5HT6R_RAT
ID 5HT6R_RAT Reviewed; 436 AA.
AC P31388;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=5-hydroxytryptamine receptor 6;
DE Short=5-HT-6;
DE Short=5-HT6;
DE AltName: Full=ST-B17;
DE AltName: Full=Serotonin receptor 6;
GN Name=Htr6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Corpus striatum;
RX PubMed=7680751;
RA Monsma F.J. Jr., Shen Y., Ward R.P., Hamblin M.W., Sibley D.R.;
RT "Cloning and expression of a novel serotonin receptor with high affinity
RT for tricyclic psychotropic drugs.";
RL Mol. Pharmacol. 43:320-327(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8389146; DOI=10.1006/bbrc.1993.1619;
RA Ruat M., Traiffort E., Arrang J.-M., Tardivel-Lacombe J., Diaz J.,
RA Leurs R., Schwartz J.-C.;
RT "A novel rat serotonin (5-HT6) receptor: molecular cloning, localization
RT and stimulation of cAMP accumulation.";
RL Biochem. Biophys. Res. Commun. 193:268-276(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Martial R.;
RT "A novel rat serotonin (5HT6) receptor.";
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: This is one of the several different receptors for 5-
CC hydroxytryptamine (serotonin), a biogenic hormone that functions 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 (PubMed:7680751).
CC Controls pyramidal neurons migration during corticogenesis, through the
CC regulation of CDK5 activity (By similarity). Is an activator of TOR
CC signaling (By similarity). {ECO:0000250|UniProtKB:P50406,
CC ECO:0000250|UniProtKB:Q9R1C8, ECO:0000269|PubMed:7680751}.
CC -!- SUBUNIT: Interacts with MTOR, RPTOR and NF1 (By similarity). Interacts
CC with CDK5 (By similarity). {ECO:0000250|UniProtKB:P50406,
CC ECO:0000250|UniProtKB:Q9R1C8}.
CC -!- INTERACTION:
CC P31388; P15205: Map1b; NbExp=2; IntAct=EBI-21279242, EBI-349666;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Localized exclusively in the central nervous
CC system, predominantly in the corpus striatum but also in various limbic
CC and cortical regions.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L03202; AAA40618.1; -; mRNA.
DR EMBL; S62043; AAB26908.1; -; mRNA.
DR EMBL; L19656; AAA40611.1; -; mRNA.
DR PIR; I57942; I57942.
DR PIR; JN0591; JN0591.
DR AlphaFoldDB; P31388; -.
DR SMR; P31388; -.
DR BioGRID; 249039; 2.
DR IntAct; P31388; 3.
DR STRING; 10116.ENSRNOP00000064366; -.
DR BindingDB; P31388; -.
DR ChEMBL; CHEMBL3372; -.
DR DrugCentral; P31388; -.
DR GuidetoPHARMACOLOGY; 11; -.
DR GlyGen; P31388; 1 site.
DR iPTMnet; P31388; -.
DR PhosphoSitePlus; P31388; -.
DR PaxDb; P31388; -.
DR PRIDE; P31388; -.
DR RGD; 62044; Htr6.
DR VEuPathDB; HostDB:ENSRNOG00000049761; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P31388; -.
DR OrthoDB; 800636at2759; -.
DR Reactome; R-RNO-390666; Serotonin receptors.
DR PRO; PR:P31388; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000049761; Expressed in frontal cortex.
DR ExpressionAtlas; P31388; baseline and differential.
DR Genevisible; P31388; RN.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISS: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; IMP:RGD.
DR GO; GO:0007612; P:learning; IDA:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0014058; P:negative regulation of acetylcholine secretion, neurotransmission; IMP:RGD.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IMP:RGD.
DR GO; GO:0014050; P:negative regulation of glutamate secretion; IMP:RGD.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IMP:RGD.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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..436
FT /note="5-hydroxytryptamine receptor 6"
FT /id="PRO_0000068977"
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..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 266..290
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 291..295
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 296..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 321..436
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"
FT CONFLICT 57
FT /note="L -> V (in Ref. 1; AAA40618)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..436
FT /note="PCVHCPPEHRPALPPPPCGPLTAVPDQASACSRCCLCLCRQTQIQTPLQGAP
FT RACSSQPSFCCLERPPGTPRHPPGPPLWSTSLSQTLWSLRYGRIHSVPP -> HASTVP
FT RSTGQPCLPLHVDLSQRCQTRPQLQQVLALPLPPNSDSDSASGGTSGLQLTAQLLLPGE
FT ATRDPPPPTRATTVVNFFVTDSVEPEIRPHPLSSPVN (in Ref. 1;
FT AAA40618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 46923 MW; 6BC00F6A3CBA5FB4 CRC64;
MVPEPGPVNS STPAWGPGPP PAPGGSGWVA AALCVVIVLT AAANSLLIVL ICTQPALRNT
SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI
SLDRYLLILS PLRYKLRMTA PRALALILGA WSLAALASFL PLLLGWHELG KARTPAPGQC
RLLASLPFVL VASGVTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGTA GQALETLQVP
RTPRPGMESA DSRRLATKHS RKALKASLTL GILLGMFFVT WLPFFVANIA QAVCDCISPG
LFDVLTWLGY CNSTMNPIIY PLFMRDFKRA LGRFLPCVHC PPEHRPALPP PPCGPLTAVP
DQASACSRCC LCLCRQTQIQ TPLQGAPRAC SSQPSFCCLE RPPGTPRHPP GPPLWSTSLS
QTLWSLRYGR IHSVPP
