CUE_DROAN
ID CUE_DROAN Reviewed; 643 AA.
AC B3M8G0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GF25031;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV38895.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV38895.1};
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; CH902618; EDV38895.1; -; Genomic_DNA.
DR RefSeq; XP_001956089.1; XM_001956053.2.
DR AlphaFoldDB; B3M8G0; -.
DR SMR; B3M8G0; -.
DR STRING; 7217.FBpp0128223; -.
DR EnsemblMetazoa; FBtr0129731; FBpp0128223; FBgn0102023.
DR GeneID; 6507657; -.
DR KEGG; dan:6507657; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; B3M8G0; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B3M8G0; -.
DR Proteomes; UP000007801; 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; 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..643
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386569"
FT TOPO_DOM 22..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 116..163
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 164..208
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 209..254
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT DOMAIN 363..397
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 398..429
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 432..470
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 276..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 372..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 387..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 405..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 436..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 440..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 460..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 643 AA; 72639 MW; 3C61DE38046F06DC CRC64;
MMIWVPALIF LSACLLPRSN GTPLEWDFAV TLRTKIQFLD SSWQTIATAA HEFDELSALT
FDESEELIYF NDRQHQNGSI FSLRRDAYAA SHVAQQAIQR TGNESVGGLA YDPLNRNLFW
SDTLQRKIFF ASIDSPPSQP PKVLVDLSQE GARPEGVAVD ICRRKLYWTN SNITHPTVER
IDVDGSNRVI IADSDIDMPK GIVVDQLSDR LFWIDDLKGV FFAVMSSNLD GSDRQVVLKD
KHHEPQNLAL TNDAIFWTDR TTKAVWSHPK RAAVKATTTV RPEVESSTDG TESESKQESE
PVEDCPLVRV ANLSEEARGI VARTGFYQRL QKDAHCSSIV RKIKLRLDEM SEKKEVRSLV
DERMDQLERD HCMNGGSYIS KRDLCICPAG FKGSRCEIRE CHNYCVHGTC QMSDLAYPKC
YCQPGFTGER CEVSNCAGLC LNGGHCRLGE TEKDQPSCEC PANFAGERCE QNSTQICSLF
CRLLKHEPEI HVPFGCHDIC EELALDNSTN IAIPQYQHLE VCQTPFVWTS SVIIILVVGI
VFSLLLITTI IHGIRRLYKP KRPRIRKTFV VRKQPRTNSA GDTPLTNRPM TAEQCEITIE
NCCNMNICET PCFDPKLVEQ TLAKSSCKED KKILIHNMED DLY
