Expressed in saliva-secreting gland and 12 other tissues.
DR Genevisible; Q95RU0; DM.
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:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; SM00179; EGF_CA; 1.
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 1: Evidence at protein level;
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..644
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386572"
FT TOPO_DOM 27..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 121..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 398..430
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 433..471
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
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 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 402..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 406..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 437..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 441..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 461..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 644 AA; 72623 MW; 1FF14BFD962E95EC CRC64;
MIRIRFGMDV LLVLLLATCL LTPAHGTPLE WDFAVTLRTK IQFMDSSWQT IATAAHEFDE
LSALTFDESE ELIYFNDLKH RNGSIFSLKR DLIAANHVAE QTIARTGNES VGGLAYDPLN
MNLFWSDTEQ RKIFFAPIHG SATPQVLVDL SAEGGRPDGV AVDVCRRKLY WTNSNVTHPT
VERINLDGSN RTVIISSNID MPRGIVVDQL SDRLFWIDDL KGVFFSVESS KLDGSDRQVV
LKDKHHEPLN LAVTNDAIYW TDRTTRAVWS HPKVPVIKVT TTSKPDEEDS TDSTDFKDPE
PVAEDCPLVR VANLSEEARG IVARTGFYQR LQKDHHCASI VRKVKERVDE QSRKFEIRSL
LDQKIKVLED ERCMNDGEYR AATDLCICPT GFKGSRCEIR ECHNYCVHGT CQMSELAYPK
CYCQPGFKGE RCELSVCSGL CLNGGHCRVS KDENEAPSCE CPAKFGGARC EQNSTEICSL
FCRLLKHEPE MYVPFGCHSI CEELAQDNST NIAIPQYQHL EVCLTPRVWT SSVIIILVVG
IVSSLLLVAV IVQGIRRLYK PKRPRIRKTF VVRKQARTNS AGDTPLTNRP LATEQCEITI
ENCCNMNICE TPCFDPKLVE QTLSKSSCKE DKKILIHNME DDLY
