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5-hydroxytryptamine receptor 1B (5-HT-1B) (5-HT1B) (5-HTR1B) (5-HT1D subtype beta) (Serotonin receptor 1B)

 5HT1B_CANLF             Reviewed;         389 AA.
P79250; Q6VVV0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
25-OCT-2017, entry version 99.
RecName: Full=5-hydroxytryptamine receptor 1B;
Short=5-HT-1B;
Short=5-HT1B;
Short=5-HTR1B;
AltName: Full=5-HT1D subtype beta;
AltName: Full=Serotonin receptor 1B;
Name=HTR1B;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=14729271; DOI=10.1016/j.gene.2003.10.028;
van den Berg L., Imholz S., Versteeg S.A., Leegwater P.A.J.,
Zijlstra C., Bosma A.A., van Oost B.A.;
"Isolation and characterization of the canine serotonin receptor 1B
gene (htr1B).";
Gene 326:131-139(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle;
PubMed=15353848; DOI=10.1292/jvms.66.965;
Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.;
"Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C
genes and identification of polymorphisms in the 5-HTR1B gene.";
J. Vet. Med. Sci. 66:965-972(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15220384; DOI=10.1093/jhered/esh033;
Kukekova A.V., Trut L.N., Oskina I.N., Kharlamova A.V.,
Shikhevich S.G., Kirkness E.F., Aguirre G.D., Acland G.M.;
"A marker set for construction of a genetic map of the silver fox
(Vulpes vulpes).";
J. Hered. 95:185-194(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 192-352.
STRAIN=Alsatian, and Beagle; TISSUE=Artery;
PubMed=8763409; DOI=10.1016/0008-6363(96)00014-4;
Sgard F., Faure C., Graham D.;
"Evidence for 5-HT1D beta but not 5-HT1D alpha receptor subtype
expression in canine large coronary arteries and saphenous vein.";
Cardiovasc. Res. 31:793-799(1996).
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin). Also functions as a receptor for various alkaloids
and psychoactive substances. Ligand binding causes a conformation
change that triggers signaling via guanine nucleotide-binding
proteins (G proteins) and modulates the activity of down-stream
effectors, such as adenylate cyclase. Signaling inhibits adenylate
cyclase activity. Arrestin family members inhibit signaling via G
proteins and mediate activation of alternative signaling pathways.
Regulates the release of 5-hydroxytryptamine, dopamine and
acetylcholine in the brain, and thereby affects neural activity,
nociceptive processing, pain perception, mood and behavior.
Besides, plays a role in vasoconstriction of cerebral arteries (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Heterodimer with HTR1D (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
transmembrane helices. {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- PTM: Palmitoylated. {ECO:0000250}.
-!- MISCELLANEOUS: A residue in the 7th transmembrane region ('Thr-
355' in human, 'Asn-351' in mouse and rat) is important for
species-specific sensitivity to various agonists. {ECO:0000250}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AY323909; AAQ89935.1; -; Genomic_DNA.
EMBL; AB193090; BAD60920.1; -; mRNA.
EMBL; AY204572; AAP12469.1; -; Genomic_DNA.
EMBL; S82461; AAB37488.2; -; mRNA.
RefSeq; NP_001006949.1; NM_001006948.1.
UniGene; Cfa.3604; -.
ProteinModelPortal; P79250; -.
BindingDB; P79250; -.
GeneID; 403741; -.
KEGG; cfa:403741; -.
CTD; 3351; -.
HOVERGEN; HBG106962; -.
InParanoid; P79250; -.
KO; K04153; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; ISS:UniProtKB.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0046849; P:bone remodeling; IEA:InterPro.
GO; GO:0071312; P:cellular response to alkaloid; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
GO; GO:0007631; P:feeding behavior; IEA:InterPro.
GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB.
GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
InterPro; IPR002147; 5HT1B_rcpt.
InterPro; IPR002231; 5HT_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24247:SF16; PTHR24247:SF16; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00513; 5HT1BRECEPTR.
PRINTS; PR01101; 5HTRECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Behavior; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
CHAIN 1 389 5-hydroxytryptamine receptor 1B.
/FTId=PRO_0000068910.
TOPO_DOM 1 48 Extracellular. {ECO:0000250}.
TRANSMEM 49 74 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 75 83 Cytoplasmic. {ECO:0000250}.
TRANSMEM 84 109 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 110 122 Extracellular. {ECO:0000250}.
TRANSMEM 123 144 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 145 164 Cytoplasmic. {ECO:0000250}.
TRANSMEM 165 186 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 187 204 Extracellular. {ECO:0000250}.
TRANSMEM 205 227 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 228 314 Cytoplasmic. {ECO:0000250}.
TRANSMEM 315 335 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 336 348 Extracellular. {ECO:0000250}.
TRANSMEM 349 370 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 371 389 Cytoplasmic. {ECO:0000250}.
REGION 124 133 Agonist binding. {ECO:0000250}.
REGION 326 330 Agonist binding. {ECO:0000250}.
MOTIF 145 147 DRY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250}.
MOTIF 364 368 NPxxY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250}.
SITE 354 354 Important for species-specific agonist
sensitivity. {ECO:0000250}.
LIPID 387 387 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 31 31 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 121 198 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 389 AA; 42930 MW; 4CCB4CCB5792936D CRC64;
MEAAGAPCAP PPPAGSQTGA PPANLSSAPH NCSAEGYIYQ DSVALPWKVL LVILLALITL
ATTLSNAFVI ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV
CDLWLSSDIT CCTASILHLC VIALDRYWAI TDAVEYSAKR TPKRAAVMIA LVWVFSISIS
LPPFFWRQAK AEEEVSDCVV NTDHILYTVY STVGAFYFPT LLLIALYGRI YVEARSRILK
QTPNRTGKRL TRAQLITDSP GSTSSVTSVN SRAPDVPSES GSPVYVNQVK VRVSDALLEK
KKLMAARERK ATKTLGIILG AFIVCWLPFF IISLVMPICK DACWFHLAIF DFFTWLGYLN
SLINPIIYTM SNEDFKQAFH KLIRFKCAG


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