ID 5HT1B_MOUSE Reviewed; 386 AA.
AC P28334;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 27-MAR-2024, entry version 169.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=1557407; DOI=10.1073/pnas.89.7.3020;
RA Maroteaux L., Saudou F., Amlaiky N., Boschert U., Plassat J.-L., Hen R.;
RT "Mouse 5HT1B serotonin receptor: cloning, functional expression, and
RT localization in motor control centers.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3020-3024(1992).
RN [2]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8091214; DOI=10.1126/science.8091214;
RA Saudou F., Amara D.A., Dierich A., LeMeur M., Ramboz S., Segu L.,
RA Buhot M.C., Hen R.;
RT "Enhanced aggressive behavior in mice lacking 5-HT1B receptor.";
RL Science 265:1875-1878(1994).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8742487;
RA Pineyro G., Castanon N., Hen R., Blier P.;
RT "Regulation of [3H]5-HT release in raphe, frontal cortex and hippocampus of
RT 5-HT1B knock-out mice.";
RL NeuroReport 7:353-359(1995).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9349547; DOI=10.1046/j.1471-4159.1997.69052019.x;
RA Trillat A.C., Malagie I., Scearce K., Pons D., Anmella M.C., Jacquot C.,
RA Hen R., Gardier A.M.;
RT "Regulation of serotonin release in the frontal cortex and ventral
RT hippocampus of homozygous mice lacking 5-HT1B receptors: in vivo
RT microdialysis studies.";
RL J. Neurochem. 69:2019-2025(1997).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=10651141; DOI=10.1007/s002109900163;
RA Sarhan H., Grimaldi B., Hen R., Fillion G.;
RT "5-HT1B receptors modulate release of [3H]dopamine from rat striatal
RT synaptosomes: further evidence using 5-HT moduline, polyclonal 5-HT1B
RT receptor antibodies and 5-HT1B receptor knock-out mice.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 361:12-18(2000).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16750486; DOI=10.1016/j.brainresbull.2006.04.004;
RA Rutz S., Riegert C., Rothmaier A.K., Buhot M.C., Cassel J.C., Jackisch R.;
RT "Presynaptic serotonergic modulation of 5-HT and acetylcholine release in
RT the hippocampus and the cortex of 5-HT1B-receptor knockout mice.";
RL Brain Res. Bull. 70:81-93(2006).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids and
CC psychoactive substances. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC Arrestin family members inhibit signaling via G proteins and mediate
CC activation of alternative signaling pathways. Regulates the release of
CC 5-hydroxytryptamine, dopamine and acetylcholine in the brain, and
CC thereby affects neural activity, nociceptive processing, pain
CC perception, mood and behavior. Besides, plays a role in
CC vasoconstriction of cerebral arteries. {ECO:0000269|PubMed:10651141,
CC ECO:0000269|PubMed:1557407, ECO:0000269|PubMed:16750486,
CC ECO:0000269|PubMed:8091214, ECO:0000269|PubMed:8742487,
CC ECO:0000269|PubMed:9349547}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1557407};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1557407}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in striatum and Purkinje
CC cells. {ECO:0000269|PubMed:1557407}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant male mice display increased aggressivity
CC towards intruders. Treatment with a Htr1b agonist does not trigger
CC increased locomotor behavior in mutant mice, contrary to what is
CC observed with wild-type mice. Treatment with a Htr1b agonist does not
CC inhibit 5-hydroxytryptamine release in the frontal cortex and
CC hippocampus of mutant mice, contrary to what is observed with wild-type
CC mice. Likewise, Htr1b agonists do not inhibit dopamine and
CC acetylcholine release in brains from mutant mice.
CC {ECO:0000269|PubMed:10651141, ECO:0000269|PubMed:16750486,
CC ECO:0000269|PubMed:8091214, ECO:0000269|PubMed:8742487,
CC ECO:0000269|PubMed:9349547}.
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. {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; Z11597; CAA77678.1; -; Genomic_DNA.
DR EMBL; M85151; AAA83221.1; -; Genomic_DNA.
DR CCDS; CCDS23370.1; -.
DR PIR; A42688; A42688.
DR RefSeq; NP_034612.1; NM_010482.1.
DR AlphaFoldDB; P28334; -.
DR SMR; P28334; -.
DR STRING; 10090.ENSMUSP00000139389; -.
DR BindingDB; P28334; -.
DR ChEMBL; CHEMBL3708691; -.
DR DrugCentral; P28334; -.
DR GuidetoPHARMACOLOGY; 2; -.
DR GlyCosmos; P28334; 2 sites, No reported glycans.
DR GlyGen; P28334; 2 sites.
DR iPTMnet; P28334; -.
DR PhosphoSitePlus; P28334; -.
DR PaxDb; 10090-ENSMUSP00000139389; -.
DR ProteomicsDB; 285572; -.
DR Antibodypedia; 18374; 337 antibodies from 38 providers.
DR DNASU; 15551; -.
DR Ensembl; ENSMUST00000051005.5; ENSMUSP00000050898.5; ENSMUSG00000049511.6.
DR Ensembl; ENSMUST00000183482.2; ENSMUSP00000139389.2; ENSMUSG00000049511.6.
DR GeneID; 15551; -.
DR KEGG; mmu:15551; -.
DR UCSC; uc009qvl.1; mouse.
DR AGR; MGI:96274; -.
DR CTD; 3351; -.
DR MGI; MGI:96274; Htr1b.
DR VEuPathDB; HostDB:ENSMUSG00000049511; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P28334; -.
DR OMA; LIRFRCC; -.
DR OrthoDB; 2999405at2759; -.
DR PhylomeDB; P28334; -.
DR TreeFam; TF316350; -.
DR Reactome; R-MMU-390666; Serotonin receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 15551; 2 hits in 78 CRISPR screens.
DR PRO; PR:P28334; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P28334; Protein.
DR Bgee; ENSMUSG00000049511; Expressed in caudate-putamen and 145 other cell types or tissues.
DR ExpressionAtlas; P28334; baseline and differential.
DR Genevisible; P28334; MM.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR GO; GO:0099154; C:serotonergic synapse; IDA:SynGO.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:UniProtKB.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046849; P:bone remodeling; IGI:MGI.
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0042756; P:drinking behavior; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; ISO:MGI.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IMP:UniProtKB.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:MGI.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR GO; GO:0045471; P:response to ethanol; ISO:MGI.
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.
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_0000068917"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 46..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..119
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 142..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..201
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 202..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..332
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 333..345
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 346..367
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 368..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 255..278
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"
FT MOTIF 361..365
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
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"
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; 43079 MW; 58F70FBEA770C0B3 CRC64;
MEEQGIQCAP PPPAASQTGV PLTNLSHNCS ADGYIYQDSI ALPWKVLLVA LLALITLATT
LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF
WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYSAKRTPK RAAIMIVLVW VFSISISLPP
FFWRQAKAEE EMLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP
NKTGKRLTRA QLITDSPGST SSVTSINSRA PDVPSESGSP VYVNQVKVRV SDALLEKKKL
MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI
NPIIYTMSNE DFKQAFHKLI RFKCAG
//
