5HT6R_MOUSE
ID 5HT6R_MOUSE Reviewed; 440 AA.
AC Q9R1C8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=5-hydroxytryptamine receptor 6;
DE Short=5-HT-6;
DE Short=5-HT6;
DE AltName: Full=Serotonin receptor 6;
GN Name=Htr6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Brain;
RX PubMed=11406289; DOI=10.1016/s0169-328x(01)00090-0;
RA Kohen R., Fashingbauer L.A., Heidmann D.E.A., Guthrie C.R., Hamblin M.W.;
RT "Cloning of the mouse 5-HT6 serotonin receptor and mutagenesis studies of
RT the third cytoplasmic loop.";
RL Brain Res. Mol. Brain Res. 90:110-117(2001).
RN [2]
RP FUNCTION, AND INTERACTION WITH MTOR.
RX PubMed=23027611; DOI=10.1002/emmm.201201410;
RA Meffre J., Chaumont-Dubel S., Mannoury la Cour C., Loiseau F., Watson D.J.,
RA Dekeyne A., Seveno M., Rivet J.M., Gaven F., Deleris P., Herve D.,
RA Fone K.C., Bockaert J., Millan M.J., Marin P.;
RT "5-HT(6) receptor recruitment of mTOR as a mechanism for perturbed
RT cognition in schizophrenia.";
RL EMBO Mol. Med. 4:1043-1056(2012).
RN [3]
RP FUNCTION, AND INTERACTION WITH CDK5.
RX PubMed=25078650; DOI=10.1242/dev.108043;
RA Jacobshagen M., Niquille M., Chaumont-Dubel S., Marin P., Dayer A.;
RT "The serotonin 6 receptor controls neuronal migration during corticogenesis
RT via a ligand-independent Cdk5-dependent mechanism.";
RL Development 141:3370-3377(2014).
CC -!- FUNCTION: This is one of the several different receptors for 5-
CC hydroxytryptamine (serotonin), a biogenic hormone that function as a
CC neurotransmitter, a hormone, and a mitogen. The activity of this
CC receptor is mediated by G proteins that stimulate adenylate cyclase. It
CC has a high affinity for tricyclic psychotropic drugs (By similarity).
CC Controls pyramidal neurons migration during corticogenesis, through the
CC regulation of CDK5 activity (PubMed:25078650). Is an activator of TOR
CC signaling (PubMed:23027611). {ECO:0000250|UniProtKB:P31388,
CC ECO:0000269|PubMed:23027611, ECO:0000269|PubMed:25078650}.
CC -!- SUBUNIT: Interacts with CDK5 (PubMed:25078650). Interacts with MTOR
CC (PubMed:23027611). Interacts with RPTOR and NF1 (By similarity).
CC {ECO:0000250|UniProtKB:P50406, ECO:0000269|PubMed:23027611,
CC ECO:0000269|PubMed:25078650}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF134158; AAD46490.1; -; mRNA.
DR CCDS; CCDS18838.1; -.
DR RefSeq; NP_067333.1; NM_021358.2.
DR RefSeq; XP_011248498.1; XM_011250196.2.
DR AlphaFoldDB; Q9R1C8; -.
DR SMR; Q9R1C8; -.
DR BioGRID; 200479; 3.
DR STRING; 10090.ENSMUSP00000101428; -.
DR BindingDB; Q9R1C8; -.
DR ChEMBL; CHEMBL1075268; -.
DR GlyGen; Q9R1C8; 1 site.
DR PhosphoSitePlus; Q9R1C8; -.
DR PaxDb; Q9R1C8; -.
DR PRIDE; Q9R1C8; -.
DR Antibodypedia; 15009; 113 antibodies from 28 providers.
DR DNASU; 15565; -.
DR Ensembl; ENSMUST00000068036; ENSMUSP00000068333; ENSMUSG00000028747.
DR Ensembl; ENSMUST00000105802; ENSMUSP00000101428; ENSMUSG00000028747.
DR GeneID; 15565; -.
DR UCSC; uc008vlr.1; mouse.
DR CTD; 3362; -.
DR MGI; MGI:1196627; Htr6.
DR VEuPathDB; HostDB:ENSMUSG00000028747; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q9R1C8; -.
DR OMA; RFLPCPH; -.
DR OrthoDB; 1173208at2759; -.
DR PhylomeDB; Q9R1C8; -.
DR TreeFam; TF351753; -.
DR Reactome; R-MMU-390666; Serotonin receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 15565; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9R1C8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9R1C8; protein.
DR Bgee; ENSMUSG00000028747; Expressed in cerebral cortex subventricular zone and 22 other tissues.
DR ExpressionAtlas; Q9R1C8; baseline and differential.
DR Genevisible; Q9R1C8; MM.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0014058; P:negative regulation of acetylcholine secretion, neurotransmission; ISO:MGI.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; ISO:MGI.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:UniProtKB.
DR CDD; cd15054; 7tmA_5-HT6; 1.
DR InterPro; IPR002232; 5HT6_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..440
FT /note="5-hydroxytryptamine receptor 6"
FT /id="PRO_0000068975"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 58..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..85
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 86..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..122
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 123..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 167..184
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 209..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..292
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 293..297
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 298..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 323..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 440 AA; 46998 MW; 4440CDEBE01FEF0C CRC64;
MVPEPGPVNS STPAWGPGPP PAPGGSGWVA AALCVVIVLT AAANSLLIAL ICTQPALRNT
SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI
SLDRYLLILS PLRYKLRMTA PRALALILGA WSLAALASFL PLLLGWHELG KARTSAPGQC
RLLASLPYVL VASGVTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGTA TAGQALETLQ
VPRTPRPGME SADSRRLTTK HSRKALKASL TLGILLSMFF VTWLPFFVAS IAQAVCDCIS
PGLFDVLTWL GYCNSTMNPI IYPLFMRDFK RALGRFVPCV HCPPEHRASP ASPSMWTSHS
GARPGLSLQQ VLPLPLPPNS DSDSASGGTS GLQLTAQLLL PGEATRDPPP PTRAPTVVNF
FVTDSVEPEI RQHPLGSPMN
