Q02152 (5HT2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5-hydroxytryptamine receptor 2B
Short name=5-HT-2B
Short name=5-HT2B

Alternative name(s):
5-HT-2F
NP75 protein
Serotonin receptor 2B

Gene names

Name:

Htr2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Plays a role in the regulation of impulsive behavior.
Subunit structure	Interacts with MPDZ By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Intestine and heart, but also in brain and kidney.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Sequence caution	The sequence CAA78824.1 differs from that shown. Reason: Erroneous termination at position 480. Translated as stop.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ERK1 and ERK2 cascade Inferred from mutant phenotype PubMed 20450948PubMed 8621713. Source: UniProtKB G-protein coupled receptor internalization Inferred from direct assay PubMed 17325130. Source: UniProtKB cGMP biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB calcium-mediated signaling Inferred from sequence or structural similarity. Source: UniProtKB cardiac muscle hypertrophy Inferred from mutant phenotype PubMed 19023134. Source: UniProtKB cellular response to calcium ion Inferred from sequence or structural similarity. Source: UniProtKB cellular response to temperature stimulus Inferred from direct assay PubMed 17325130. Source: UniProtKB embryonic morphogenesis Inferred from mutant phenotype PubMed 9165122. Source: UniProtKB heart morphogenesis Inferred from mutant phenotype PubMed 9165122. Source: UniProtKB intestine smooth muscle contraction Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype PubMed 9165122. Source: UniProtKB negative regulation of autophagy Inferred from sequence or structural similarity. Source: UniProtKB neural crest cell migration Inferred from mutant phenotype PubMed 9165122. Source: UniProtKB phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB phospholipase C-activating serotonin receptor signaling pathway Traceable author statement PubMed 10944220. Source: MGI phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from mutant phenotype PubMed 8621713. Source: UniProtKB positive regulation of cytokine production Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cytokine secretion Inferred from mutant phenotype PubMed 19023134. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from mutant phenotype PubMed 19308295. Source: UniProtKB positive regulation of nitric-oxide synthase activity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C-activating G-protein coupled receptor signaling pathway Inferred from mutant phenotype PubMed 17325130. Source: UniProtKB regulation of behavior Inferred from mutant phenotype Ref.6. Source: UniProtKB release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from direct assay PubMed 17325130. Source: UniProtKB vasoconstriction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 17325130. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 17325130. Source: UniProtKB
Molecular_function	G-protein alpha-subunit binding Inferred from sequence or structural similarity. Source: UniProtKB Ras GTPase activator activity Inferred from mutant phenotype PubMed 8621713. Source: UniProtKB calcium channel activity Inferred from sequence or structural similarity. Source: UniProtKB drug binding Inferred from direct assay PubMed 17325130. Source: UniProtKB phosphatidylinositol phospholipase C activity Inferred from sequence or structural similarity. Source: UniProtKB serotonin binding Inferred from direct assay PubMed 17325130. Source: UniProtKB serotonin receptor activity Inferred from direct assay PubMed 17325130. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	5-hydroxytryptamine receptor 2B		PRO_0000068954
Regions
	Topological domain	1 – 55	55	Extracellular By similarity
	Transmembrane	56 – 78	23	Helical; Name=1; By similarity
	Topological domain	79 – 90	12	Cytoplasmic By similarity
	Transmembrane	91 – 112	22	Helical; Name=2; By similarity
	Topological domain	113 – 128	16	Extracellular By similarity
	Transmembrane	129 – 150	22	Helical; Name=3; By similarity
	Topological domain	151 – 170	20	Cytoplasmic By similarity
	Transmembrane	171 – 191	21	Helical; Name=4; By similarity
	Topological domain	192 – 215	24	Extracellular By similarity
	Transmembrane	216 – 238	23	Helical; Name=5; By similarity
	Topological domain	239 – 323	85	Cytoplasmic By similarity
	Transmembrane	324 – 344	21	Helical; Name=6; By similarity
	Topological domain	345 – 359	15	Extracellular By similarity
	Transmembrane	360 – 382	23	Helical; Name=7; By similarity
	Topological domain	383 – 479	97	Cytoplasmic By similarity
	Motif	477 – 479	3	PDZ-binding
Amino acid modifications
	Lipidation	396	1	S-palmitoyl cysteine Potential
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
	Disulfide bond	127 ↔ 206		By similarity
Experimental info
	Sequence conflict	167	1	S → T in CAA78824. Ref.1
	Sequence conflict	227	1	V → A Ref.3
	Sequence conflict	227	1	V → A Ref.4
	Sequence conflict	227	1	V → A Ref.5
	Sequence conflict	449	1	S → C in CAA78824. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02152 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: FDB030D809079B6D	FASTA	479	53,625
	10 20 30 40 50 60 MASSYKMSEQ STTSEHILQK TCDHLILTNR SGLETDSVAE EMKQTVEGQG HTVHWAALLI 70 80 90 100 110 120 LAVIIPTIGG NILVILAVAL EKRLQYATNY FLMSLAIADL LVGLFVMPIA LLTIMFEAIW 130 140 150 160 170 180 PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRAT AFIKITVVWL 190 200 210 220 230 240 ISIGIAIPVP IKGIETDVIN PHNVTCELTK DRFGSFMVFG SLAAFFVPLT IMVVTYFLTI 250 260 270 280 290 300 HTLQKKAYLV KNKPPQRLTR WTVPTVFLRE DSSFSSPEKV AMLDGSHRDK ILPNSSDETL 310 320 330 340 350 360 MRRMSSVGKR SAQTISNEQR ASKALGVVFF LFLLMWCPFF ITNLTLALCD SCNQTTLKTL 370 380 390 400 410 420 LEIFVWIGYV SSGVNPLIYT LFNKTFREAF GRYITCNYRA TKSVKALRKF SSTLCFGNSM 430 440 450 460 470 VENSKFFTKH GIRNGINPAM YQSPMRLRSS TIQSSSIILL DTLLTENDGD KAEEQVSYI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"New mouse 5-HT2-like receptor. Expression in brain, heart and intestine." Loric S., Launay J.-M., Colas J.-F., Maroteaux L. FEBS Lett. 312:203-207(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Genomic sequence of the 5-HT2B receptor locus." Choi D.S., Maroteaux L. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/Sv.
[3]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." 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. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cecum.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[6]	"A population-specific HTR2B stop codon predisposes to severe impulsivity." 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. Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN IMPULSIVE BEHAVIOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z15119 mRNA. Translation: CAA78824.1. Sequence problems. AJ012488 Genomic DNA. Translation: CAA10051.1. AF498254 mRNA. Translation: AAM22971.1. AF498255 mRNA. Translation: AAM22972.1. AK033713 mRNA. Translation: BAC28441.1. BC023690 mRNA. Translation: AAH23690.1.
IPI	IPI00124615.
PIR	S27269.
RefSeq	NP_032337.2. NM_008311.2.
UniGene	Mm.439747.
3D structure databases
ProteinModelPortal	Q02152.
SMR	Q02152. Positions 41-394.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	Q02152.
Proteomic databases
PRIDE	Q02152.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
GeneID	15559.
KEGG	mmu:15559.
UCSC	uc007buz.1. mouse.
Organism-specific databases
CTD	3357.
MGI	MGI:109323. Htr2b.
Phylogenomic databases
eggNOG	NOG247243.
GeneTree	ENSGT00700000104081.
HOGENOM	HOG000240378.
HOVERGEN	HBG107487.
InParanoid	Q02152.
KO	K04157.
OrthoDB	EOG41ZF9R.
Gene expression databases
ArrayExpress	Q02152.
Bgee	Q02152.
CleanEx	MM_HTR2B.
Genevestigator	Q02152.
GermOnline	ENSMUSG00000026228. Mus musculus.
Family and domain databases
InterPro	IPR000482. 5HT2B_rcpt. IPR002231. 5HT_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00651. 5HT2BRECEPTR. PR01101. 5HTRECEPTOR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q02152.
ChEMBL	CHEMBL2583.
NextBio	288504.
SOURCE	Search...

Entry information

Entry name

5HT2B_MOUSE

Accession

Primary (citable) accession number: Q02152
Secondary accession number(s): Q8JZK5, Q9QWS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	June 21, 2005
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program