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P30994 (5HT2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5-hydroxytryptamine receptor 2B

Short name=5-HT-2B
Short name=5-HT2B
Alternative name(s):
5-HT-2F
Serotonin receptor 2B
Stomach fundus serotonin receptor
Gene names
Name:Htr2b
Synonyms:Srl
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream 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 down-stream signaling cascades and promotes the release of Ca2+ ions from intracellular stores. 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. Ref.1 Ref.3

Subunit structure

Interacts with MPDZ By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsesynaptosome By similarity Ref.1.

Tissue specificity

Stomach fundus. Ref.1

Domain

Ligands are bound in a hydrophobic pocket formed by the transmembrane helices By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processBehavior
   Cellular componentCell junction
Cell membrane
Membrane
Synapse
Synaptosome
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

behavior

Inferred from electronic annotation. Source: UniProtKB-KW

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 sequence or structural similarity. Source: UniProtKB

cellular response to temperature stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

heart morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

intestine smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell death

Inferred from sequence or structural similarity. Source: UniProtKB

neural crest cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

neural crest cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Ras GTPase activity

Inferred from sequence or structural similarity. Source: GOC

positive regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C signaling

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of behavior

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

serotonin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

vasoconstriction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 19023134. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionG-protein alpha-subunit binding

Inferred from sequence or structural similarity. Source: UniProtKB

Ras GTPase activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

serotonin binding

Inferred from sequence or structural similarity. Source: UniProtKB

serotonin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4794795-hydroxytryptamine receptor 2B
PRO_0000068956

Regions

Topological domain1 – 5555Extracellular By similarity
Transmembrane56 – 7823Helical; Name=1; By similarity
Topological domain79 – 8911Cytoplasmic By similarity
Transmembrane90 – 11223Helical; Name=2; By similarity
Topological domain113 – 12816Extracellular By similarity
Transmembrane129 – 15022Helical; Name=3; By similarity
Topological domain151 – 17020Cytoplasmic By similarity
Transmembrane171 – 19121Helical; Name=4; By similarity
Topological domain192 – 21524Extracellular By similarity
Transmembrane216 – 23823Helical; Name=5; By similarity
Topological domain239 – 32385Cytoplasmic By similarity
Transmembrane324 – 34421Helical; Name=6; By similarity
Topological domain345 – 35915Extracellular By similarity
Transmembrane360 – 38122Helical; Name=7; By similarity
Topological domain382 – 47998Cytoplasmic By similarity
Region134 – 1396Agonist binding By similarity
Region336 – 3405Agonist binding By similarity
Motif151 – 1533DRY motif; important for ligand-induced conformation changes By similarity
Motif211 – 2144[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members By similarity
Motif375 – 3795NPxxY motif; important for ligand-induced conformation changes and signaling By similarity
Motif477 – 4793PDZ-binding

Amino acid modifications

Lipidation3961S-palmitoyl cysteine Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Disulfide bond127 ↔ 206 By similarity
Disulfide bond349 ↔ 352 By similarity

Experimental info

Sequence conflict2811V → A Ref.2
Sequence conflict2961T → I no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P30994 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 17FFC73213B42038

FASTA47953,652
        10         20         30         40         50         60 
MASSYKMSEQ STISEHILQK TCDHLILTDR SGLKAESAAE EMKQTAENQG NTVHWAALLI 

        70         80         90        100        110        120 
FAVIIPTIGG NILVILAVSL EKRLQYATNY FLMSLAVADL LVGLFVMPIA LLTIMFEATW 

       130        140        150        160        170        180 
PLPLALCPAW LFLDVLFSTA SIMHLCAISL DRYIAIKKPI QANQCNSRTT AFVKITVVWL 

       190        200        210        220        230        240 
ISIGIAIPVP IKGIEADVVN AHNITCELTK DRFGSFMLFG SLAAFFAPLT IMIVTYFLTI 

       250        260        270        280        290        300 
HALRKKAYLV RNRPPQRLTR WTVSTVLQRE DSSFSSPEKM VMLDGSHKDK ILPNSTDETL 

       310        320        330        340        350        360 
MRRMSSAGKK PAQTISNEQR ASKVLGIVFL FFLLMWCPFF ITNVTLALCD SCNQTTLKTL 

       370        380        390        400        410        420 
LQIFVWVGYV SSGVNPLIYT LFNKTFREAF GRYITCNYQA TKSVKVLRKC SSTLYFGNSM 

       430        440        450        460        470 
VENSKFFTKH GIRNGINPAM YQSPVRLRSS TIQSSSIILL NTFLTENDGD KVEDQVSYI 

« Hide

References

[1]"Cloning and functional characterization of the rat stomach fundus serotonin receptor."
Foguet M., Hoyer D., Pardo L.A., Parekh A., Kluxen F.-W., Kalkman M.O., Stuehmer W., Luebbert H.
EMBO J. 11:3481-3487(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
[2]"Molecular cloning, functional expression, and pharmacological characterization of a novel serotonin receptor (5-hydroxytryptamine2F) from rat stomach fundus."
Kursar J.D., Nelson D.L., Wainscott D.B., Cohen M.L., Baez M.
Mol. Pharmacol. 42:549-557(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Gastric fundus.
[3]"Antinociceptive effect of peripheral serotonin 5-HT2B receptor activation on neuropathic pain."
Urtikova N., Berson N., Van Steenwinckel J., Doly S., Truchetto J., Maroteaux L., Pohl M., Conrath M.
Pain 153:1320-1331(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66842 mRNA. Translation: CAA47318.1.
PIRS23562.
RefSeqNP_058946.1. NM_017250.1.
UniGeneRn.10425.

3D structure databases

ProteinModelPortalP30994.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248214. 1 interaction.
IntActP30994. 1 interaction.
MINTMINT-4000039.
STRING10116.ENSRNOP00000023829.

Chemistry

BindingDBP30994.
ChEMBLCHEMBL2094123.
GuidetoPHARMACOLOGY7.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP30994.

Proteomic databases

PRIDEP30994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29581.
KEGGrno:29581.
UCSCRGD:61801. rat.

Organism-specific databases

CTD3357.
RGD61801. Htr2b.

Phylogenomic databases

eggNOGNOG247243.
HOGENOMHOG000240378.
HOVERGENHBG107487.
InParanoidP30994.
KOK04157.
PhylomeDBP30994.

Gene expression databases

GenevestigatorP30994.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio609690.

Entry information

Entry name5HT2B_RAT
AccessionPrimary (citable) accession number: P30994
Secondary accession number(s): Q9QW44
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries