5HT2B_MOUSE
ID 5HT2B_MOUSE Reviewed; 479 AA.
AC Q02152; Q8JZK5; Q9QWS2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=5-hydroxytryptamine receptor 2B;
DE Short=5-HT-2B;
DE Short=5-HT2B;
DE AltName: Full=5-HT-2F;
DE AltName: Full=NP75 protein;
DE AltName: Full=Serotonin receptor 2B;
GN Name=Htr2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1426253; DOI=10.1016/0014-5793(92)80936-b;
RA Loric S., Launay J.-M., Colas J.-F., Maroteaux L.;
RT "New mouse 5-HT2-like receptor. Expression in brain, heart and intestine.";
RL FEBS Lett. 312:203-207(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Choi D.S., Maroteaux L.;
RT "Genomic sequence of the 5-HT2B receptor locus.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10944220; DOI=10.1073/pnas.97.17.9508;
RA Nebigil C.G., Choi D.S., Dierich A., Hickel P., Le Meur M., Messaddeq N.,
RA Launay J.M., Maroteaux L.;
RT "Serotonin 2B receptor is required for heart development.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9508-9513(2000).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11413089; DOI=10.1161/01.cir.103.24.2973;
RA Nebigil C.G., Hickel P., Messaddeq N., Vonesch J.L., Douchet M.P.,
RA Monassier L., Gyorgy K., Matz R., Andriantsitohaina R., Manivet P.,
RA Launay J.M., Maroteaux L.;
RT "Ablation of serotonin 5-HT(2B) receptors in mice leads to abnormal cardiac
RT structure and function.";
RL Circulation 103:2973-2979(2001).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12244304; DOI=10.1038/nm764;
RA Launay J.M., Herve P., Peoc'h K., Tournois C., Callebert J., Nebigil C.G.,
RA Etienne N., Drouet L., Humbert M., Simonneau G., Maroteaux L.;
RT "Function of the serotonin 5-hydroxytryptamine 2B receptor in pulmonary
RT hypertension.";
RL Nat. Med. 8:1129-1135(2002).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12738797; DOI=10.1096/fj.02-1122fje;
RA Nebigil C.G., Etienne N., Messaddeq N., Maroteaux L.;
RT "Serotonin is a novel survival factor of cardiomyocytes: mitochondria as a
RT target of 5-HT2B receptor signaling.";
RL FASEB J. 17:1373-1375(2003).
RN [10]
RP FUNCTION.
RX PubMed=16940156; DOI=10.1096/fj.06-5724com;
RA Launay J.M., Schneider B., Loric S., Da Prada M., Kellermann O.;
RT "Serotonin transport and serotonin transporter-mediated antidepressant
RT recognition are controlled by 5-HT2B receptor signaling in serotonergic
RT neuronal cells.";
RL FASEB J. 20:1843-1854(2006).
RN [11]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17846081; DOI=10.1096/fj.07-9209com;
RA Collet C., Schiltz C., Geoffroy V., Maroteaux L., Launay J.M.,
RA de Vernejoul M.C.;
RT "The serotonin 5-HT2B receptor controls bone mass via osteoblast
RT recruitment and proliferation.";
RL FASEB J. 22:418-427(2008).
RN [12]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18337424; DOI=10.1523/jneurosci.5723-07.2008;
RA Doly S., Valjent E., Setola V., Callebert J., Herve D., Launay J.M.,
RA Maroteaux L.;
RT "Serotonin 5-HT2B receptors are required for 3,4-
RT methylenedioxymethamphetamine-induced hyperlocomotion and 5-HT release in
RT vivo and in vitro.";
RL J. Neurosci. 28:2933-2940(2008).
RN [13]
RP INVOLVEMENT IN IMPULSIVE BEHAVIOR, AND FUNCTION.
RX PubMed=21179162; DOI=10.1038/nature09629;
RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A.,
RA Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L.,
RA Virkkunen M., Goldman D.;
RT "A population-specific HTR2B stop codon predisposes to severe
RT impulsivity.";
RL Nature 468:1061-1066(2010).
RN [14]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19941613; DOI=10.1111/j.1365-2982.2009.01435.x;
RA Tharayil V.S., Wouters M.M., Stanich J.E., Roeder J.L., Lei S., Beyder A.,
RA Gomez-Pinilla P.J., Gershon M.D., Maroteaux L., Gibbons S.J., Farrugia G.;
RT "Lack of serotonin 5-HT2B receptor alters proliferation and network volume
RT of interstitial cells of Cajal in vivo.";
RL Neurogastroenterol. Motil. 22:462-469(2010).
RN [15]
RP TISSUE SPECIFICITY, AND POSSIBLE FUNCTION IN PAIN PERCEPTION.
RX PubMed=21273425; DOI=10.1523/jneurosci.4682-10.2011;
RA Lin S.Y., Chang W.J., Lin C.S., Huang C.Y., Wang H.F., Sun W.H.;
RT "Serotonin receptor 5-HT2B mediates serotonin-induced mechanical
RT hyperalgesia.";
RL J. Neurosci. 31:1410-1418(2011).
RN [16]
RP FUNCTION.
RX PubMed=23346101; DOI=10.1155/2012/398406;
RA Nelson P.M., Harrod J.S., Lamping K.G.;
RT "5HT(2A) and 5HT(2B) receptors contribute to serotonin-induced vascular
RT dysfunction in diabetes.";
RL Exp. Diabetes Res. 2012:398406-398406(2012).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin) (PubMed:1426253). Also functions as a receptor for various
CC ergot alkaloid derivatives and psychoactive substances (PubMed:1426253,
CC PubMed:16940156). Ligand binding causes a conformation change that
CC triggers signaling via guanine nucleotide-binding proteins (G proteins)
CC and modulates the activity of downstream effectors. Beta-arrestin
CC family members inhibit signaling via G proteins and mediate activation
CC of alternative signaling pathways. Signaling activates a
CC phosphatidylinositol-calcium second messenger system that modulates the
CC activity of phosphatidylinositol 3-kinase and downstream signaling
CC cascades and promotes the release of Ca(2+) ions from intracellular
CC stores (By similarity). Plays a role in the regulation of dopamine and
CC 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the
CC regulation of extracellular dopamine and 5-hydroxytryptamine levels,
CC and thereby affects neural activity (PubMed:16940156, PubMed:18337424).
CC May play a role in the perception of pain (PubMed:21273425). Plays a
CC role in the regulation of behavior, including impulsive behavior
CC (PubMed:21179162). Required for normal proliferation of embryonic
CC cardiac myocytes and normal heart development (PubMed:10944220,
CC PubMed:11413089). Protects cardiomyocytes against apoptosis
CC (PubMed:12738797). Plays a role in the adaptation of pulmonary arteries
CC to chronic hypoxia (PubMed:12244304). Plays a role in vasoconstriction
CC (PubMed:12244304, PubMed:23346101). Required for normal osteoblast
CC function and proliferation, and for maintaining normal bone density
CC (PubMed:17846081). Required for normal proliferation of the
CC interstitial cells of Cajal in the intestine (PubMed:19941613).
CC {ECO:0000250|UniProtKB:P41595, ECO:0000269|PubMed:10944220,
CC ECO:0000269|PubMed:11413089, ECO:0000269|PubMed:12244304,
CC ECO:0000269|PubMed:12738797, ECO:0000269|PubMed:1426253,
CC ECO:0000269|PubMed:16940156, ECO:0000269|PubMed:17846081,
CC ECO:0000269|PubMed:18337424, ECO:0000269|PubMed:19941613,
CC ECO:0000269|PubMed:21179162, ECO:0000269|PubMed:21273425,
CC ECO:0000269|PubMed:23346101}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MPDZ.
CC {ECO:0000250|UniProtKB:P41595}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1426253};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P41595}. Synapse,
CC synaptosome {ECO:0000269|PubMed:18337424}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in intestine, heart, skeletal
CC muscle, testis, urinary bladder, stomach, liver, lung, brain and
CC kidney. Detected in osteoblasts. Detected in the raphe nucleus in the
CC brain, in dorsal root ganglion neurons, the brain stem, cerebellum and
CC spinal cord. Detected in interstitial cells of Cajal in the small
CC intestine. {ECO:0000269|PubMed:10944220, ECO:0000269|PubMed:1426253,
CC ECO:0000269|PubMed:17846081, ECO:0000269|PubMed:18337424,
CC ECO:0000269|PubMed:19941613, ECO:0000269|PubMed:21273425}.
CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
CC transmembrane helices. {ECO:0000250|UniProtKB:P41595}.
CC -!- DISRUPTION PHENOTYPE: Partial embryonic and perinatal lethality, due to
CC heart ventricle hypoplasia and impaired proliferative capacity of heart
CC myocytes. Mutant mice that survive into adulthood have a decreased
CC heart weight relative to body weight. They display dilated
CC cardiomyopathy with a loss of ventricular mass, due to a reduction in
CC the number and size of cardiomyocytes. The myocardium from mutant mice
CC displays abnormal organization of the contractile elements, with an
CC irregular array of sarcomeric myofibrils and abnormally wide Z bands.
CC In addition, heart muscle mitochondria display structural and
CC functional defects. Mutant mice do not respond to chronic exposure to
CC low oxygen levels by remodeling of their lung arteries, unlike wild-
CC type mice, and as a consequence, do not develop increased right
CC ventricular systolic pressure in response to chronic hypoxia. Adult
CC mutant female mice display reduced bone density that worsens with age.
CC Osteopenia is due to reduced proliferation and delayed differentiation
CC of osteoblasts and reduced calcium incorporation by osteoblasts
CC (PubMed:17846081). In addition, mutant mice display a reduced number of
CC proliferating interstitial cells of Cajal in the myenteric plexus in
CC jejunum muscle, and a reduced number of interstitial cells of Cajal in
CC the deep muscular plexus (PubMed:19941613). Mutant mice also show
CC increased locomotor activity in a novel environment, compared to the
CC wild-type. Unlike the wild-type, they do not respond to the drug 3,4-
CC methylenedioxymethamphetamine with increased locomotion and increased
CC 5-hydroxytryptamine and dopamine levels in the brain (PubMed:18337424).
CC {ECO:0000269|PubMed:10944220, ECO:0000269|PubMed:11413089,
CC ECO:0000269|PubMed:12244304, ECO:0000269|PubMed:12738797,
CC ECO:0000269|PubMed:17846081, ECO:0000269|PubMed:18337424,
CC ECO:0000269|PubMed:19941613}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78824.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z15119; CAA78824.1; ALT_SEQ; mRNA.
DR EMBL; AJ012488; CAA10051.1; -; Genomic_DNA.
DR EMBL; AF498254; AAM22971.1; -; mRNA.
DR EMBL; AF498255; AAM22972.1; -; mRNA.
DR EMBL; AK033713; BAC28441.1; -; mRNA.
DR EMBL; BC023690; AAH23690.1; -; mRNA.
DR CCDS; CCDS35644.1; -.
DR PIR; S27269; S27269.
DR RefSeq; NP_032337.2; NM_008311.2.
DR RefSeq; XP_006529210.1; XM_006529147.2.
DR AlphaFoldDB; Q02152; -.
DR SMR; Q02152; -.
DR STRING; 10090.ENSMUSP00000027431; -.
DR BindingDB; Q02152; -.
DR ChEMBL; CHEMBL2583; -.
DR DrugCentral; Q02152; -.
DR GlyGen; Q02152; 1 site.
DR iPTMnet; Q02152; -.
DR PhosphoSitePlus; Q02152; -.
DR PaxDb; Q02152; -.
DR PRIDE; Q02152; -.
DR Antibodypedia; 2921; 402 antibodies from 33 providers.
DR DNASU; 15559; -.
DR Ensembl; ENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
DR GeneID; 15559; -.
DR KEGG; mmu:15559; -.
DR UCSC; uc007buz.1; mouse.
DR CTD; 3357; -.
DR MGI; MGI:109323; Htr2b.
DR VEuPathDB; HostDB:ENSMUSG00000026228; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244937; -.
DR HOGENOM; CLU_009579_11_3_1; -.
DR InParanoid; Q02152; -.
DR OMA; TYFLTIQ; -.
DR OrthoDB; 962038at2759; -.
DR PhylomeDB; Q02152; -.
DR TreeFam; TF316350; -.
DR Reactome; R-MMU-390666; Serotonin receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 15559; 0 hits in 59 CRISPR screens.
DR PRO; PR:Q02152; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q02152; protein.
DR Bgee; ENSMUSG00000026228; Expressed in decidua and 67 other tissues.
DR ExpressionAtlas; Q02152; baseline and differential.
DR Genevisible; Q02152; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0071418; P:cellular response to amine stimulus; ISO:MGI.
DR GO; GO:1904015; P:cellular response to serotonin; ISO:MGI.
DR GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0002031; P:G protein-coupled receptor internalization; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0014827; P:intestine smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0014033; P:neural crest cell differentiation; IMP:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:UniProtKB.
DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0042310; P:vasoconstriction; ISS:UniProtKB.
DR InterPro; IPR000482; 5HT2B_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF31; PTHR24247:SF31; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00651; 5HT2BRECEPTR.
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 1: Evidence at protein level;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW Reference proteome; Synapse; Synaptosome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="5-hydroxytryptamine receptor 2B"
FT /id="PRO_0000068954"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 56..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 79..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 90..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 113..128
FT /note="Extracellular"
FT /evidence="ECO:0000250, ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 129..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 151..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 171..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 192..215
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 216..238
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 239..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 324..344
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 345..359
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TRANSMEM 360..381
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT TOPO_DOM 382..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 151..153
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 211..214
FT /note="[DE]RFG motif; may stabilize a conformation that
FT preferentially activates signaling via beta-arrestin family
FT members"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 375..379
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT MOTIF 477..479
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 134
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 139
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 208
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT SITE 208
FT /note="Hydrophobic barrier that decreases the speed of
FT ligand binding and dissociation"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT LIPID 396
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 349..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 167
FT /note="S -> T (in Ref. 1; CAA78824)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> V (in Ref. 1; CAA78824 and 2; CAA10051)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="S -> C (in Ref. 1; CAA78824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53597 MW; F02B30D80C8C9B6D CRC64;
MASSYKMSEQ STTSEHILQK TCDHLILTNR SGLETDSVAE EMKQTVEGQG HTVHWAALLI
LAVIIPTIGG NILVILAVAL EKRLQYATNY FLMSLAIADL LVGLFVMPIA LLTIMFEAIW
PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRAT AFIKITVVWL
ISIGIAIPVP IKGIETDVIN PHNVTCELTK DRFGSFMVFG SLAAFFAPLT IMVVTYFLTI
HTLQKKAYLV KNKPPQRLTR WTVPTVFLRE DSSFSSPEKV AMLDGSHRDK ILPNSSDETL
MRRMSSVGKR SAQTISNEQR ASKALGVVFF LFLLMWCPFF ITNLTLALCD SCNQTTLKTL
LEIFVWIGYV SSGVNPLIYT LFNKTFREAF GRYITCNYRA TKSVKALRKF SSTLCFGNSM
VENSKFFTKH GIRNGINPAM YQSPMRLRSS TIQSSSIILL DTLLTENDGD KAEEQVSYI
