CUE_DROYA
ID CUE_DROYA Reviewed; 644 AA.
AC B4PD96;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GE20954;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW92844.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW92844.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000159; EDW92844.1; -; Genomic_DNA.
DR RefSeq; XP_002093132.1; XM_002093096.2.
DR AlphaFoldDB; B4PD96; -.
DR SMR; B4PD96; -.
DR STRING; 7245.FBpp0265964; -.
DR EnsemblMetazoa; FBtr0267472; FBpp0265964; FBgn0238239.
DR GeneID; 6532381; -.
DR KEGG; dya:Dyak_GE20954; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B4PD96; -.
DR Proteomes; UP000002282; Chromosome 3L.
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: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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR Pfam; PF00058; Ldl_recept_b; 2.
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 3: Inferred from homology;
KW Cell membrane; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Oogenesis; Repeat; Signal; Spermatogenesis;
KW 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_0000386580"
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 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:0000255"
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; 72388 MW; 865FA87B331D86C9 CRC64;
MIRIRFGMDV LLVLLLATCL LSPTHGTPLE WDFAVTLRTK IQFMDSSWQT IATAAHEFDE
LSALTFDESE ELIYFNDLKH RNGSIFSLKR DLIAANHVVE QTIARTGNES VAGLAYDPLT
TNLFWSDTEQ RKIFFASIHG SATPKVLVDL SAEGGRPDGV AVDVCRRKLY WTNSNVTHPT
VERIDLDGSN RTVIVNSDID MPRGIVVDQL SDRLFWIDDL KGVFFSVESS KLDGSDRQVV
LKDKHHEPLN LAVTNDAIYW TDRTTRSVWS HPKVPVIRVT TTSKPEEEDS TDATDFKDPE
PVAEDCPLVR VANLSEEARG IVARTGFYQR LQKDHHCASI VRKVKQRVDE QSRKFEVSSL
LDQKMKVLEN ERCMNNGEYK AATDLCICPT GFKGSRCEIR ECHNYCVHGT CQMSESAYPK
CYCQPGFTGE RCEVSVCAGL CLNGGHCRAS KEENEAPTCE CPAKFGGARC EQNSTEICSL
FCRLLKHEPE MYVPFGCHSI CEELAQGNST NIAVPQYQHL EVCLTPTVWT SSVIIILVVG
IVSSLLLVAV IVHGIRRLYK PKRPRIRKTF VVRKQARTNS AGDTPLTNRP LATEQCEITI
ENCCNMNICE TPCFDPKLVE QTLSKSSCKE DKKILIHNME DDLY
