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 27-MAR-2024, entry version 205. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-4358; -. 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; DB12540; Lecozotan. 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 GlyCosmos; P28222; 3 sites, 1 glycan. 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; 9606-ENSP00000358963; -. DR PeptideAtlas; P28222; -. DR ProteomicsDB; 54452; -. DR Antibodypedia; 18374; 337 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 AGR; HGNC:5287; -. DR CTD; 3351; -. DR DisGeNET; 3351; -. DR GeneCards; HTR1B; -. DR HGNC; HGNC:5287; HTR1B. DR HPA; ENSG00000135312; Tissue enhanced (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; 2999405at2759; -. 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; 15 hits in 1153 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 92 other cell types or tissues. DR ExpressionAtlas; P28222; baseline and differential. 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:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. 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:1901363; F:heterocyclic compound binding; IEA:Ensembl. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0051378; F:serotonin binding; IEA:Ensembl. 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 CDD; cd15333; 7tmA_5-HT1B_1D; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24248:SF191; G-PROTEIN COUPLED RECEPTORS FAMILY 1 PROFILE DOMAIN-CONTAINING PROTEIN; 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 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. DR Genevisible; P28222; HS. 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 //