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5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (5-HT-2F) (NP75 protein) (Serotonin receptor 2B)

 5HT2B_MOUSE             Reviewed;         479 AA.
Q02152; Q8JZK5; Q9QWS2;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 3.
10-OCT-2018, entry version 164.
RecName: Full=5-hydroxytryptamine receptor 2B;
Short=5-HT-2B;
Short=5-HT2B;
AltName: Full=5-HT-2F;
AltName: Full=NP75 protein;
AltName: Full=Serotonin receptor 2B;
Name=Htr2b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=1426253; DOI=10.1016/0014-5793(92)80936-B;
Loric S., Launay J.-M., Colas J.-F., Maroteaux L.;
"New mouse 5-HT2-like receptor. Expression in brain, heart and
intestine.";
FEBS Lett. 312:203-207(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
Choi D.S., Maroteaux L.;
"Genomic sequence of the 5-HT2B receptor locus.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ILS, and ISS;
PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
"High-throughput sequence identification of gene coding variants
within alcohol-related QTLs.";
Mamm. Genome 12:657-663(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10944220; DOI=10.1073/pnas.97.17.9508;
Nebigil C.G., Choi D.S., Dierich A., Hickel P., Le Meur M.,
Messaddeq N., Launay J.M., Maroteaux L.;
"Serotonin 2B receptor is required for heart development.";
Proc. Natl. Acad. Sci. U.S.A. 97:9508-9513(2000).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11413089; DOI=10.1161/01.CIR.103.24.2973;
Nebigil C.G., Hickel P., Messaddeq N., Vonesch J.L., Douchet M.P.,
Monassier L., Gyorgy K., Matz R., Andriantsitohaina R., Manivet P.,
Launay J.M., Maroteaux L.;
"Ablation of serotonin 5-HT(2B) receptors in mice leads to abnormal
cardiac structure and function.";
Circulation 103:2973-2979(2001).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12244304; DOI=10.1038/nm764;
Launay J.M., Herve P., Peoc'h K., Tournois C., Callebert J.,
Nebigil C.G., Etienne N., Drouet L., Humbert M., Simonneau G.,
Maroteaux L.;
"Function of the serotonin 5-hydroxytryptamine 2B receptor in
pulmonary hypertension.";
Nat. Med. 8:1129-1135(2002).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12738797; DOI=10.1096/fj.02-1122fje;
Nebigil C.G., Etienne N., Messaddeq N., Maroteaux L.;
"Serotonin is a novel survival factor of cardiomyocytes: mitochondria
as a target of 5-HT2B receptor signaling.";
FASEB J. 17:1373-1375(2003).
[10]
FUNCTION.
PubMed=16940156; DOI=10.1096/fj.06-5724com;
Launay J.M., Schneider B., Loric S., Da Prada M., Kellermann O.;
"Serotonin transport and serotonin transporter-mediated antidepressant
recognition are controlled by 5-HT2B receptor signaling in
serotonergic neuronal cells.";
FASEB J. 20:1843-1854(2006).
[11]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17846081; DOI=10.1096/fj.07-9209com;
Collet C., Schiltz C., Geoffroy V., Maroteaux L., Launay J.M.,
de Vernejoul M.C.;
"The serotonin 5-HT2B receptor controls bone mass via osteoblast
recruitment and proliferation.";
FASEB J. 22:418-427(2008).
[12]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=18337424; DOI=10.1523/JNEUROSCI.5723-07.2008;
Doly S., Valjent E., Setola V., Callebert J., Herve D., Launay J.M.,
Maroteaux L.;
"Serotonin 5-HT2B receptors are required for 3,4-
methylenedioxymethamphetamine-induced hyperlocomotion and 5-HT release
in vivo and in vitro.";
J. Neurosci. 28:2933-2940(2008).
[13]
INVOLVEMENT IN IMPULSIVE BEHAVIOR, AND FUNCTION.
PubMed=21179162; DOI=10.1038/nature09629;
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A.,
Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J.,
Peltonen L., Virkkunen M., Goldman D.;
"A population-specific HTR2B stop codon predisposes to severe
impulsivity.";
Nature 468:1061-1066(2010).
[14]
DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19941613; DOI=10.1111/j.1365-2982.2009.01435.x;
Tharayil V.S., Wouters M.M., Stanich J.E., Roeder J.L., Lei S.,
Beyder A., Gomez-Pinilla P.J., Gershon M.D., Maroteaux L.,
Gibbons S.J., Farrugia G.;
"Lack of serotonin 5-HT2B receptor alters proliferation and network
volume of interstitial cells of Cajal in vivo.";
Neurogastroenterol. Motil. 22:462-469(2010).
[15]
TISSUE SPECIFICITY, AND POSSIBLE FUNCTION IN PAIN PERCEPTION.
PubMed=21273425; DOI=10.1523/JNEUROSCI.4682-10.2011;
Lin S.Y., Chang W.J., Lin C.S., Huang C.Y., Wang H.F., Sun W.H.;
"Serotonin receptor 5-HT2B mediates serotonin-induced mechanical
hyperalgesia.";
J. Neurosci. 31:1410-1418(2011).
[16]
FUNCTION.
PubMed=23346101; DOI=10.1155/2012/398406;
Nelson P.M., Harrod J.S., Lamping K.G.;
"5HT(2A) and 5HT(2B) receptors contribute to serotonin-induced
vascular dysfunction in diabetes.";
Exp. Diabetes Res. 2012:398406-398406(2012).
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin) (PubMed:1426253). Also functions as a receptor for
various ergot alkaloid derivatives and psychoactive substances
(PubMed:1426253, PubMed:16940156). Ligand binding causes a
conformation change that triggers signaling via guanine
nucleotide-binding proteins (G proteins) and modulates the
activity of downstream effectors. 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
downstream 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 (PubMed:16940156, PubMed:18337424). May play a
role in the perception of pain (PubMed:21273425). Plays a role in
the regulation of behavior, including impulsive behavior
(PubMed:21179162). Required for normal proliferation of embryonic
cardiac myocytes and normal heart development (PubMed:10944220,
PubMed:11413089). Protects cardiomyocytes against apoptosis
(PubMed:12738797). Plays a role in the adaptation of pulmonary
arteries to chronic hypoxia (PubMed:12244304). Plays a role in
vasoconstriction (PubMed:12244304, PubMed:23346101). Required for
normal osteoblast function and proliferation, and for maintaining
normal bone density (PubMed:17846081). Required for normal
proliferation of the interstitial cells of Cajal in the intestine
(PubMed:19941613). {ECO:0000250|UniProtKB:P41595,
ECO:0000269|PubMed:10944220, ECO:0000269|PubMed:11413089,
ECO:0000269|PubMed:12244304, ECO:0000269|PubMed:12738797,
ECO:0000269|PubMed:1426253, ECO:0000269|PubMed:16940156,
ECO:0000269|PubMed:17846081, ECO:0000269|PubMed:18337424,
ECO:0000269|PubMed:19941613, ECO:0000269|PubMed:21179162,
ECO:0000269|PubMed:21273425, ECO:0000269|PubMed:23346101}.
-!- SUBUNIT: Interacts (via C-terminus) with MPDZ.
{ECO:0000250|UniProtKB:P41595}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1426253};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P41595}. Cell
junction, synapse, synaptosome {ECO:0000269|PubMed:18337424}.
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in intestine, heart,
skeletal muscle, testis, urinary bladder, stomach, liver, lung,
brain and kidney. Detected in osteoblasts. Detected in the raphe
nucleus in the brain, in dorsal root ganglion neurons, the brain
stem, cerebellum and spinal cord. Detected in interstitial cells
of Cajal in the small intestine. {ECO:0000269|PubMed:10944220,
ECO:0000269|PubMed:1426253, ECO:0000269|PubMed:17846081,
ECO:0000269|PubMed:18337424, ECO:0000269|PubMed:19941613,
ECO:0000269|PubMed:21273425}.
-!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the
transmembrane helices. {ECO:0000250|UniProtKB:P41595}.
-!- DISRUPTION PHENOTYPE: Partial embryonic and perinatal lethality,
due to heart ventricle hypoplasia and impaired proliferative
capacity of heart myocytes. Mutant mice that survive into
adulthood have a decreased heart weight relative to body weight.
They display dilated cardiomyopathy with a loss of ventricular
mass, due to a reduction in the number and size of cardiomyocytes.
The myocardium from mutant mice displays abnormal organization of
the contractile elements, with an irregular array of sarcomeric
myofibrils and abnormally wide Z bands. In addition, heart muscle
mitochondria display structural and functional defects. Mutant
mice do not respond to chronic exposure to low oxygen levels by
remodeling of their lung arteries, unlike wild-type mice, and as a
consequence, do not develop increased right ventricular systolic
pressure in response to chronic hypoxia. Adult mutant female mice
display reduced bone density that worsens with age. Osteopenia is
due to reduced proliferation and delayed differentiation of
osteoblasts and reduced calcium incorporation by osteoblasts
(PubMed:17846081). In addition, mutant mice display a reduced
number of proliferating interstitial cells of Cajal in the
myenteric plexus in jejunum muscle, and a reduced number of
interstitial cells of Cajal in the deep muscular plexus
(PubMed:19941613). Mutant mice also show increased locomotor
activity in a novel environment, compared to the wild-type. Unlike
the wild-type, they do not respond to the drug 3,4-
methylenedioxymethamphetamine with increased locomotion and
increased 5-hydroxytryptamine and dopamine levels in the brain
(PubMed:18337424). {ECO:0000269|PubMed:10944220,
ECO:0000269|PubMed:11413089, ECO:0000269|PubMed:12244304,
ECO:0000269|PubMed:12738797, ECO:0000269|PubMed:17846081,
ECO:0000269|PubMed:18337424, ECO:0000269|PubMed:19941613}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=CAA78824.1; Type=Erroneous termination; Positions=480; Note=Translated as stop.; Evidence={ECO:0000305};
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EMBL; Z15119; CAA78824.1; ALT_SEQ; mRNA.
EMBL; AJ012488; CAA10051.1; -; Genomic_DNA.
EMBL; AF498254; AAM22971.1; -; mRNA.
EMBL; AF498255; AAM22972.1; -; mRNA.
EMBL; AK033713; BAC28441.1; -; mRNA.
EMBL; BC023690; AAH23690.1; -; mRNA.
CCDS; CCDS35644.1; -.
PIR; S27269; S27269.
RefSeq; NP_032337.2; NM_008311.2.
RefSeq; XP_006529210.1; XM_006529147.2.
UniGene; Mm.439747; -.
ProteinModelPortal; Q02152; -.
SMR; Q02152; -.
STRING; 10090.ENSMUSP00000027431; -.
BindingDB; Q02152; -.
ChEMBL; CHEMBL2583; -.
iPTMnet; Q02152; -.
PhosphoSitePlus; Q02152; -.
PaxDb; Q02152; -.
PRIDE; Q02152; -.
Ensembl; ENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
GeneID; 15559; -.
KEGG; mmu:15559; -.
UCSC; uc007buz.1; mouse.
CTD; 3357; -.
MGI; MGI:109323; Htr2b.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00890000139331; -.
HOGENOM; HOG000240378; -.
HOVERGEN; HBG107487; -.
InParanoid; Q02152; -.
KO; K04157; -.
OMA; VWLISIG; -.
OrthoDB; EOG091G06VI; -.
TreeFam; TF316350; -.
Reactome; R-MMU-390666; Serotonin receptors.
Reactome; R-MMU-416476; G alpha (q) signalling events.
PRO; PR:Q02152; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026228; Expressed in 66 organ(s), highest expression level in decidua.
CleanEx; MM_HTR2B; -.
ExpressionAtlas; Q02152; baseline and differential.
Genevisible; Q02152; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; ISS:UniProtKB.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
GO; GO:0071418; P:cellular response to amine stimulus; ISO:MGI.
GO; GO:1904015; P:cellular response to serotonin; ISO:MGI.
GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0002031; P:G-protein coupled receptor internalization; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
GO; GO:0014827; P:intestine smooth muscle contraction; ISS:UniProtKB.
GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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; IMP:UniProtKB.
GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; TAS:MGI.
GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IMP: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; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
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; IMP:UniProtKB.
GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IDA: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.
1: Evidence at protein 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_0000068954.
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,
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 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 127 206 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 349 352 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 167 167 S -> T (in Ref. 1; CAA78824).
{ECO:0000305}.
CONFLICT 227 227 A -> V (in Ref. 1; CAA78824 and 2;
CAA10051). {ECO:0000305}.
CONFLICT 449 449 S -> C (in Ref. 1; CAA78824).
{ECO:0000305}.
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


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