CUE_DROVI
ID CUE_DROVI Reviewed; 636 AA.
AC B4LCX4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GJ12465;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW68835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW68835.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(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; CH940647; EDW68835.1; -; Genomic_DNA.
DR RefSeq; XP_002046493.1; XM_002046457.2.
DR AlphaFoldDB; B4LCX4; -.
DR SMR; B4LCX4; -.
DR STRING; 7244.FBpp0226882; -.
DR EnsemblMetazoa; FBtr0228390; FBpp0226882; FBgn0199707.
DR GeneID; 6622899; -.
DR KEGG; dvi:6622899; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; B4LCX4; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B4LCX4; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
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:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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 CDD; cd00055; EGF_Lam; 1.
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 InterPro; IPR002049; LE_dom.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00135; LY; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..636
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386578"
FT TOPO_DOM 28..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 122..169
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 170..214
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 215..260
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT DOMAIN 350..384
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 419..456
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
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 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 359..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 423..433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 427..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 446..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 636 AA; 71607 MW; 0A45D1C702FA06FB CRC64;
MKLCTSQQFG VAVLFIVLNI CSPLADASPI AWDFAVTLRD KILFVDNRWR TIGSAAHEFE
ELSALAFDEA EELIYFNDQQ HQNGSIFSLR RDATVASHIV EQAVQRTGND SVSGLAYDPL
NRNLFWADMR QSKIYFASID TLYTEPPKVL VDLSAEGGRP DGVAVDICRR QLYWTNCKIN
HATVERIGLN GTGRETIIKQ DIDMPRGIVI DQLSDRIFWI DDKVGIFFAL ESARLDGSDR
QLVLKDKHQS PIQLAITEDT IYWTDKADKA VWSYPKPAYN KPATNSSETQ PQPTKLASWK
DDVYGIVART GFYQHLQKDA HCASVVRKVK QRLDNKLNNR THERSAVEER MDALEREHCL
NGASYMSRGN FCICPVGYKG ARCEISECHN FCVHGTCEIS DMGYPKCYCQ EDFYGERCEY
YKCNGHCLND GHCLVDKESG ELSCDCRENF TGTRCEHNET AHCASYCQHL KQHPDAFVPA
SCVDICEELH LSNGTIVTEY QAAAPLCADG PSSLRSGSVI IVLVVGIVSS LALVAVIVHG
LRLIYKPKRP RIKKTFVVRK QARLNSASDT PLTNRPLATE QCEITIENCC NMNICETPCF
DPKLVEQQFA ARDRKSPCVK EDKKILIHNM EDDLLT
