5HT1B_DIDVI
ID 5HT1B_DIDVI Reviewed; 388 AA.
AC P35404;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=8302276;
RA Cerutis D., Hass N.A., Iversen L.J., Bylund D.B.;
RT "The cloning and expression of an OK cell cDNA encoding a 5-
RT hydroxytryptamine1B receptor.";
RL Mol. Pharmacol. 45:20-28(1994).
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:8302276}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8302276};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8302276}.
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; U04311; AAA17567.1; -; mRNA.
DR AlphaFoldDB; P35404; -.
DR SMR; P35404; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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: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..388
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068913"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 75..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 110..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 145..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 165..186
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..203
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 204..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 227..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 314..334
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 335..347
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 348..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 370..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 145..147
FT /note="DRY motif; important for ligand-induced conformation
FT changes and signaling"
FT /evidence="ECO:0000250"
FT MOTIF 363..367
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 133
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 199
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT SITE 353
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 388 AA; 43111 MW; DB5E8A033325615A CRC64;
MEQPSRLCSP PASGSLTSSQ TNHSTFPNPN CSAPDLEPYQ DSIALPWKVL LATFLGLITL
GTTLSNAFVI ATVSRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV
CDFWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAGMII MVWVFSVSIS
MPPLFWRQAK AEEVADCSVN TDHILYTVYS TVGAFYFPTL LLIALYGRIY VEARSRILKQ
TPNRTGKRLT RAQLITDSPG SSSSGTSINS RAPEGPSESG SPVYVNQVKV KVSDALLEKK
KLMAARERKA TRTLGIILGA FIVCWLPFFI ISLALPICDD ACWFHLAIFD FFNWLGYLNS
LINPIIYTKS NDDFKQAFQK LMRFRRTS
