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   02-SEP-2026, entry version 104.
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; DOI=10.1016/s0026-895x(25)09899-2;
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) (PubMed:8302276). Also functions as a receptor for ergot
CC       alkaloid derivatives, various anxiolytic and antidepressant drugs and
CC       other psychoactive substances, such as lysergic acid diethylamide
CC       (LSD). Ligand binding causes a conformation change that triggers
CC       signaling via guanine nucleotide-binding proteins (G proteins) and
CC       modulates the activity of downstream effectors, such as adenylate
CC       cyclase. HTR1B is coupled to G(i)/G(o) G alpha proteins and mediates
CC       inhibitory neurotransmission by inhibiting 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).
CC       {ECO:0000250|UniProtKB:P28222, ECO:0000269|PubMed:8302276}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with HTR1D.
CC       {ECO:0000250|UniProtKB:P28222}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8302276};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC       transmembrane helices. {ECO:0000250|UniProtKB:P28222}.
CC   -!- DOMAIN: A residue in the 7th transmembrane region ('Thr-355' in human,
CC       'Asn-351' in mouse and rat) is important for species-specific
CC       sensitivity to various agonists. {ECO:0000250|UniProtKB:P28222}.
CC   -!- PTM: Phosphorylated. Desensitization of the receptor may be mediated by
CC       its phosphorylation. {ECO:0000250|UniProtKB:P28222}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P28222}.
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   GlyCosmos; P35404; 2 sites, No reported glycans.
DR   GO; GO:0005886; C:plasma membrane; EXP: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:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
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:0043410; P:positive regulation of MAPK cascade; IEA:TreeGrafter.
DR   GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
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:SF201; 5-HYDROXYTRYPTAMINE RECEPTOR 1B; 1.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 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   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..388
FT                   /note="5-hydroxytryptamine receptor 1B"
FT                   /id="PRO_0000068913"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        46..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        72..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        86..110
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        111..118
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        119..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        145..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        165..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        184..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        204..227
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        228..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        314..335
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        336..345
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TRANSMEM        346..368
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   TOPO_DOM        369..388
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
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|UniProtKB:P41595"
FT   MOTIF           363..367
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   COMPBIAS        12..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..270
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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|UniProtKB:P28222"
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
//