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Protein

5-hydroxytryptamine receptor 2C

Gene

Htr2c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). 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. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and feeding behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis.1 Publication

GO - Molecular functioni

GO - Biological processi

  • animal organ regeneration Source: RGD
  • behavioral fear response Source: UniProtKB
  • behavioral response to nicotine Source: RGD
  • feeding behavior Source: RGD
  • G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger Source: RGD
  • inositol phosphate-mediated signaling Source: MGI
  • locomotory behavior Source: InterPro
  • negative regulation of dopamine metabolic process Source: RGD
  • negative regulation of locomotion Source: RGD
  • phospholipase C-activating serotonin receptor signaling pathway Source: RGD
  • phospholipase D-activating G-protein coupled receptor signaling pathway Source: RGD
  • positive regulation of acetylcholine secretion, neurotransmission Source: RGD
  • positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: UniProtKB
  • positive regulation of gamma-aminobutyric acid secretion Source: RGD
  • positive regulation of vasoconstriction Source: RGD
  • regulation of appetite Source: UniProtKB
  • regulation of corticotropin-releasing hormone secretion Source: UniProtKB
  • regulation of neurological system process Source: UniProtKB
  • regulation of sensory perception of pain Source: RGD
  • release of sequestered calcium ion into cytosol Source: GO_Central
  • response to drug Source: RGD

Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer
Biological processBehavior

Names & Taxonomyi

Protein namesi
Recommended name:
5-hydroxytryptamine receptor 2C
Short name:
5-HT-2C
Short name:
5-HT2C
Short name:
5-HTR2C
Alternative name(s):
5-hydroxytryptamine receptor 1C
Short name:
5-HT-1C
Short name:
5-HT1C
Serotonin receptor 2C
Gene namesi
Name:Htr2c
Synonyms:5ht1c, Htr1c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2848 Htr2c

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 53ExtracellularBy similarityAdd BLAST21
Transmembranei54 – 79Helical; Name=1By similarityAdd BLAST26
Topological domaini80 – 90CytoplasmicBy similarityAdd BLAST11
Transmembranei91 – 111Helical; Name=2By similarityAdd BLAST21
Topological domaini112 – 128ExtracellularBy similarityAdd BLAST17
Transmembranei129 – 151Helical; Name=3By similarityAdd BLAST23
Topological domaini152 – 171CytoplasmicBy similarityAdd BLAST20
Transmembranei172 – 194Helical; Name=4By similarityAdd BLAST23
Topological domaini195 – 214ExtracellularBy similarityAdd BLAST20
Transmembranei215 – 236Helical; Name=5By similarityAdd BLAST22
Topological domaini237 – 313CytoplasmicBy similarityAdd BLAST77
Transmembranei314 – 335Helical; Name=6By similarityAdd BLAST22
Topological domaini336 – 350ExtracellularBy similarityAdd BLAST15
Transmembranei351 – 373Helical; Name=7By similarityAdd BLAST23
Topological domaini374 – 460CytoplasmicBy similarityAdd BLAST87

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi458S → A or D: Loss of interaction with MPDZ. 1 Publication1
Mutagenesisi459S → D: No effect on interaction with MPDZ. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL324
DrugBankiDB00540 Nortriptyline
DB00726 Trimipramine
GuidetoPHARMACOLOGYi8

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32By similarityAdd BLAST32
ChainiPRO_000006896133 – 4605-hydroxytryptamine receptor 2CAdd BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi128 ↔ 208PROSITE-ProRule annotation
Glycosylationi204N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi205N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi339 ↔ 343PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08909
PRIDEiP08909

PTM databases

iPTMnetiP08909
PhosphoSitePlusiP08909

Interactioni

Subunit structurei

Interacts with MPDZ. Interacts with ARRB2 (By similarity).By similarity

Protein-protein interaction databases

MINTiP08909
STRINGi10116.ENSRNOP00000060345

Chemistry databases

BindingDBiP08909

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MHONMR-B452-460[»]
ProteinModelPortaliP08909
SMRiP08909
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 140Agonist bindingBy similarity6
Regioni326 – 330Agonist bindingBy similarity5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi152 – 154DRY motif; important for ligand-induced conformation changesBy similarity3
Motifi366 – 370NPxxY motif; important for ligand-induced conformation changes and signalingBy similarity5
Motifi458 – 460PDZ-binding3

Domaini

The PDZ domain-binding motif is involved in the interaction with MPDZ.

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
HOGENOMiHOG000240378
HOVERGENiHBG107487
InParanoidiP08909
KOiK04157
PhylomeDBiP08909

Family and domain databases

InterProiView protein in InterPro
IPR000377 5HT2C_rcpt
IPR002231 5HT_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PANTHERiPTHR24247:SF32 PTHR24247:SF32, 1 hit
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR00517 5HT2CRECEPTR
PR01101 5HTRECEPTOR
PR00237 GPCRRHODOPSN
SMARTiView protein in SMART
SM01381 7TM_GPCR_Srsx, 1 hit
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08909-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNLGNAVRS LLMHLIGLLV WQFDISISPV AAIVTDTFNS SDGGRLFQFP
60 70 80 90 100
DGVQNWPALS IVVIIIMTIG GNILVIMAVS MEKKLHNATN YFLMSLAIAD
110 120 130 140 150
MLVGLLVMPL SLLAILYDYV WPLPRYLCPV WISLDVLFST ASIMHLCAIS
160 170 180 190 200
LDRYVAIRNP IEHSRFNSRT KAIMKIAIVW AISIGVSVPI PVIGLRDESK
210 220 230 240 250
VFVNNTTCVL NDPNFVLIGS FVAFFIPLTI MVITYFLTIY VLRRQTLMLL
260 270 280 290 300
RGHTEEELAN MSLNFLNCCC KKNGGEEENA PNPNPDQKPR RKKKEKRPRG
310 320 330 340 350
TMQAINNEKK ASKVLGIVFF VFLIMWCPFF ITNILSVLCG KACNQKLMEK
360 370 380 390 400
LLNVFVWIGY VCSGINPLVY TLFNKIYRRA FSKYLRCDYK PDKKPPVRQI
410 420 430 440 450
PRVAATALSG RELNVNIYRH TNERVARKAN DPEPGIEMQV ENLELPVNPS
460
NVVSERISSV
Length:460
Mass (Da):51,917
Last modified:November 1, 1988 - v1
Checksum:iD44E977D8F80047E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21410 Genomic DNA Translation: AAA42177.1
PIRiA32605
RefSeqiNP_036897.2, NM_012765.3
UniGeneiRn.9935

Genome annotation databases

GeneIDi25187
KEGGirno:25187

Similar proteinsi

Entry informationi

Entry namei5HT2C_RAT
AccessioniPrimary (citable) accession number: P08909
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 23, 2018
This is version 147 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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