5HT1B_GORGO
ID 5HT1B_GORGO Reviewed; 390 AA.
AC Q9N2B7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB041372; BAA94457.1; -; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000019686; -.
DR BindingDB; Q9N2B7; -.
DR ChEMBL; CHEMBL2304408; -.
DR DrugCentral; Q9N2B7; -.
DR PRIDE; Q9N2B7; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9N2B7; -.
DR Proteomes; UP000001519; Unplaced.
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; 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 3: Inferred from homology;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..390
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068915"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 76..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 85..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..123
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 124..145
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 166..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..205
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 206..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 229..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 337..349
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 350..371
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 372..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 146..148
FT /note="DRY motif; important for ligand-induced conformation
FT changes and signaling"
FT /evidence="ECO:0000250"
FT MOTIF 365..369
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 134
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 201
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT SITE 355
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT LIPID 388
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 390 AA; 43566 MW; 37D54B95E3277FC3 CRC64;
MEEPGAQCAP PXPAGSETWV PQANLSSAPS QNCSAKDYIY QDSIALPWKV LLVMLLALIT
LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV
VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI
SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL
KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE
KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL
NSLINPIIYT MSNEDFKQAF HKLIRFKCTS
