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P08909 (5HT2C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 106. 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 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 names
Name:Htr2c
Synonyms:5ht1c, Htr1c
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Subunit structure

Interacts with MPDZ. Interacts with ARRB2 By similarity. Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein.

Domain

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

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processG-protein signaling, coupled to cyclic nucleotide second messenger

Traceable author statement. Source: RGD

activation of phospholipase C activity by serotonin receptor signaling pathway

Inferred from direct assay. Source: RGD

activation of phospholipase D activity by G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype. Source: RGD

behavioral response to nicotine

Inferred from mutant phenotype. Source: RGD

feeding behavior

Inferred from mutant phenotype. Source: RGD

negative regulation of dopamine metabolic process

Inferred from mutant phenotype. Source: RGD

negative regulation of locomotion

Inferred from mutant phenotype. Source: RGD

organ regeneration

Inferred from expression pattern. Source: RGD

positive regulation of acetylcholine secretion

Inferred from mutant phenotype. Source: RGD

positive regulation of gamma-aminobutyric acid secretion

Inferred from mutant phenotype. Source: RGD

positive regulation of vasoconstriction

Inferred from mutant phenotype. Source: RGD

regulation of sensory perception of pain

Inferred from mutant phenotype. Source: RGD

response to drug

Inferred from mutant phenotype. Source: RGD

   Cellular componentexternal side of plasma membrane

Inferred from direct assay. Source: MGI

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionprotein binding

Inferred from physical interaction. Source: RGD

serotonin receptor activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4604605-hydroxytryptamine receptor 2C
PRO_0000068961

Regions

Topological domain1 – 5353Extracellular By similarity
Transmembrane54 – 7926Helical; Name=1; By similarity
Topological domain80 – 9011Cytoplasmic By similarity
Transmembrane91 – 11121Helical; Name=2; By similarity
Topological domain112 – 12817Extracellular By similarity
Transmembrane129 – 15123Helical; Name=3; By similarity
Topological domain152 – 17120Cytoplasmic By similarity
Transmembrane172 – 19423Helical; Name=4; By similarity
Topological domain195 – 21420Extracellular By similarity
Transmembrane215 – 23622Helical; Name=5; By similarity
Topological domain237 – 31377Cytoplasmic By similarity
Transmembrane314 – 33522Helical; Name=6; By similarity
Topological domain336 – 35015Extracellular By similarity
Transmembrane351 – 37323Helical; Name=7; By similarity
Topological domain374 – 46087Cytoplasmic By similarity
Motif458 – 4603PDZ-binding

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) By similarity
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Disulfide bond128 ↔ 208 By similarity

Experimental info

Mutagenesis4581S → A or D: Loss of interaction with MPDZ. Ref.2
Mutagenesis4591S → D: No effect on interaction with MPDZ. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08909 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: D44E977D8F80047E

FASTA46051,917
        10         20         30         40         50         60 
MVNLGNAVRS LLMHLIGLLV WQFDISISPV AAIVTDTFNS SDGGRLFQFP DGVQNWPALS 

        70         80         90        100        110        120 
IVVIIIMTIG GNILVIMAVS MEKKLHNATN YFLMSLAIAD MLVGLLVMPL SLLAILYDYV 

       130        140        150        160        170        180 
WPLPRYLCPV WISLDVLFST ASIMHLCAIS LDRYVAIRNP IEHSRFNSRT KAIMKIAIVW 

       190        200        210        220        230        240 
AISIGVSVPI PVIGLRDESK VFVNNTTCVL NDPNFVLIGS FVAFFIPLTI MVITYFLTIY 

       250        260        270        280        290        300 
VLRRQTLMLL RGHTEEELAN MSLNFLNCCC KKNGGEEENA PNPNPDQKPR RKKKEKRPRG 

       310        320        330        340        350        360 
TMQAINNEKK ASKVLGIVFF VFLIMWCPFF ITNILSVLCG KACNQKLMEK LLNVFVWIGY 

       370        380        390        400        410        420 
VCSGINPLVY TLFNKIYRRA FSKYLRCDYK PDKKPPVRQI PRVAATALSG RELNVNIYRH 

       430        440        450        460 
TNERVARKAN DPEPGIEMQV ENLELPVNPS NVVSERISSV 

« Hide

References

[1]"Molecular characterization of a functional cDNA encoding the serotonin 1c receptor."
Julius D., McDermott A.B., Axel R., Jessell T.M.
Science 241:558-564(1988) [PubMed: 3399891] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Agonist-induced phosphorylation of the serotonin 5-HT2C receptor regulates its interaction with multiple PDZ protein 1."
Parker L.L., Backstrom J.R., Sanders-Bush E., Shieh B.H.
J. Biol. Chem. 278:21576-21583(2003) [PubMed: 12682077] [Abstract]
Cited for: INTERACTION WITH MPDZ, MUTAGENESIS OF SER-458 AND SER-459.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21410 Genomic DNA. Translation: AAA42177.1.
IPIIPI00187680.
PIRA32605.
RefSeqNP_036897.2. NM_012765.3.
UniGeneRn.9935.

3D structure databases

ProteinModelPortalP08909.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-443850.
STRINGP08909.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP08909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25187.
KEGGrno:25187.
UCSCU35315. rat.

Organism-specific databases

CTD3358.
RGD2848. Htr2c.

Phylogenomic databases

eggNOGroNOG05307.
GeneTreeENSGT00580000081527.
HOVERGENHBG107487.
InParanoidP08909.

Gene expression databases

ArrayExpressP08909.
GenevestigatorP08909.
GermOnlineENSRNOG00000030877. Rattus norvegicus.

Family and domain databases

InterProIPR000377. 5HT2C_rcpt.
IPR002231. 5HT_rcpt.
IPR000276. 7TM_GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]
KOK04157.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00517. 5HT2CRECEPTR.
PR01101. 5HTRECEPTOR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605689.

Entry information

Entry name5HT2C_RAT
AccessionPrimary (citable) accession number: P08909
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 16, 2011
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families