5HT6R_PANTR
ID 5HT6R_PANTR Reviewed; 440 AA.
AC Q5IS65;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 (By similarity).
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:P31388,
CC ECO:0000250|UniProtKB:P50406, ECO:0000250|UniProtKB:Q9R1C8}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY665263; AAV74301.1; -; mRNA.
DR RefSeq; NP_001029264.1; NM_001034092.1.
DR AlphaFoldDB; Q5IS65; -.
DR SMR; Q5IS65; -.
DR STRING; 9598.ENSPTRP00000000474; -.
DR PaxDb; Q5IS65; -.
DR Ensembl; ENSPTRT00000000546; ENSPTRP00000000474; ENSPTRG00000000271.
DR GeneID; 469199; -.
DR KEGG; ptr:469199; -.
DR CTD; 3362; -.
DR VGNC; VGNC:8052; HTR6.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q5IS65; -.
DR OMA; RFLPCPH; -.
DR OrthoDB; 1173208at2759; -.
DR TreeFam; TF351753; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000000271; Expressed in dorsolateral prefrontal cortex and 3 other tissues.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS: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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..440
FT /note="5-hydroxytryptamine receptor 6"
FT /id="PRO_0000068976"
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..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 346..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 99..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 440 AA; 46952 MW; 75CFFF4D27F126EE CRC64;
MVPEPGPSAN STPAWGAGPP SAPGGSGWVA AALCVVIALT AAANSLLIAL ICTQPALRNT
SNFFLVSLFT SDLMVGLVVM PPAMLNALYG RWVLARGLCL LWTAFDVMCC SASILNLCLI
SLDRYLLILS PLRYKLRMTP PRALALVLGA WSLAALASFL PLLLGWHELG HARPPVPGQC
RLLASLPFVL VASGLTFFLP SGAICFTYCR ILLAARKQAV QVASLTTGMA SQASETLQVP
RTPRPGVESA DSRRLATKHS RKALKASLTL GILLGMFFVT WLPFFVANIV QAVCDCISPG
LFDVLTWLGY CNSTMNPIIY PLFMRDFKRA LGRFLPCPRC PRERQASLAS PSLRTSHSGP
RPGLSLQQVL PLPLPPDSDS DSDAGSGGSS GLRLTAQLLL PGEATRDPPL PTRAAAAVNF
FNIDPAEPEL RPHPLGIPTN
