ID   QVR_DROYA               Reviewed;         158 AA.
AC   B4P641;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein quiver {ECO:0000250|UniProtKB:B5A5T4};
DE   AltName: Full=Protein sleepless;
DE   Flags: Precursor;
GN   Name=qvr {ECO:0000250|UniProtKB:B5A5T4}; Synonyms=sss; ORFNames=GE12364;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1] {ECO:0000312|EMBL:EDW90916.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW90916.1};
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: 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 (By similarity).
CC       {ECO:0000250|UniProtKB:B5A5T4}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:B5A5T4};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:B5A5T4}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:B5A5T4}.
CC   -!- SIMILARITY: Belongs to the quiver family. {ECO:0000305}.
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DR   EMBL; CM000158; EDW90916.1; -; Genomic_DNA.
DR   RefSeq; XP_002091204.1; XM_002091168.2.
DR   AlphaFoldDB; B4P641; -.
DR   STRING; 7245.FBpp0257374; -.
DR   EnsemblMetazoa; FBtr0258882; FBpp0257374; FBgn0230111.
DR   GeneID; 6530272; -.
DR   KEGG; dya:Dyak_GE12364; -.
DR   eggNOG; ENOG502S199; Eukaryota.
DR   HOGENOM; CLU_137010_0_0_1; -.
DR   OMA; ICMYESK; -.
DR   OrthoDB; 1561620at2759; -.
DR   PhylomeDB; B4P641; -.
DR   ChiTaRS; qvr; fly.
DR   Proteomes; UP000002282; Chromosome 2R.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR   GO; GO:1903049; P:negative regulation of acetylcholine-gated cation channel activity; IEA:EnsemblMetazoa.
DR   GO; GO:0045837; P:negative regulation of membrane potential; IEA:EnsemblMetazoa.
DR   GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
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; ISS:UniProtKB.
DR   GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IEA:EnsemblMetazoa.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0030431; P:sleep; IEA:EnsemblMetazoa.
DR   InterPro; IPR031424; QVR.
DR   Pfam; PF17064; QVR; 1.
PE   3: Inferred from homology;
KW   Biological rhythms; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..127
FT                   /note="Protein quiver"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000365476"
FT   PROPEP          128..158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:B5A5T4"
FT                   /id="PRO_0000365477"
FT   LIPID           127
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:B5A5T4"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   158 AA;  18098 MW;  A34E8327EC40A59A CRC64;
     MWTQRNAVGN WLLVLTAVIG FLTFIWIPQT SAECQTRSIY CYECDSWTDA RCKDPFNYTA
     LPRDQPPLMT CNGCCVKMVR HQRSPYEVVR RMCTSQLQIN LFMVDHVCMM ESSGNGHMCF
     CEEDMCNSSK NLHTNGCQLH LIAIAVAVSW LMGQLLSR