CUE_DROWI
ID CUE_DROWI Reviewed; 651 AA.
AC B4MLE8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GK17203;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW72804.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW72804.1};
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; CH963847; EDW72804.1; -; Genomic_DNA.
DR RefSeq; XP_002061818.1; XM_002061782.2.
DR AlphaFoldDB; B4MLE8; -.
DR SMR; B4MLE8; -.
DR STRING; 7260.FBpp0246346; -.
DR EnsemblMetazoa; FBtr0247854; FBpp0246346; FBgn0219202.
DR GeneID; 6638883; -.
DR KEGG; dwi:6638883; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; B4MLE8; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B4MLE8; -.
DR Proteomes; UP000007798; 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: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; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..651
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386579"
FT TOPO_DOM 22..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 115..162
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 163..207
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 208..253
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT DOMAIN 374..408
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..440
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 443..480
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 290..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 383..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 398..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 416..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 447..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 451..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 470..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 651 AA; 73571 MW; 216C66517CD3EBC2 CRC64;
MILRLFILLS IITVYLQLSV GIQQQFEFAI TLKSKILFVD EHWNVVNTAA HEFDELSALT
FDESEERIYF NDGQHQNSSI FSLRKVGKSN HLAEQTIQRY GNESVGGIAY DPLNRTIYWS
DLLQKKIFYA SIDTVATEMP KILVDLSEEN GTPYGVAIDI CGRKLYWTNS NINHPTVERI
DLNGTGRLAI IDKNIDSPRG IVVDQGAKRI FWIDDLKGIF FAVMSAQLDG SDVKLVLKDK
NHEPQNLAVT RNAIYWTDRT TKSVWSHLKE PEIATTTTTT TTSTTQIPTV EGEEGTGAMD
DNDIWPVGDF ETTPKKSPLE RKINLTEEAR GIVARTGFYQ LQKDSQCSKV IQLVKQRLDE
SQQNNRVLNV VDEQLDELQR EHCLGGGTYY PQQKFCVCVP GYKGTRCETN ECHNFCVHGT
CQISEMGYPK CYCQPGYSGE RCEVKKCLNF CQNGGDCQLD ELTGEASCQC PSNFGGLRCE
HNSTEICGLF CRLLKHDSNT SVPFGCHDIC EQLAKDSSDL IAIPEYKHLD VCLAPNAWTG
SVLMPLMISL ILILLLLTIF IHGLRRLYKP KRPHIKKTFV VRKQARTNSS SDTPLTNRPL
ATEQCEITIE NCCNMNICET PCFDPKLVEF AKSNCKDDKK ILIHNMEDDL Y
