QVR_DROME
ID QVR_DROME Reviewed; 158 AA.
AC B5A5T4; A1Z8M0; B7YZF3; Q8SXP9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein quiver;
DE AltName: Full=Protein sleepless;
DE Flags: Precursor;
GN Name=qvr; Synonyms=sss; ORFNames=CG33472;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GPI-ANCHOR AT ASN-127, GLYCOSYLATION,
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18635795; DOI=10.1126/science.1155942;
RA Koh K., Joiner W.J., Wu M.N., Yue Z., Smith C.J., Sehgal A.;
RT "Identification of SLEEPLESS, a sleep-promoting factor.";
RL Science 321:372-376(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Required for homeostatic regulation of sleep under normal
CC conditions and after sleep deprivation. Important regulator of the Sh
CC K(+) channel, acting as a signaling molecule that connects sleep drive
CC to lowered membrane excitability, possibly by enhancing K(+) channel
CC activity and thus reducing neuronal excitability.
CC {ECO:0000269|PubMed:18635795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Enriched in brain and head.
CC {ECO:0000269|PubMed:18635795}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18635795}.
CC -!- DISRUPTION PHENOTYPE: Both daytime and nighttime sleep are severely
CC reduced in both males and females. A small percentage of flies (around
CC 9%) do not sleep at all. A moderate reduction has minimal effects on
CC baseline sleep but markedly reduces the amount of recovery sleep after
CC sleep deprivation. Mutants have impaired Sh-dependent K(+) current.
CC {ECO:0000269|PubMed:18635795}.
CC -!- SIMILARITY: Belongs to the quiver family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90233.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Sleepless nights - Issue 101
CC of January 2009;
CC URL="https://web.expasy.org/spotlight/back_issues/101";
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DR EMBL; EU816195; ACF58241.1; -; mRNA.
DR EMBL; AE013599; ACL83100.1; -; Genomic_DNA.
DR EMBL; AY089495; AAL90233.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001137646.1; NM_001144174.3.
DR AlphaFoldDB; B5A5T4; -.
DR BioGRID; 77570; 9.
DR STRING; 7227.FBpp0113067; -.
DR GlyGen; B5A5T4; 1 site.
DR PaxDb; B5A5T4; -.
DR PRIDE; B5A5T4; -.
DR EnsemblMetazoa; FBtr0114575; FBpp0113067; FBgn0260499.
DR GeneID; 2768718; -.
DR KEGG; dme:Dmel_CG33472; -.
DR UCSC; CG33472-RA; d. melanogaster.
DR UCSC; CG33472-RB; d. melanogaster.
DR CTD; 2768718; -.
DR FlyBase; FBgn0260499; qvr.
DR VEuPathDB; VectorBase:FBgn0260499; -.
DR eggNOG; ENOG502S199; Eukaryota.
DR HOGENOM; CLU_137010_0_0_1; -.
DR InParanoid; B5A5T4; -.
DR OMA; ICMYESK; -.
DR OrthoDB; 1561620at2759; -.
DR PhylomeDB; B5A5T4; -.
DR BioGRID-ORCS; 2768718; 0 hits in 1 CRISPR screen.
DR ChiTaRS; qvr; fly.
DR GenomeRNAi; 2768718; -.
DR PRO; PR:B5A5T4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0260499; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; B5A5T4; baseline and differential.
DR Genevisible; B5A5T4; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034235; F:GPI anchor binding; IDA:UniProtKB.
DR GO; GO:1903049; P:negative regulation of acetylcholine-gated cation channel activity; IGI:FlyBase.
DR GO; GO:0045837; P:negative regulation of membrane potential; IGI:FlyBase.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IMP:FlyBase.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0030431; P:sleep; IGI:FlyBase.
DR InterPro; IPR031424; QVR.
DR Pfam; PF17064; QVR; 1.
PE 1: Evidence at protein level;
KW Biological rhythms; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..127
FT /note="Protein quiver"
FT /id="PRO_0000359760"
FT PROPEP 128..158
FT /note="Removed in mature form"
FT /id="PRO_0000359761"
FT LIPID 127
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000305|PubMed:18635795"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 110..117
FT /note="MESSGNGH -> VEGSGSGR (in Ref. 1; ACF58241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18124 MW; BF3E8327EC40A58F CRC64;
MWTQRNAVGN WLLVLTAVIG FLTFIWIPQT SAECQTRSIY CYECDSWTDA RCKDPFNYTA
LPRDQPPLMT CNGCCVKMVR HQRSPYEVVR RMCTSQLQIN LFMVDHVCMM ESSGNGHMCF
CEEDMCNSSK NLHTNGCQLH LIPIAVAVSW LMGQLLSR
