CUE_CULQU
ID CUE_CULQU Reviewed; 658 AA.
AC B0WH58;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE Flags: Precursor;
GN Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=CPIJ006575;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000312|EMBL:EDS27565.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000312|EMBL:EDS27565.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231933; EDS27565.1; -; Genomic_DNA.
DR RefSeq; XP_001848072.1; XM_001848020.1.
DR AlphaFoldDB; B0WH58; -.
DR SMR; B0WH58; -.
DR STRING; 7176.CPIJ006575-PA; -.
DR GeneID; 6038248; -.
DR KEGG; cqu:CpipJ_CPIJ006575; -.
DR VEuPathDB; VectorBase:CPIJ006575; -.
DR VEuPathDB; VectorBase:CQUJHB001382; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_026602_0_0_1; -.
DR InParanoid; B0WH58; -.
DR OMA; KLYWTNS; -.
DR OrthoDB; 520442at2759; -.
DR PhylomeDB; B0WH58; -.
DR Proteomes; UP000002320; Partially assembled 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:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 SMART; SM00181; EGF; 5.
DR SMART; SM00135; LY; 5.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..658
FT /note="Protein cueball"
FT /evidence="ECO:0000255"
FT /id="PRO_0000386568"
FT TOPO_DOM 1..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 100..142
FT /note="LDL-receptor class B 1"
FT /evidence="ECO:0000255"
FT REPEAT 152..195
FT /note="LDL-receptor class B 2"
FT /evidence="ECO:0000255"
FT REPEAT 196..241
FT /note="LDL-receptor class B 3"
FT /evidence="ECO:0000255"
FT DOMAIN 352..384
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 387..422
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 458..495
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 356..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 360..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 395..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 412..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 462..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 466..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 485..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 658 AA; 74118 MW; 19BFDB063361CA8E CRC64;
MSGVTARMEN SIITTDSGIL FFDQNWTQVS SGGHQFQHIS AFAYDEVKQK LYFSDLKDPK
FRIFSLDANP QEEYHKVTKL LPKSDETAYI TGLVFDHLER KLYWTERGTH ALYSVEVDKI
GNGTDAGSLI STVTKVEDNH DLAGLAIDEC RRHLYWTNSY LQTSNVVRAT MAGKVLNSHT
EDVYEPKGIA VDHYSNRIYW VEKKFGRAFS IQSVNLEVED VKTFISENDK APTHVALNSR
YLYWVDQQVG EVHETLKSDS TQSRVVYRGN RPTAIIIKSA LLLNHQNNNP SCKSVIAKIL
DNVKRESEGE LPQADKPTSA KPEMIICLNN GILNHNTNSC ICLPEYQGNF CEIPICNNYC
VHGKCVIGRD NRPTCECDAK FEGERCDRSK CDGFCLNSGN CSFSDATATC ACPKNFSGKR
CETAICTSDY CYNGRCMVEE GGSPKCQCNV GYRGERCEEY TCNNYCLNDG KCVLNNETML
VECRCGAEYT GKRCEIPKRF CSLDTGNPEL QPYCDGIPLS SQQQQQQLVE PQISYCKNSF
NRTVVYASLA FAASLFILMV ILLIVRRFYE EGRPRITKRF KVTSNHTQMT SRPATQCEIT
IENCCNMNVC ETPCFDTNLL QKSSSKAEDK QYLLDDIENI AGSYRKLPSC AGGDKNLP
