GenomeNet

Database: UniProt
Entry: A0A140TAV9_RABIT
LinkDB: A0A140TAV9_RABIT
Original site: A0A140TAV9_RABIT 
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}.
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; 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
//
DBGET integrated database retrieval system