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Protein

5-hydroxytryptamine receptor 2C

Gene

Htr2c

Organism
Rattus norvegicus (Rat)
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 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

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • 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
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Behavior

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2848. Htr2c.

Subcellular locationi

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

GO - Cellular componenti

  • cell surface Source: RGD
  • dendrite Source: GO_Central
  • external side of plasma membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • intracellular Source: GOC
Complete GO annotation...

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...)By similarity1
Disulfide bondi128 ↔ 208PROSITE-ProRule annotation
Glycosylationi204N-linked (GlcNAc...)Sequence analysis1
Glycosylationi205N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi339 ↔ 343PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08909.

PTM databases

iPTMnetiP08909.
PhosphoSitePlusiP08909.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

MINTiMINT-443850.
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

InterProiIPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF32. PTHR24247:SF32. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00517. 5HT2CRECEPTR.
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.

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.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

MINTiMINT-443850.
STRINGi10116.ENSRNOP00000060345.

Chemistry databases

BindingDBiP08909.
ChEMBLiCHEMBL324.
DrugBankiDB00540. Nortriptyline.
DB00726. Trimipramine.
GuidetoPHARMACOLOGYi8.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP08909.
PhosphoSitePlusiP08909.

Proteomic databases

PaxDbiP08909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25187.
KEGGirno:25187.

Organism-specific databases

CTDi3358.
RGDi2848. Htr2c.

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
HOGENOMiHOG000240378.
HOVERGENiHBG107487.
InParanoidiP08909.
KOiK04157.
PhylomeDBiP08909.

Miscellaneous databases

PROiP08909.

Family and domain databases

InterProiIPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24247:SF32. PTHR24247:SF32. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00517. 5HT2CRECEPTR.
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 namei5HT2C_RAT
AccessioniPrimary (citable) accession number: P08909
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.