ID 5HT5A_HUMAN Reviewed; 357 AA.
AC P47898; Q2M2D2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=5-hydroxytryptamine receptor 5A;
DE Short=5-HT-5;
DE Short=5-HT-5A;
DE Short=5-HT5A;
DE AltName: Full=Serotonin receptor 5A;
GN Name=HTR5A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7988681; DOI=10.1016/0014-5793(94)01209-1;
RA Rees S., den Daas I., Foord S., Goodson S., Bull D., Kilpatrick G., Lee M.;
RT "Cloning and characterisation of the human 5-HT5A serotonin receptor.";
RL FEBS Lett. 355:242-246(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-262.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(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.
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; X81411; CAA57168.1; -; Genomic_DNA.
DR EMBL; X81412; CAA57168.1; JOINED; Genomic_DNA.
DR EMBL; AF498985; AAM21132.1; -; mRNA.
DR EMBL; BC112021; AAI12022.1; -; mRNA.
DR CCDS; CCDS5936.1; -.
DR PIR; I37107; I37107.
DR RefSeq; NP_076917.1; NM_024012.3.
DR PDB; 7UM4; X-ray; 2.80 A; A=22-357.
DR PDB; 7UM5; EM; 2.73 A; A=32-357.
DR PDB; 7UM6; EM; 2.79 A; A=32-357.
DR PDB; 7UM7; EM; 2.75 A; A=32-357.
DR PDB; 7X5H; EM; 3.10 A; R=2-357.
DR PDBsum; 7UM4; -.
DR PDBsum; 7UM5; -.
DR PDBsum; 7UM6; -.
DR PDBsum; 7UM7; -.
DR PDBsum; 7X5H; -.
DR AlphaFoldDB; P47898; -.
DR EMDB; EMD-26597; -.
DR EMDB; EMD-26598; -.
DR EMDB; EMD-26599; -.
DR SMR; P47898; -.
DR BioGRID; 109593; 2.
DR IntAct; P47898; 1.
DR MINT; P47898; -.
DR STRING; 9606.ENSP00000287907; -.
DR BindingDB; P47898; -.
DR ChEMBL; CHEMBL3426; -.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugCentral; P47898; -.
DR GuidetoPHARMACOLOGY; 10; -.
DR GlyCosmos; P47898; 2 sites, No reported glycans.
DR GlyGen; P47898; 2 sites.
DR iPTMnet; P47898; -.
DR PhosphoSitePlus; P47898; -.
DR BioMuta; HTR5A; -.
DR DMDM; 1345607; -.
DR PaxDb; 9606-ENSP00000287907; -.
DR PeptideAtlas; P47898; -.
DR Antibodypedia; 18848; 390 antibodies from 30 providers.
DR DNASU; 3361; -.
DR Ensembl; ENST00000287907.3; ENSP00000287907.2; ENSG00000157219.5.
DR GeneID; 3361; -.
DR KEGG; hsa:3361; -.
DR MANE-Select; ENST00000287907.3; ENSP00000287907.2; NM_024012.4; NP_076917.1.
DR UCSC; uc003wlu.3; human.
DR AGR; HGNC:5300; -.
DR CTD; 3361; -.
DR DisGeNET; 3361; -.
DR GeneCards; HTR5A; -.
DR HGNC; HGNC:5300; HTR5A.
DR HPA; ENSG00000157219; Tissue enriched (brain).
DR MIM; 601305; gene.
DR neXtProt; NX_P47898; -.
DR OpenTargets; ENSG00000157219; -.
DR PharmGKB; PA29558; -.
DR VEuPathDB; HostDB:ENSG00000157219; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_6_1; -.
DR InParanoid; P47898; -.
DR OMA; NLFFRQH; -.
DR OrthoDB; 2999405at2759; -.
DR PhylomeDB; P47898; -.
DR TreeFam; TF316350; -.
DR PathwayCommons; P47898; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P47898; -.
DR SIGNOR; P47898; -.
DR BioGRID-ORCS; 3361; 9 hits in 1140 CRISPR screens.
DR GeneWiki; 5-HT5A_receptor; -.
DR GenomeRNAi; 3361; -.
DR Pharos; P47898; Tchem.
DR PRO; PR:P47898; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P47898; Protein.
DR Bgee; ENSG00000157219; Expressed in cerebellar hemisphere and 47 other cell types or tissues.
DR ExpressionAtlas; P47898; baseline and differential.
DR Genevisible; P47898; HS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR CDD; cd15328; 7tmA_5-HT5; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR001397; 5HT5A_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR PANTHER; PTHR24247:SF108; 5-HYDROXYTRYPTAMINE RECEPTOR 5A; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00518; 5HT5ARECEPTR.
DR PRINTS; PR01101; 5HTRECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..357
FT /note="5-hydroxytryptamine receptor 5A"
FT /id="PRO_0000068969"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 41..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 64..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 79..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 100..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 138..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 159..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..198
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 199..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 220..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 283..303
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 304..320
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 321..341
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 342..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 262
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs746290830)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035753"
FT HELIX 42..67
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:7UM6"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:7UM5"
FT TURN 98..105
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 111..144
FT /evidence="ECO:0007829|PDB:7UM5"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 152..178
FT /evidence="ECO:0007829|PDB:7UM5"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 278..307
FT /evidence="ECO:0007829|PDB:7UM5"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 317..333
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:7UM5"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:7UM5"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:7UM5"
SQ SEQUENCE 357 AA; 40255 MW; 92F8A78C69169790 CRC64;
MDLPVNLTSF SLSTPSPLET NHSLGKDDLR PSSPLLSVFG VLILTLLGFL VAATFAWNLL
VLATILRVRT FHRVPHNLVA SMAVSDVLVA ALVMPLSLVH ELSGRRWQLG RRLCQLWIAC
DVLCCTASIW NVTAIALDRY WSITRHMEYT LRTRKCVSNV MIALTWALSA VISLAPLLFG
WGETYSEGSE ECQVSREPSY AVFSTVGAFY LPLCVVLFVY WKIYKAAKFR VGSRKTNSVS
PISEAVEVKD SAKQPQMVFT VRHATVTFQP EGDTWREQKE QRAALMVGIL IGVFVLCWIP
FFLTELISPL CSCDIPAIWK SIFLWLGYSN SFFNPLIYTA FNKNYNSAFK NFFSRQH
//
