5HT1B_RAT
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 03-AUG-2022, entry version 151.
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). 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:1836757,
CC ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1836757,
CC ECO:0000269|Ref.1}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:1836757, ECO:0000269|Ref.1}.
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 -!- 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; M89954; AAA40613.1; -; Genomic_DNA.
DR EMBL; X62944; CAA44716.1; -; mRNA.
DR PIR; S18637; S18637.
DR RefSeq; NP_071561.1; NM_022225.1.
DR AlphaFoldDB; P28564; -.
DR SMR; P28564; -.
DR STRING; 10116.ENSRNOP00000017411; -.
DR BindingDB; P28564; -.
DR ChEMBL; CHEMBL3459; -.
DR DrugCentral; P28564; -.
DR GuidetoPHARMACOLOGY; 2; -.
DR GlyGen; P28564; 2 sites.
DR iPTMnet; P28564; -.
DR PhosphoSitePlus; P28564; -.
DR PaxDb; P28564; -.
DR Ensembl; ENSRNOT00000017411; ENSRNOP00000017411; ENSRNOG00000013042.
DR GeneID; 25075; -.
DR KEGG; rno:25075; -.
DR UCSC; RGD:2846; rat.
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; LIRFRCC; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; P28564; -.
DR TreeFam; TF316350; -.
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 tissues.
DR Genevisible; P28564; RN.
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:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA: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: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:0071502; P:cellular response to temperature stimulus; ISO:RGD.
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:0002031; P:G protein-coupled receptor internalization; ISO: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:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; 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:0009636; P:response to toxic substance; ISO:RGD.
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 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..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..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"
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; 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
