CUE_DROSE
ID CUE_DROSE Reviewed; 644 AA.
AC B4HVU2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GM14208;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW50057.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW50057.1};
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; CH480817; EDW50057.1; -; Genomic_DNA.
DR RefSeq; XP_002034921.1; XM_002034885.1.
DR AlphaFoldDB; B4HVU2; -.
DR SMR; B4HVU2; -.
DR STRING; 7238.B4HVU2; -.
DR EnsemblMetazoa; FBtr0197193; FBpp0195685; FBgn0169134.
DR GeneID; 6610335; -.
DR KEGG; dse:6610335; -.
DR HOGENOM; CLU_026602_0_0_1; -.
DR OMA; KLYWTNS; -.
DR PhylomeDB; B4HVU2; -.
DR Proteomes; UP000001292; 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: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; 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 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..644
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386576"
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..301
FT /note="Disordered"
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: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; 72715 MW; 92C3C29A9B8AA059 CRC64;
MIRIRFGMDV LLVLLLATCL LTPAHGTPLE WDFAVTLRTK IQFMDSSWQT IATAAHEFDE
LSALTFDESE ELIYFNDLKH RNGSIFSLKR DLVAANHVAE QTIARTGNES VGGLAYDPLN
MNLFWSDTEQ RKIFFAPIYG SATPKVLVDL SAEGGRPDGV AVDVCRRKLY WTNSNVTHPT
VERINLDGSN RTVIINSDID MPRGIVVDQL SDRLFWIDDL KGVFFSVESC KLDGSDRQVV
LKDKHHEPLN LAVTNDAIYW TDRTTRAVWS HPKVPVIKVT TTSKPEEEDS TDSTDFTDPE
PMAEDCPLVR VANLSEEARG IVVRTGFYQR LQKDHHCASI VRKVKERVVE QNRKFEIRSM
LDQKIKVLED ERCMNGGEYR AATDLCICPT GFKGSRCEIR ECHNYCVHGT CQMSELAYPK
CYCQPGFTGE RCELSVCSGL CLNGGHCRVS KDENEAPSCE CPAKFGGARC EQNSTEICSL
FCRLLKHEPE MYVPFGCHSI CEELAQDNST YIAVPQYEHL EVCLTPRVWT SSVIIILVVG
IVSSLLLVAV IVHGIRRLYK PKRPRIRKTF VVRKQARTNS AGDTPLTNRP LATEQCEITI
ENCCNMNICE TPCFDPKLVE QTLSKSSCKE DKKILIHNME DDLY
