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5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (5-HT-2F) (Serotonin receptor 2B) (Stomach fundus serotonin receptor)

 5HT2B_RAT               Reviewed;         479 AA.
P30994; Q9QW44;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=5-hydroxytryptamine receptor 2B;
Short=5-HT-2B;
Short=5-HT2B;
AltName: Full=5-HT-2F {ECO:0000303|PubMed:1331748};
AltName: Full=Serotonin receptor 2B;
AltName: Full=Stomach fundus serotonin receptor {ECO:0000303|PubMed:1505525};
Name=Htr2b; Synonyms=Srl;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=1505525;
Foguet M., Hoyer D., Pardo L.A., Parekh A., Kluxen F.-W.,
Kalkman M.O., Stuehmer W., Luebbert H.;
"Cloning and functional characterization of the rat stomach fundus
serotonin receptor.";
EMBO J. 11:3481-3487(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Gastric fundus;
PubMed=1331748;
Kursar J.D., Nelson D.L., Wainscott D.B., Cohen M.L., Baez M.;
"Molecular cloning, functional expression, and pharmacological
characterization of a novel serotonin receptor (5-hydroxytryptamine2F)
from rat stomach fundus.";
Mol. Pharmacol. 42:549-557(1992).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22525520; DOI=10.1016/j.pain.2012.03.024;
Urtikova N., Berson N., Van Steenwinckel J., Doly S., Truchetto J.,
Maroteaux L., Pohl M., Conrath M.;
"Antinociceptive effect of peripheral serotonin 5-HT2B receptor
activation on neuropathic pain.";
Pain 153:1320-1331(2012).
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin) (PubMed:1505525, PubMed:1331748). Also functions as a
receptor for various ergot alkaloid derivatives and psychoactive
substances (PubMed:22525520). Ligand binding causes a conformation
change that triggers signaling via guanine nucleotide-binding
proteins (G proteins) and modulates the activity of down-stream
effectors (PubMed:1505525, PubMed:1331748). Beta-arrestin family
members inhibit signaling via G proteins and mediate activation of
alternative signaling pathways. Signaling activates a
phosphatidylinositol-calcium second messenger system that
modulates the activity of phosphatidylinositol 3-kinase and down-
stream signaling cascades and promotes the release of Ca(2+) ions
from intracellular stores (By similarity). Plays a role in the
regulation of dopamine and 5-hydroxytryptamine release, 5-
hydroxytryptamine uptake and in the regulation of extracellular
dopamine and 5-hydroxytryptamine levels, and thereby affects
neural activity. Plays a role in the regulation of behavior,
including impulsive behavior. Required for normal proliferation of
embryonic cardiac myocytes and normal heart development. Protects
cardiomyocytes against apoptosis. Plays a role in the adaptation
of pulmonary arteries to chronic hypoxia. Plays a role in
vasoconstriction. Required for normal osteoblast function and
proliferation, and for maintaining normal bone density. Required
for normal proliferation of the interstitial cells of Cajal in the
intestine (By similarity). May play a role in the perception of
pain (PubMed:22525520). {ECO:0000250|UniProtKB:P41595,
ECO:0000250|UniProtKB:Q02152, ECO:0000269|PubMed:1331748,
ECO:0000269|PubMed:1505525, ECO:0000269|PubMed:22525520}.
-!- SUBUNIT: Interacts (via C-terminus) with MPDZ.
{ECO:0000250|UniProtKB:P41595}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1331748,
ECO:0000269|PubMed:1505525, ECO:0000269|PubMed:22525520}; Multi-
pass membrane protein {ECO:0000269|PubMed:1505525}. Cell junction,
synapse, synaptosome {ECO:0000250|UniProtKB:Q02152}.
-!- TISSUE SPECIFICITY: Stomach fundus. {ECO:0000269|PubMed:1331748,
ECO:0000269|PubMed:1505525}.
-!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
transmembrane helices. {ECO:0000250|UniProtKB:P41595}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; X66842; CAA47318.1; -; mRNA.
PIR; S23562; S23562.
RefSeq; NP_058946.1; NM_017250.1.
UniGene; Rn.10425; -.
ProteinModelPortal; P30994; -.
BioGrid; 248214; 1.
IntAct; P30994; 1.
MINT; MINT-4000039; -.
STRING; 10116.ENSRNOP00000023829; -.
BindingDB; P30994; -.
ChEMBL; CHEMBL323; -.
GuidetoPHARMACOLOGY; 7; -.
PhosphoSitePlus; P30994; -.
PaxDb; P30994; -.
PRIDE; P30994; -.
GeneID; 29581; -.
KEGG; rno:29581; -.
UCSC; RGD:61801; rat.
CTD; 3357; -.
RGD; 61801; Htr2b.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000240378; -.
HOVERGEN; HBG107487; -.
InParanoid; P30994; -.
KO; K04157; -.
PhylomeDB; P30994; -.
PRO; PR:P30994; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0051378; F:serotonin binding; IDA:RGD.
GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0003300; P:cardiac muscle hypertrophy; ISS:UniProtKB.
GO; GO:0071418; P:cellular response to amine stimulus; IDA:RGD.
GO; GO:1904015; P:cellular response to serotonin; IDA:RGD.
GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
GO; GO:0035733; P:hepatic stellate cell activation; IEP:RGD.
GO; GO:0043647; P:inositol phosphate metabolic process; IEP:RGD.
GO; GO:0014827; P:intestine smooth muscle contraction; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:0014033; P:neural crest cell differentiation; ISS:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:UniProtKB.
GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; ISS:UniProtKB.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0050795; P:regulation of behavior; ISS:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042310; P:vasoconstriction; ISS:UniProtKB.
InterPro; IPR000482; 5HT2B_rcpt.
InterPro; IPR002231; 5HT_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24247:SF31; PTHR24247:SF31; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00651; 5HT2BRECEPTR.
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 junction; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
Membrane; Palmitate; Receptor; Reference proteome; Synapse;
Synaptosome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 479 5-hydroxytryptamine receptor 2B.
/FTId=PRO_0000068956.
TOPO_DOM 1 55 Extracellular.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 56 78 Helical; Name=1.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 79 89 Cytoplasmic.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 90 112 Helical; Name=2.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 113 128 Extracellular.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 129 150 Helical; Name=3.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 151 170 Cytoplasmic.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 171 191 Helical; Name=4.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 192 215 Extracellular.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 216 238 Helical; Name=5.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 239 323 Cytoplasmic.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 324 344 Helical; Name=6.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 345 359 Extracellular.
{ECO:0000250|UniProtKB:P41595}.
TRANSMEM 360 381 Helical; Name=7.
{ECO:0000250|UniProtKB:P41595}.
TOPO_DOM 382 479 Cytoplasmic.
{ECO:0000250|UniProtKB:P41595}.
REGION 134 139 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
REGION 336 340 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 151 153 DRY motif; important for ligand-induced
conformation changes.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 211 214 [DE]RFG motif; may stabilize a
conformation that preferentially
activates signaling via beta-arrestin
family members.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 375 379 NPxxY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 477 479 PDZ-binding.
{ECO:0000250|UniProtKB:P41595}.
SITE 208 208 Hydrophobic barrier that decreases the
speed of ligand binding and dissociation.
{ECO:0000250|UniProtKB:P41595}.
LIPID 396 396 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 127 206 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 349 352 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 281 281 V -> A (in Ref. 2). {ECO:0000305}.
CONFLICT 296 296 T -> I (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 479 AA; 53652 MW; 17FFC73213B42038 CRC64;
MASSYKMSEQ STISEHILQK TCDHLILTDR SGLKAESAAE EMKQTAENQG NTVHWAALLI
FAVIIPTIGG NILVILAVSL EKRLQYATNY FLMSLAVADL LVGLFVMPIA LLTIMFEATW
PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRTT AFVKITVVWL
ISIGIAIPVP IKGIEADVVN AHNITCELTK DRFGSFMLFG SLAAFFAPLT IMIVTYFLTI
HALRKKAYLV RNRPPQRLTR WTVSTVLQRE DSSFSSPEKM VMLDGSHKDK ILPNSTDETL
MRRMSSAGKK PAQTISNEQR ASKVLGIVFL FFLLMWCPFF ITNVTLALCD SCNQTTLKTL
LQIFVWVGYV SSGVNPLIYT LFNKTFREAF GRYITCNYQA TKSVKVLRKC SSTLYFGNSM
VENSKFFTKH GIRNGINPAM YQSPVRLRSS TIQSSSIILL NTFLTENDGD KVEDQVSYI


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