5HT1B_HUMAN
ID 5HT1B_HUMAN Reviewed; 390 AA.
AC P28222; Q4VAY7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=5-hydroxytryptamine receptor 1B;
DE Short=5-HT-1B;
DE Short=5-HT1B;
DE AltName: Full=S12;
DE AltName: Full=Serotonin 1D beta receptor;
DE Short=5-HT-1D-beta;
DE AltName: Full=Serotonin receptor 1B;
GN Name=HTR1B; Synonyms=HTR1DB;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1315531; DOI=10.1016/0006-291x(92)90654-4;
RA Hamblin M.W., Metcalf M.A., McGuffin R.W., Karpells S.;
RT "Molecular cloning and functional characterization of a human 5-HT1B
RT serotonin receptor: a homologue of the rat 5-HT1B receptor with 5-HT1D-like
RT pharmacological specificity.";
RL Biochem. Biophys. Res. Commun. 184:752-759(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1610347; DOI=10.1016/0006-291x(92)91655-a;
RA Mochizuki D., Yuyama Y., Tsujita R., Komaki H., Sagai H.;
RT "Cloning and expression of the human 5-HT1B-type receptor gene.";
RL Biochem. Biophys. Res. Commun. 185:517-523(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=1348246; DOI=10.1016/s0021-9258(18)42612-9;
RA Jin H., Oksenberg D., Ashkenazi A., Peroutka S.J., Duncan A.M.V.,
RA Rozmahel R., Yang Y., Mengod G., Palacios J.M., O'Dowd B.F.;
RT "Characterization of the human 5-hydroxytryptamine1B receptor.";
RL J. Biol. Chem. 267:5735-5738(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1559993; DOI=10.1016/s0021-9258(18)42552-5;
RA Levy F.O., Gudermann T., Perez-Reyes E., Birnbaumer M., Kaumann A.J.,
RA Birnbaumer L.;
RT "Molecular cloning of a human serotonin receptor (S12) with a
RT pharmacological profile resembling that of the 5-HT1D subtype.";
RL J. Biol. Chem. 267:7553-7562(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=1565658; DOI=10.1073/pnas.89.8.3630;
RA Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., Hartig P.R.;
RT "Human serotonin 1D receptor is encoded by a subfamily of two distinct
RT genes: 5-HT1D alpha and 5-HT1D beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=1351684; DOI=10.1073/pnas.89.12.5522;
RA Demchyshyn L., Sunahara R.K., Miller K., Teitler M., Hoffman B.J.,
RA Kennedy J.L., Seeman P., van Tol H.H.M., Niznik H.B.;
RT "A human serotonin 1D receptor variant (5HT1D beta) encoded by an
RT intronless gene on chromosome 6.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5522-5526(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1328844;
RA Veldman S.A., Bienkowski M.J.;
RT "Cloning and pharmacological characterization of a novel human 5-
RT hydroxytryptamine1D receptor subtype.";
RL Mol. Pharmacol. 42:439-444(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "Isolation of complete coding sequence for 5-hydroxytryptamine (serotonin)
RT receptor 1B (HTR1B).";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [12]
RP PALMITOYLATION, PHOSPHORYLATION, AND FUNCTION.
RX PubMed=8218242; DOI=10.1021/bi00094a032;
RA Ng G.Y.K., George S.R., Zastawny R.L., Caron M., Bouvier M., Dennis M.,
RA O'Dowd B.F.;
RT "Human serotonin1B receptor expression in Sf9 cells: phosphorylation,
RT palmitoylation, and adenylyl cyclase inhibition.";
RL Biochemistry 32:11727-11733(1993).
RN [13]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10452531; DOI=10.1016/s0014-5793(99)00918-7;
RA Xie Z., Lee S.P., O'Dowd B.F., George S.R.;
RT "Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone
RT and heterodimers when co-expressed.";
RL FEBS Lett. 456:63-67(1999).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15853772; DOI=10.1042/cs20050016;
RA Edvinsson L., Uddman E., Wackenfors A., Davenport A., Longmore J.,
RA Malmsjo M.;
RT "Triptan-induced contractile (5-HT1B receptor) responses in human cerebral
RT and coronary arteries: relationship to clinical effect.";
RL Clin. Sci. 109:335-342(2005).
RN [15]
RP REVIEW.
RX PubMed=18476671; DOI=10.1021/cr078224o;
RA Nichols D.E., Nichols C.D.;
RT "Serotonin receptors.";
RL Chem. Rev. 108:1614-1641(2008).
RN [16]
RP REVIEW.
RX PubMed=20945968; DOI=10.33549/physiolres.931903;
RA Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT "Serotonin receptors - from molecular biology to clinical applications.";
RL Physiol. Res. 60:15-25(2011).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23519215; DOI=10.1126/science.1232808;
RA Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E.,
RA McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., Cherezov V.,
RA Roth B.L., Stevens R.C.;
RT "Structural features for functional selectivity at serotonin receptors.";
RL Science 340:615-619(2013).
RN [18] {ECO:0007744|PDB:4IAQ, ECO:0007744|PDB:4IAR}
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-239 AND 306-390 IN COMPLEXES
RP WITH ERGOTAMINE AND DIHYDROERGOTAMINE, FUNCTION, SUBCELLULAR LOCATION,
RP MEMBRANE TOPOLOGY, DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF LEU-126;
RP ASP-129; ILE-130; CYS-133; THR-134; VAL-200; VAL-201; THR-203; THR-209;
RP SER-212; ALA-216; TRP-327; PHE-330; PHE-331; SER-334; MET-337; PHE-351;
RP ASP-352; THR-355 AND TYR-359.
RX PubMed=23519210; DOI=10.1126/science.1232807;
RA Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., Liu W.,
RA Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., Melcher K.,
RA Zhang C., Bai F., Yang H., Yang L., Jiang H., Roth B.L., Cherezov V.,
RA Stevens R.C., Xu H.E.;
RT "Structural basis for molecular recognition at serotonin receptors.";
RL Science 340:610-614(2013).
RN [19]
RP VARIANT CYS-124.
RX PubMed=7802650; DOI=10.1006/bbrc.1994.2792;
RA Nothen M.M., Erdmann J., Shimron-Abarbanell D., Propping P.;
RT "Identification of genetic variation in the human serotonin 1D beta
RT receptor gene.";
RL Biochem. Biophys. Res. Commun. 205:1194-1200(1994).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for ergot alkaloid
CC derivatives, various anxiolytic and antidepressant drugs and other
CC psychoactive substances, such as lysergic acid diethylamide (LSD).
CC Ligand binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase. Signaling
CC inhibits adenylate cyclase activity. Arrestin family members inhibit
CC signaling via G proteins and mediate activation of alternative
CC signaling pathways. Regulates the release of 5-hydroxytryptamine,
CC dopamine and acetylcholine in the brain, and thereby affects neural
CC activity, nociceptive processing, pain perception, mood and behavior.
CC Besides, plays a role in vasoconstriction of cerebral arteries.
CC {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1315531,
CC ECO:0000269|PubMed:1328844, ECO:0000269|PubMed:1348246,
CC ECO:0000269|PubMed:1351684, ECO:0000269|PubMed:1559993,
CC ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:15853772,
CC ECO:0000269|PubMed:1610347, ECO:0000269|PubMed:23519210,
CC ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:8218242}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D.
CC {ECO:0000269|PubMed:10452531}.
CC -!- INTERACTION:
CC P28222; P35609: ACTN2; NbExp=3; IntAct=EBI-1056863, EBI-77797;
CC P28222; Q99750: MDFI; NbExp=7; IntAct=EBI-1056863, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10452531,
CC ECO:0000269|PubMed:1315531, ECO:0000269|PubMed:1328844,
CC ECO:0000269|PubMed:1348246, ECO:0000269|PubMed:1351684,
CC ECO:0000269|PubMed:1559993, ECO:0000269|PubMed:1565658,
CC ECO:0000269|PubMed:1610347, ECO:0000269|PubMed:23519210,
CC ECO:0000269|PubMed:23519215}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1315531,
CC ECO:0000269|PubMed:1328844, ECO:0000269|PubMed:1348246,
CC ECO:0000269|PubMed:1351684, ECO:0000269|PubMed:1559993,
CC ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1610347,
CC ECO:0000269|PubMed:23519210, ECO:0000269|PubMed:23519215}.
CC -!- TISSUE SPECIFICITY: Detected in cerebral artery smooth muscle cells (at
CC protein level). Detected in brain cortex, striatum, amygdala, medulla,
CC hippocampus, caudate nucleus and putamen. {ECO:0000269|PubMed:1348246,
CC ECO:0000269|PubMed:1351684, ECO:0000269|PubMed:15853772}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000269|PubMed:23519210}.
CC -!- PTM: Phosphorylated. Desensitization of the receptor may be mediated by
CC its phosphorylation. {ECO:0000269|PubMed:8218242}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:8218242}.
CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region (Thr-355 in
CC human, 'Asn-351' in mouse and rat) is important for species-specific
CC sensitivity to various agonists.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M89478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D10995; BAA01763.1; -; Genomic_DNA.
DR EMBL; M83180; AAA36029.1; -; Genomic_DNA.
DR EMBL; L09732; AAA36030.1; -; Genomic_DNA.
DR EMBL; M81590; AAA60316.1; -; mRNA.
DR EMBL; M75128; AAA58675.1; -; Genomic_DNA.
DR EMBL; AB041370; BAA94455.1; -; Genomic_DNA.
DR EMBL; AY225227; AAO67712.1; -; Genomic_DNA.
DR EMBL; AL049595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069065; AAH69065.1; -; mRNA.
DR EMBL; BC096206; AAH96206.1; -; mRNA.
DR EMBL; BC096207; AAH96207.1; -; mRNA.
DR EMBL; BC096208; AAH96208.1; -; mRNA.
DR CCDS; CCDS4986.1; -.
DR PIR; JN0268; JN0268.
DR RefSeq; NP_000854.1; NM_000863.2.
DR PDB; 4IAQ; X-ray; 2.80 A; A=33-239, A=304-390.
DR PDB; 4IAR; X-ray; 2.70 A; A=33-239, A=306-390.
DR PDB; 5V54; X-ray; 3.90 A; A/B=37-390.
DR PDB; 6G79; EM; 3.78 A; S=34-390.
DR PDB; 7C61; X-ray; 3.00 A; A=33-239, A=306-390.
DR PDBsum; 4IAQ; -.
DR PDBsum; 4IAR; -.
DR PDBsum; 5V54; -.
DR PDBsum; 6G79; -.
DR PDBsum; 7C61; -.
DR AlphaFoldDB; P28222; -.
DR SMR; P28222; -.
DR BioGRID; 109583; 75.
DR CORUM; P28222; -.
DR IntAct; P28222; 7.
DR STRING; 9606.ENSP00000358963; -.
DR BindingDB; P28222; -.
DR ChEMBL; CHEMBL1898; -.
DR DrugBank; DB00918; Almotriptan.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB00543; Amoxapine.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB08807; Bopindolol.
DR DrugBank; DB01200; Bromocriptine.
DR DrugBank; DB00248; Cabergoline.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB00363; Clozapine.
DR DrugBank; DB04884; Dapoxetine.
DR DrugBank; DB11273; Dihydroergocornine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB00216; Eletriptan.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00696; Ergotamine.
DR DrugBank; DB00998; Frovatriptan.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB00589; Lisuride.
DR DrugBank; DB00408; Loxapine.
DR DrugBank; DB00247; Methysergide.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00952; Naratriptan.
DR DrugBank; DB06096; NXN-188.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB00904; Ondansetron.
DR DrugBank; DB00935; Oxymetazoline.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB01359; Penbutolol.
DR DrugBank; DB01186; Pergolide.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB06153; Pizotifen.
DR DrugBank; DB00571; Propranolol.
DR DrugBank; DB01224; Quetiapine.
DR DrugBank; DB00953; Rizatriptan.
DR DrugBank; DB09304; Setiptiline.
DR DrugBank; DB00669; Sumatriptan.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB09068; Vortioxetine.
DR DrugBank; DB01392; Yohimbine.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugCentral; P28222; -.
DR GuidetoPHARMACOLOGY; 2; -.
DR TCDB; 9.A.14.3.6; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P28222; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P28222; -.
DR PhosphoSitePlus; P28222; -.
DR BioMuta; HTR1B; -.
DR DMDM; 112821; -.
DR MassIVE; P28222; -.
DR PaxDb; P28222; -.
DR PeptideAtlas; P28222; -.
DR PRIDE; P28222; -.
DR ProteomicsDB; 54452; -.
DR Antibodypedia; 18374; 300 antibodies from 38 providers.
DR DNASU; 3351; -.
DR Ensembl; ENST00000369947.5; ENSP00000358963.3; ENSG00000135312.7.
DR GeneID; 3351; -.
DR KEGG; hsa:3351; -.
DR MANE-Select; ENST00000369947.5; ENSP00000358963.3; NM_000863.3; NP_000854.1.
DR CTD; 3351; -.
DR DisGeNET; 3351; -.
DR GeneCards; HTR1B; -.
DR HGNC; HGNC:5287; HTR1B.
DR HPA; ENSG00000135312; Group enriched (brain, placenta, stomach).
DR MIM; 182131; gene.
DR neXtProt; NX_P28222; -.
DR OpenTargets; ENSG00000135312; -.
DR PharmGKB; PA29549; -.
DR VEuPathDB; HostDB:ENSG00000135312; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P28222; -.
DR OMA; LIRFRCC; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; P28222; -.
DR TreeFam; TF316350; -.
DR PathwayCommons; P28222; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P28222; -.
DR SIGNOR; P28222; -.
DR BioGRID-ORCS; 3351; 14 hits in 1071 CRISPR screens.
DR GeneWiki; 5-HT1B_receptor; -.
DR GenomeRNAi; 3351; -.
DR Pharos; P28222; Tclin.
DR PRO; PR:P28222; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P28222; protein.
DR Bgee; ENSG00000135312; Expressed in popliteal artery and 91 other tissues.
DR ExpressionAtlas; P28222; baseline and differential.
DR Genevisible; P28222; HS.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0099154; C:serotonergic synapse; IEA:Ensembl.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0071312; P:cellular response to alkaloid; IDA:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR002147; 5HT1B_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF16; PTHR24247:SF16; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00513; 5HT1BRECEPTR.
DR PRINTS; PR01101; 5HTRECEPTOR.
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 3D-structure; Behavior; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..390
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068916"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT TRANSMEM 50..75
FT /note="Helical; Name=1"
FT TOPO_DOM 76..84
FT /note="Cytoplasmic"
FT TRANSMEM 85..110
FT /note="Helical; Name=2"
FT TOPO_DOM 111..123
FT /note="Extracellular"
FT TRANSMEM 124..145
FT /note="Helical; Name=3"
FT TOPO_DOM 146..165
FT /note="Cytoplasmic"
FT TRANSMEM 166..187
FT /note="Helical; Name=4"
FT TOPO_DOM 188..205
FT /note="Extracellular"
FT TRANSMEM 206..228
FT /note="Helical; Name=5"
FT TOPO_DOM 229..315
FT /note="Cytoplasmic"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT TOPO_DOM 337..349
FT /note="Extracellular"
FT TRANSMEM 350..371
FT /note="Helical; Name=7"
FT TOPO_DOM 372..390
FT /note="Cytoplasmic"
FT REGION 259..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..148
FT /note="DRY motif; important for ligand-induced conformation
FT changes and signaling"
FT MOTIF 365..369
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT BINDING 129
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519210,
FT ECO:0007744|PDB:4IAR"
FT BINDING 134
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519210,
FT ECO:0007744|PDB:4IAR"
FT BINDING 201
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:23519210,
FT ECO:0007744|PDB:4IAR"
FT SITE 355
FT /note="Important for species-specific agonist sensitivity"
FT LIPID 388
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:23519210"
FT VARIANT 124
FT /note="F -> C (in dbSNP:rs130060)"
FT /evidence="ECO:0000269|PubMed:7802650"
FT /id="VAR_011715"
FT VARIANT 219
FT /note="F -> L (in dbSNP:rs130061)"
FT /id="VAR_011831"
FT VARIANT 367
FT /note="I -> V (in dbSNP:rs130063)"
FT /id="VAR_011832"
FT VARIANT 374
FT /note="E -> K (in dbSNP:rs130064)"
FT /id="VAR_011833"
FT MUTAGEN 126
FT /note="L->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 129
FT /note="D->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 130
FT /note="I->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 133
FT /note="C->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 134
FT /note="T->A: Slightly decreases agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 200
FT /note="V->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 201
FT /note="V->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 203
FT /note="T->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 209
FT /note="T->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 212
FT /note="S->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 216
FT /note="A->S: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 327
FT /note="W->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 330
FT /note="F->A: Abolishes agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 331
FT /note="F->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 334
FT /note="S->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 337
FT /note="M->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 351
FT /note="F->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 352
FT /note="D->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 355
FT /note="T->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT MUTAGEN 359
FT /note="Y->A: No effect on agonist binding."
FT /evidence="ECO:0000269|PubMed:23519210"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 46..76
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 83..101
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 118..152
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 163..181
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 218..239
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 311..336
FT /evidence="ECO:0007829|PDB:4IAR"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:7C61"
FT HELIX 349..372
FT /evidence="ECO:0007829|PDB:4IAR"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:4IAR"
SQ SEQUENCE 390 AA; 43568 MW; CD874DC7EB44CF12 CRC64;
MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT
LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI
SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL
KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL
NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
