5HT1B_CRIGR
ID 5HT1B_CRIGR Reviewed; 386 AA.
AC P46636;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung fibroblast;
RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.;
RT "Molecular cloning and expression of a Chinese hamster lung fibroblast cDNA
RT encoding a 5-HT1B receptor.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; X86458; CAA60175.1; -; mRNA.
DR PIR; S54153; S54153.
DR RefSeq; NP_001233683.1; NM_001246754.1.
DR AlphaFoldDB; P46636; -.
DR SMR; P46636; -.
DR STRING; 10029.NP_001233683.1; -.
DR BindingDB; P46636; -.
DR ChEMBL; CHEMBL3707466; -.
DR GeneID; 100689321; -.
DR KEGG; cge:100689321; -.
DR CTD; 3351; -.
DR eggNOG; KOG3656; Eukaryota.
DR OrthoDB; 703991at2759; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099154; C:serotonergic synapse; IDA:SynGO.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0046849; P:bone remodeling; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
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 Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..386
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068912"
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; 42896 MW; B0DC6211C2B6DECE CRC64;
MEEQGIQCAP PPPAASQTGV PLVNLSHNCS AESHIYQDSI ALPWKVLLVA LLALITLATT
LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP VSTMYTVTGR WTLGQVVCDF
WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYAAKRTPK RAAIMIALVW VFSISISLPP
FFWRQAKAEE EVLTCLVNTD HVLYTVYSTG GAFYLPTLLL IALYGRIYVE ARSRILKQTP
NKTGKRLTRA QLITDSPGST TSVTSINSRA PDLPSESGSP VYVNQVKVRV SDALLEKKKL
MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMATLDFF NWLGYLNSLI
NPIIYTMSNE DFKQAFHKLI RFKCAG
