CUE_DROGR
ID CUE_DROGR Reviewed; 605 AA.
AC B4IXJ2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GH15203;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDV96429.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDV96429.1};
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; CH916366; EDV96429.1; -; Genomic_DNA.
DR RefSeq; XP_001984081.1; XM_001984045.1.
DR AlphaFoldDB; B4IXJ2; -.
DR SMR; B4IXJ2; -.
DR STRING; 7222.FBpp0149109; -.
DR EnsemblMetazoa; FBtr0465496; FBpp0415738; FBgn0122678.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; B4IXJ2; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B4IXJ2; -.
DR Proteomes; UP000001070; 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; 4.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS51120; LDLRB; 4.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..605
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386571"
FT TOPO_DOM 32..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 53..97
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 98..145
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 146..190
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT REPEAT 191..236
FT /note="LDL-receptor class B 4"
FT /evidence="ECO:0000255"
FT DOMAIN 322..359
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 394..431
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 349..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 398..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 402..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 421..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 605 AA; 68309 MW; 0440A5BC27FE9A90 CRC64;
MAYIDQKHNT FWDDFAIALR DKIVFLNSTW GEIHASAHRF EDLSALAFDE AEEMIYFSDQ
THQNGSIFAL RRDDSTPIVV QRTGNDSVEG LAYDPLNRNL FWADMRQQKI FFSSVDTLAT
ELPKVLVDLS GEGGQPDGIA VDICRRQLYW TNGNIKSASV ERIGLDGKGR QTIISADIDM
PRGIVVDQLS DRIFWVDNKV GIFFAIESAR LDGSDRQVVV KGKHQDPKHL AINEDAIYWT
DRMDKAVWSY PKPTYSQEVT NVTQAEPELA KPFSKEKAYG IVTRTGFYQR LQKDAHCASI
VKKVKQQLNT RLNNRTHIRS AEGDRISQLE REHCLNGASF MSRGEFCICP VGFKGARCEI
SECHNYCVHG TCEISDAGFP KCYCQAEFYG ERCEYHKCNG HCLNSGHCSM DKESDAMRCE
CRPNFGGERC EHNLTEQCAI YCQHPETQLP VSCLDFCEEW SNSNDTATIT EYQTAGQCGP
APPVQGPLII VIVLGLVTTS GLVALTVHGV RLIYKPKRPR IKKTFVVRKQ ARLNSSSDTP
LTNRPLTTEQ CEITIENCCN MNICETPCFD PKLVEQTFSS RDRKAPCVKE DKKILIHSME
DNLLS
