ID A0A140TAV9_RABIT Unreviewed; 389 AA.
AC A0A140TAV9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=5-hydroxytryptamine receptor 1B {ECO:0000256|ARBA:ARBA00017606, ECO:0000256|RuleBase:RU368114};
DE Short=5-HT-1B {ECO:0000256|RuleBase:RU368114};
DE Short=5-HT1B {ECO:0000256|RuleBase:RU368114};
DE AltName: Full=Serotonin receptor 1B {ECO:0000256|ARBA:ARBA00032311, ECO:0000256|RuleBase:RU368114};
GN Name=HTR1B {ECO:0000313|Ensembl:ENSOCUP00000016295.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000016295.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000016295.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000016295.1,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000016295.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000016295.1};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025144,
CC ECO:0000256|RuleBase:RU368114}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D.
CC {ECO:0000256|ARBA:ARBA00025985, ECO:0000256|RuleBase:RU368114}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU368114}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368114}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000256|RuleBase:RU368114}.
CC -!- PTM: Palmitoylated. {ECO:0000256|RuleBase:RU368114}.
CC -!- PTM: Phosphorylated. {ECO:0000256|RuleBase:RU368114}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
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DR EMBL; AAGW02018996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A140TAV9; -.
DR SMR; A0A140TAV9; -.
DR Ensembl; ENSOCUT00000009269.2; ENSOCUP00000016295.1; ENSOCUG00000009271.2.
DR GeneTree; ENSGT01010000222287; -.
DR InParanoid; A0A140TAV9; -.
DR OMA; LIRFRCC; -.
DR Proteomes; UP000001811; Chromosome 12.
DR Bgee; ENSOCUG00000009271; Expressed in upper lobe of left lung and 7 other cell types or tissues.
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:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0099154; C:serotonergic synapse; IEA:Ensembl.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051378; F:serotonin binding; IEA:Ensembl.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-UniRule.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IEA:Ensembl.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-UniRule.
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; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24248:SF66; OCTOPAMINE RECEPTOR BETA-3R; 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 3: Inferred from homology;
KW Behavior {ECO:0000256|ARBA:ARBA00022610, ECO:0000256|RuleBase:RU368114};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU368114};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Lipoprotein {ECO:0000256|RuleBase:RU368114};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368114};
KW Palmitate {ECO:0000256|RuleBase:RU368114};
KW Phosphoprotein {ECO:0000256|RuleBase:RU368114};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368114}.
FT TRANSMEM 49..73
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 85..104
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 314..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368114"
FT DOMAIN 65..368
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 259..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 43398 MW; 485DD599A37D38A2 CRC64;
MEEPSARCAP PLAGSQIAVP QANLSAAHSH NCSAEGYIYQ DSIALPWKVL LVLLLALFTL
ATTLSNAFVV ATVYRTRKLH TPANYLIASL AVTDLLVSIL VMPISTMYTV TGRWTLGQVV
CDLWLSSDIT CCTASIMHLC VIALDRYWAI TDAVEYSAKR TPKRAAIMIA LVWVFSICIS
LPPFFWRQAK AEEEVSECLV NTDHVLYTVY STVGAFYLPT LLLIALYGRI YVEARSRILK
QTPNRTGKRL TRAQLITDSP GSTTSVTSIN SRAPDVPSES GSPVYVNQVK VRVSDALLEK
KKLMAARERK ATKTLGIILG VFIVCWLPFF IISLVMPICK DACWFHQAIF DFFTWLGYVN
SLINPIIYTM SNEDFKQAFH KLIRFKCTS
//