ID   5HT1B_RAT               Reviewed;         386 AA.
AC   P28564;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 168.
DE   RecName: Full=5-hydroxytryptamine receptor 1B;
DE            Short=5-HT-1B;
DE            Short=5-HT1B;
DE   AltName: Full=Serotonin receptor 1B;
GN   Name=Htr1b; Synonyms=5ht1b;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RA   Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.;
RT   "Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and
RT   pharmacological comparison of the two cloned receptors.";
RL   Mol. Cell. Neurosci. 3:578-587(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   PubMed=1836757; DOI=10.1002/j.1460-2075.1991.tb04977.x;
RA   Voigt M.M., Laurie D.J., Seeburg P.H., Bach A.;
RT   "Molecular cloning and characterization of a rat brain cDNA encoding a 5-
RT   hydroxytryptamine1B receptor.";
RL   EMBO J. 10:4017-4023(1991).
CC   -!- FUNCTION: G protein-coupled receptor for 5-hydroxytryptamine
CC       (serotonin) (PubMed:1836757, Ref.1). Also functions as a receptor for
CC       ergot alkaloid derivatives, various anxiolytic and antidepressant drugs
CC       and other psychoactive substances, such as lysergic acid diethylamide
CC       (LSD) (By similarity). Ligand binding causes a conformation change that
CC       triggers signaling via guanine nucleotide-binding proteins (G proteins)
CC       and modulates the activity of downstream effectors, such as adenylate
CC       cyclase (By similarity). HTR1B is coupled to G(i)/G(o) G alpha proteins
CC       and mediates inhibitory neurotransmission by inhibiting adenylate
CC       cyclase activity (By similarity). Arrestin family members inhibit
CC       signaling via G proteins and mediate activation of alternative
CC       signaling pathways (By similarity). Regulates the release of 5-
CC       hydroxytryptamine, dopamine and acetylcholine in the brain, and thereby
CC       affects neural activity, nociceptive processing, pain perception, mood
CC       and behavior (By similarity). Besides, plays a role in vasoconstriction
CC       of cerebral arteries (By similarity). {ECO:0000250|UniProtKB:P28222,
CC       ECO:0000269|PubMed:1836757, ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with HTR1D.
CC       {ECO:0000250|UniProtKB:P28222}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1836757,
CC       ECO:0000269|Ref.1}; Multi-pass membrane protein {ECO:0000255}.
CC   -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC       transmembrane helices. {ECO:0000250|UniProtKB:P28222}.
CC   -!- DOMAIN: A residue in the 7th transmembrane region ('Thr-355' in human,
CC       'Asn-351' in mouse and rat) is important for species-specific
CC       sensitivity to various agonists. {ECO:0000250|UniProtKB:P28222}.
CC   -!- PTM: Phosphorylated. Desensitization of the receptor may be mediated by
CC       its phosphorylation. {ECO:0000250|UniProtKB:P28222}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P28222}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M89954; AAA40613.1; -; Genomic_DNA.
DR   EMBL; X62944; CAA44716.1; -; mRNA.
DR   PIR; S18637; S18637.
DR   RefSeq; NP_071561.1; NM_022225.3.
DR   RefSeq; XP_063121011.1; XM_063264941.1.
DR   AlphaFoldDB; P28564; -.
DR   SMR; P28564; -.
DR   FunCoup; P28564; 1288.
DR   STRING; 10116.ENSRNOP00000017411; -.
DR   BindingDB; P28564; -.
DR   ChEMBL; CHEMBL3459; -.
DR   DrugCentral; P28564; -.
DR   GuidetoPHARMACOLOGY; 2; -.
DR   GlyCosmos; P28564; 2 sites, No reported glycans.
DR   GlyGen; P28564; 2 sites.
DR   iPTMnet; P28564; -.
DR   PhosphoSitePlus; P28564; -.
DR   PaxDb; 10116-ENSRNOP00000017411; -.
DR   Ensembl; ENSRNOT00000017411.5; ENSRNOP00000017411.1; ENSRNOG00000013042.5.
DR   Ensembl; ENSRNOT00000123084.1; ENSRNOP00000112035.1; ENSRNOG00000013042.5.
DR   Ensembl; ENSRNOT00000145729.1; ENSRNOP00000105377.1; ENSRNOG00000013042.5.
DR   Ensembl; ENSRNOT00000146843.1; ENSRNOP00000103273.1; ENSRNOG00000013042.5.
DR   Ensembl; ENSRNOT00055007617; ENSRNOP00055005736; ENSRNOG00055004785.
DR   Ensembl; ENSRNOT00055007619; ENSRNOP00055005738; ENSRNOG00055004785.
DR   GeneID; 25075; -.
DR   KEGG; rno:25075; -.
DR   UCSC; RGD:2846; rat.
DR   AGR; RGD:2846; -.
DR   CTD; 3351; -.
DR   RGD; 2846; Htr1b.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01010000222287; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; P28564; -.
DR   OMA; RFRCCRA; -.
DR   OrthoDB; 27533at9989; -.
DR   PhylomeDB; P28564; -.
DR   Reactome; R-RNO-390666; Serotonin receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:P28564; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000013042; Expressed in frontal cortex and 13 other cell types or tissues.
DR   ExpressionAtlas; P28564; baseline and differential.
DR   GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0098666; C:G protein-coupled serotonin receptor complex; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR   GO; GO:0099154; C:serotonergic synapse; ISO:RGD.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:RGD.
DR   GO; GO:0001586; F:Gi/o-coupled serotonin receptor activity; ISO:RGD.
DR   GO; GO:1901363; F:heterocyclic compound binding; IDA:RGD.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0051378; F:serotonin binding; ISO:RGD.
DR   GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0046849; P:bone remodeling; ISO:RGD.
DR   GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
DR   GO; GO:0042756; P:drinking behavior; IMP:RGD.
DR   GO; GO:0007631; P:feeding behavior; IMP:RGD.
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; IDA:CACAO.
DR   GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:RGD.
DR   GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR   GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISO:RGD.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR   GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IMP:RGD.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR   GO; GO:0042220; P:response to cocaine; IDA:RGD.
DR   GO; GO:0045471; P:response to ethanol; IMP:RGD.
DR   GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
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:SF201; 5-HYDROXYTRYPTAMINE RECEPTOR 1B; 1.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 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.
PE   2: Evidence at transcript level;
KW   Behavior; Cell membrane; Disulfide bond; G protein-coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..386
FT                   /note="5-hydroxytryptamine receptor 1B"
FT                   /id="PRO_0000068921"
FT   TOPO_DOM        1..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        43..68
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        69..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        83..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        108..115
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        116..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        142..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        162..180
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        181..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        202..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        226..311
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        312..333
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        334..343
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        344..366
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        367..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   REGION          255..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           142..144
FT                   /note="DRY motif; important for ligand-induced conformation
FT                   changes and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   MOTIF           361..365
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   COMPBIAS        255..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         130
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         197
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   SITE            351
FT                   /note="Important for species-specific agonist sensitivity"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   LIPID           384
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   386 AA;  43163 MW;  4F4E9AC1C9AED214 CRC64;
     MEEQGIQCAP PPPATSQTGV PLANLSHNCS ADDYIYQDSI ALPWKVLLVA LLALITLATT
     LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF
     WLSSDITCCT ASIMHLCVIA LDRYWAITDA VDYSAKRTPK RAAIMIVLVW VFSISISLPP
     FFWRQAKAEE EVLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP
     NKTGKRLTRA QLITDSPGST SSVTSINSRV PEVPSESGSP VYVNQVKVRV SDALLEKKKL
     MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI
     NPIIYTMSNE DFKQAFHKLI RFKCTG
//