5HT1B_PIG
ID 5HT1B_PIG Reviewed; 150 AA.
AC P79399;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=5-hydroxytryptamine receptor 1B;
DE Short=5-HT-1B;
DE Short=5-HT1B;
DE AltName: Full=Serotonin receptor 1B;
DE Flags: Fragment;
GN Name=HTR1B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RA Wurch T., Lestienne F., Colpaert F.C., Pauwels P.J.;
RL Submitted (MAR-1997) 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; Y11867; CAA72615.1; -; mRNA.
DR AlphaFoldDB; P79399; -.
DR SMR; P79399; -.
DR STRING; 9823.ENSSSCP00000004826; -.
DR BindingDB; P79399; -.
DR ChEMBL; CHEMBL4104; -.
DR PaxDb; P79399; -.
DR PRIDE; P79399; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P79399; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P79399; SS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
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:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
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; 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; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Behavior; Cell membrane; G-protein coupled receptor; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..>150
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068919"
FT TOPO_DOM <1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..104
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..117
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 118..139
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..>150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..137
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 150
SQ SEQUENCE 150 AA; 16941 MW; 084EDF34A349555A CRC64;
VEARSRILKQ TPNRTGKRLT RAQLITDSPG STSSVTSINS RAPDLPSESG SPVYVNQVKV
RVSDALLEKK KLMAARERKA TKTLGIILGA FIVCWLPFFI ISLAMPICKD ACWFHLAIFD
FFTWLGYLNS LINPIIYTMF NEDFKQAFHK
