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5-hydroxytryptamine receptor 1B (5-HT-1B) (5-HT1B) (Serotonin receptor 1B)

 5HT1B_RAT               Reviewed;         386 AA.
P28564;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
10-OCT-2018, entry version 132.
RecName: Full=5-hydroxytryptamine receptor 1B;
Short=5-HT-1B;
Short=5-HT1B;
AltName: Full=Serotonin receptor 1B;
Name=Htr1b; Synonyms=5ht1b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.;
"Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and
pharmacological comparison of the two cloned receptors.";
Mol. Cell. Neurosci. 3:578-587(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=1836757;
Voigt M.M., Laurie D.J., Seeburg P.H., Bach A.;
"Molecular cloning and characterization of a rat brain cDNA encoding a
5-hydroxytryptamine1B receptor.";
EMBO J. 10:4017-4023(1991).
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin). Also functions as a receptor for various alkaloids
and psychoactive substances. Ligand binding causes a conformation
change that triggers signaling via guanine nucleotide-binding
proteins (G proteins) and modulates the activity of down-stream
effectors, such as adenylate cyclase. Signaling inhibits adenylate
cyclase activity. Arrestin family members inhibit signaling via G
proteins and mediate activation of alternative signaling pathways.
Regulates the release of 5-hydroxytryptamine, dopamine and
acetylcholine in the brain, and thereby affects neural activity,
nociceptive processing, pain perception, mood and behavior.
Besides, plays a role in vasoconstriction of cerebral arteries.
{ECO:0000269|PubMed:1836757, ECO:0000269|Ref.1}.
-!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1836757,
ECO:0000269|Ref.1}; Multi-pass membrane protein
{ECO:0000269|PubMed:1836757, ECO:0000269|Ref.1}.
-!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
transmembrane helices. {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- PTM: Palmitoylated. {ECO:0000250}.
-!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-
355' in human, Asn-351 in mouse and rat) is important for species-
specific sensitivity to various agonists. {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; M89954; AAA40613.1; -; Genomic_DNA.
EMBL; X62944; CAA44716.1; -; mRNA.
PIR; S18637; S18637.
RefSeq; NP_071561.1; NM_022225.1.
UniGene; Rn.138109; -.
ProteinModelPortal; P28564; -.
SMR; P28564; -.
STRING; 10116.ENSRNOP00000017411; -.
BindingDB; P28564; -.
ChEMBL; CHEMBL3459; -.
GuidetoPHARMACOLOGY; 2; -.
iPTMnet; P28564; -.
PhosphoSitePlus; P28564; -.
PaxDb; P28564; -.
PRIDE; P28564; -.
Ensembl; ENSRNOT00000017411; ENSRNOP00000017411; ENSRNOG00000013042.
GeneID; 25075; -.
KEGG; rno:25075; -.
UCSC; RGD:2846; rat.
CTD; 3351; -.
RGD; 2846; Htr1b.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118795; -.
HOGENOM; HOG000239242; -.
HOVERGEN; HBG106962; -.
InParanoid; P28564; -.
KO; K04153; -.
OMA; VNTDHVL; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P28564; -.
TreeFam; TF316350; -.
Reactome; R-RNO-390666; Serotonin receptors.
Reactome; R-RNO-418594; G alpha (i) signalling events.
PRO; PR:P28564; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000013042; Expressed in 8 organ(s), highest expression level in brain.
Genevisible; P28564; RN.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0099154; C:serotonergic synapse; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; IDA:RGD.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0051378; F:serotonin binding; IDA:RGD.
GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
GO; GO:0042756; P:drinking behavior; IMP:RGD.
GO; GO:0007631; P:feeding behavior; IMP:RGD.
GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl.
GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:RGD.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:RGD.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
GO; GO:0014059; P:regulation of dopamine secretion; IMP:RGD.
GO; GO:0042220; P:response to cocaine; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IMP:RGD.
GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
InterPro; IPR002147; 5HT1B_rcpt.
InterPro; IPR002231; 5HT_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24247:SF16; PTHR24247:SF16; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00513; 5HT1BRECEPTR.
PRINTS; PR01101; 5HTRECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Behavior; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 386 5-hydroxytryptamine receptor 1B.
/FTId=PRO_0000068921.
TOPO_DOM 1 45 Extracellular. {ECO:0000250}.
TRANSMEM 46 71 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 72 80 Cytoplasmic. {ECO:0000250}.
TRANSMEM 81 106 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 107 119 Extracellular. {ECO:0000250}.
TRANSMEM 120 141 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 142 161 Cytoplasmic. {ECO:0000250}.
TRANSMEM 162 183 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 184 201 Extracellular. {ECO:0000250}.
TRANSMEM 202 224 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 225 311 Cytoplasmic. {ECO:0000250}.
TRANSMEM 312 332 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 333 345 Extracellular. {ECO:0000250}.
TRANSMEM 346 367 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 368 386 Cytoplasmic. {ECO:0000250}.
REGION 121 130 Agonist binding. {ECO:0000250}.
REGION 323 327 Agonist binding. {ECO:0000250}.
MOTIF 142 144 DRY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250}.
MOTIF 361 365 NPxxY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250}.
SITE 351 351 Important for species-specific agonist
sensitivity. {ECO:0000250}.
LIPID 384 384 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 28 28 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 118 195 {ECO:0000255|PROSITE-ProRule:PRU00521}.
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


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