QVR_DROER
ID QVR_DROER Reviewed; 158 AA.
AC B3NSF6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 50.
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=GG20204;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV56458.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV56458.1};
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; CH954179; EDV56458.1; -; Genomic_DNA.
DR RefSeq; XP_001976058.1; XM_001976022.2.
DR AlphaFoldDB; B3NSF6; -.
DR STRING; 7220.FBpp0138750; -.
DR EnsemblMetazoa; FBtr0140258; FBpp0138750; FBgn0112395.
DR GeneID; 6546862; -.
DR KEGG; der:6546862; -.
DR eggNOG; ENOG502S199; Eukaryota.
DR HOGENOM; CLU_137010_0_0_1; -.
DR OMA; ICMYESK; -.
DR OrthoDB; 1561620at2759; -.
DR PhylomeDB; B3NSF6; -.
DR ChiTaRS; qvr; fly.
DR Proteomes; UP000008711; Unassembled WGS sequence.
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_0000365458"
FT PROPEP 128..158
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:B5A5T4"
FT /id="PRO_0000365459"
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; 18124 MW; BF3E8327EC40A58F CRC64;
MWTQRNAVGN WLLVLTAVIG FLTFIWIPQT SAECQTRSIY CYECDSWTDA RCKDPFNYTA
LPRDQPPLMT CNGCCVKMVR HQRSPYEVVR RMCTSQLQIN LFMVDHVCMM ESSGNGHMCF
CEEDMCNSSK NLHTNGCQLH LIPIAVAVSW LMGQLLSR