5HT1B_FELCA
ID 5HT1B_FELCA Reviewed; 389 AA.
AC Q588Y6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Asahi D., Mori Y.;
RT "Felis catus 5-hydroxytryptamine (serotonin) receptor 1B (Htr1b), mRNA.";
RL Submitted (SEP-2004) 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; AB190344; BAD93295.1; -; mRNA.
DR RefSeq; NP_001116344.1; NM_001122872.1.
DR RefSeq; XP_019685616.1; XM_019830057.1.
DR AlphaFoldDB; Q588Y6; -.
DR SMR; Q588Y6; -.
DR STRING; 9685.ENSFCAP00000007135; -.
DR Ensembl; ENSFCAT00000007706; ENSFCAP00000007135; ENSFCAG00000007703.
DR GeneID; 100144391; -.
DR KEGG; fca:100144391; -.
DR CTD; 3351; -.
DR VGNC; VGNC:67668; HTR1B.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q588Y6; -.
DR OMA; LIRFRCC; -.
DR OrthoDB; 703991at2759; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000007703; Expressed in embryo and 7 other tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0099154; C:serotonergic synapse; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
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:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
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:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
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 Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="5-hydroxytryptamine receptor 1B"
FT /id="PRO_0000068914"
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..204
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 205..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 228..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 315..335
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 336..348
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 349..370
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 371..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..281
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 364..368
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 200
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT SITE 354
FT /note="Important for species-specific agonist sensitivity"
FT /evidence="ECO:0000250"
FT LIPID 387
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 389 AA; 43372 MW; 7FEFA1C2DB097CCC CRC64;
MEETNTHCAP PPPAGSQTGV SQANLSSAPP NCSTEGYIYQ DSIALPWKVL LILVLALFTL
ATTLSNAFVI ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV
CDFWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAVMIA LVWVFSISIS
LPPFFWRQAK AEEEVSDCRV NTDHMLYTVY STVGAFYFPT LLLIALYGRI YVEARSRILK
QTPNRTGKRL TRAQLITDSP GSTSSVTSVN SRAPDVPSES GSPVYVNQVK VRVSDALLEK
KKLMAARERK ATKTLGIILG AFIVCWLPFF IISLVMPICK DACWFHLAIF DFFTWLGYLN
SLINPIIYTM SNEDFKQAFH KLIRFKCTG
