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Protein

5-hydroxytryptamine receptor 2B

Gene

Htr2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 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 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. May play a role in the perception of pain. 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.10 Publications

GO - Molecular functioni

  • drug binding Source: UniProtKB
  • G-protein alpha-subunit binding Source: UniProtKB
  • G-protein coupled serotonin receptor activity Source: UniProtKB
  • GTPase activator activity Source: UniProtKB
  • neurotransmitter receptor activity Source: GO_Central
  • serotonin binding Source: UniProtKB

GO - Biological processi

  • activation of phospholipase C activity Source: MGI
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • behavior Source: UniProtKB-KW
  • calcium-mediated signaling Source: UniProtKB
  • cardiac muscle hypertrophy Source: UniProtKB
  • cellular calcium ion homeostasis Source: MGI
  • cellular response to temperature stimulus Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • chemical synaptic transmission Source: GO_Central
  • embryonic morphogenesis Source: UniProtKB
  • ERK1 and ERK2 cascade Source: UniProtKB
  • G-protein coupled receptor internalization Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • heart development Source: MGI
  • heart morphogenesis Source: UniProtKB
  • intestine smooth muscle contraction Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of autophagy Source: UniProtKB
  • negative regulation of cell death Source: UniProtKB
  • neural crest cell differentiation Source: UniProtKB
  • neural crest cell migration Source: UniProtKB
  • phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • phospholipase C-activating serotonin receptor signaling pathway Source: MGI
  • phosphorylation Source: UniProtKB
  • positive regulation of cell division Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cytokine production Source: UniProtKB
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of nitric-oxide synthase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol biosynthetic process Source: UniProtKB
  • protein kinase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
  • regulation of behavior Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: UniProtKB
  • response to drug Source: UniProtKB
  • serotonin receptor signaling pathway Source: UniProtKB
  • vasoconstriction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

Enzyme and pathway databases

ReactomeiR-MMU-390666. Serotonin receptors.
R-MMU-416476. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Htr2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:109323. Htr2b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 55ExtracellularBy similarityAdd BLAST55
Transmembranei56 – 78Helical; Name=1By similarityAdd BLAST23
Topological domaini79 – 89CytoplasmicBy similarityAdd BLAST11
Transmembranei90 – 112Helical; Name=2By similarityAdd BLAST23
Topological domaini113 – 128ExtracellularBy similarityAdd BLAST16
Transmembranei129 – 150Helical; Name=3By similarityAdd BLAST22
Topological domaini151 – 170CytoplasmicBy similarityAdd BLAST20
Transmembranei171 – 191Helical; Name=4By similarityAdd BLAST21
Topological domaini192 – 215ExtracellularBy similarityAdd BLAST24
Transmembranei216 – 238Helical; Name=5By similarityAdd BLAST23
Topological domaini239 – 323CytoplasmicBy similarityAdd BLAST85
Transmembranei324 – 344Helical; Name=6By similarityAdd BLAST21
Topological domaini345 – 359ExtracellularBy similarityAdd BLAST15
Transmembranei360 – 381Helical; Name=7By similarityAdd BLAST22
Topological domaini382 – 479CytoplasmicBy similarityAdd BLAST98

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • dendrite Source: GO_Central
  • integral component of plasma membrane Source: GO_Central
  • plasma membrane Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

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. 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. 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.7 Publications

Chemistry databases

ChEMBLiCHEMBL2583.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000689541 – 4795-hydroxytryptamine receptor 2BAdd BLAST479

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi127 ↔ 206PROSITE-ProRule annotation
Disulfide bondi349 ↔ 352PROSITE-ProRule annotation
Lipidationi396S-palmitoyl cysteineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ02152.
PRIDEiQ02152.

PTM databases

iPTMnetiQ02152.
PhosphoSitePlusiQ02152.

Expressioni

Tissue specificityi

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.6 Publications

Gene expression databases

BgeeiENSMUSG00000026228.
CleanExiMM_HTR2B.
ExpressionAtlasiQ02152. baseline and differential.
GenevisibleiQ02152. MM.

Interactioni

Subunit structurei

Interacts with MPDZ.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027431.

Structurei

3D structure databases

ProteinModelPortaliQ02152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni134 – 139Agonist bindingBy similarity6
Regioni336 – 340Agonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi151 – 153DRY motif; important for ligand-induced conformation changes3
Motifi211 – 214[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family membersBy similarity4
Motifi375 – 379NPxxY motif; important for ligand-induced conformation changes and signaling5
Motifi477 – 479PDZ-binding3

Domaini

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

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00780000121897.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiQ02152.
KOiK04157.
OMAiCDSCNQT.
OrthoDBiEOG091G06VI.
TreeFamiTF316350.

Family and domain databases

InterProiIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSYKMSEQ STTSEHILQK TCDHLILTNR SGLETDSVAE EMKQTVEGQG
60 70 80 90 100
HTVHWAALLI LAVIIPTIGG NILVILAVAL EKRLQYATNY FLMSLAIADL
110 120 130 140 150
LVGLFVMPIA LLTIMFEAIW PLPLALCPAW LFLDVLFSTA SIMHLCAISL
160 170 180 190 200
DRYIAIKKPI QANQCNSRAT AFIKITVVWL ISIGIAIPVP IKGIETDVIN
210 220 230 240 250
PHNVTCELTK DRFGSFMVFG SLAAFFAPLT IMVVTYFLTI HTLQKKAYLV
260 270 280 290 300
KNKPPQRLTR WTVPTVFLRE DSSFSSPEKV AMLDGSHRDK ILPNSSDETL
310 320 330 340 350
MRRMSSVGKR SAQTISNEQR ASKALGVVFF LFLLMWCPFF ITNLTLALCD
360 370 380 390 400
SCNQTTLKTL LEIFVWIGYV SSGVNPLIYT LFNKTFREAF GRYITCNYRA
410 420 430 440 450
TKSVKALRKF SSTLCFGNSM VENSKFFTKH GIRNGINPAM YQSPMRLRSS
460 470
TIQSSSIILL DTLLTENDGD KAEEQVSYI
Length:479
Mass (Da):53,597
Last modified:October 16, 2013 - v3
Checksum:iF02B30D80C8C9B6D
GO

Sequence cautioni

The sequence CAA78824 differs from that shown. Reason: Erroneous termination at position 480. Translated as stop.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167S → T in CAA78824 (PubMed:1426253).Curated1
Sequence conflicti227A → V in CAA78824 (PubMed:1426253).Curated1
Sequence conflicti227A → V in CAA10051 (Ref. 2) Curated1
Sequence conflicti449S → C in CAA78824 (PubMed:1426253).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35644.1.
PIRiS27269.
RefSeqiNP_032337.2. NM_008311.2.
XP_006529210.1. XM_006529147.2.
UniGeneiMm.439747.

Genome annotation databases

EnsembliENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
GeneIDi15559.
KEGGimmu:15559.
UCSCiuc007buz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35644.1.
PIRiS27269.
RefSeqiNP_032337.2. NM_008311.2.
XP_006529210.1. XM_006529147.2.
UniGeneiMm.439747.

3D structure databases

ProteinModelPortaliQ02152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027431.

Chemistry databases

ChEMBLiCHEMBL2583.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ02152.
PhosphoSitePlusiQ02152.

Proteomic databases

PaxDbiQ02152.
PRIDEiQ02152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027431; ENSMUSP00000027431; ENSMUSG00000026228.
GeneIDi15559.
KEGGimmu:15559.
UCSCiuc007buz.1. mouse.

Organism-specific databases

CTDi3357.
MGIiMGI:109323. Htr2b.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00780000121897.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiQ02152.
KOiK04157.
OMAiCDSCNQT.
OrthoDBiEOG091G06VI.
TreeFamiTF316350.

Enzyme and pathway databases

ReactomeiR-MMU-390666. Serotonin receptors.
R-MMU-416476. G alpha (q) signalling events.

Miscellaneous databases

PROiQ02152.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026228.
CleanExiMM_HTR2B.
ExpressionAtlasiQ02152. baseline and differential.
GenevisibleiQ02152. MM.

Family and domain databases

InterProiIPR000482. 5HT2B_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF31. PTHR24247:SF31. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00651. 5HT2BRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
SMARTiSM01381. 7TM_GPCR_Srsx. 1 hit.
[Graphical view]
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei5HT2B_MOUSE
AccessioniPrimary (citable) accession number: Q02152
Secondary accession number(s): Q8JZK5, Q9QWS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 16, 2013
Last modified: November 2, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.