Transient receptor potential cation channel subfamily V member 2 (TRPV2)

The protein contains 764 amino acids for an estimated molecular weight of 85981 Da.

 

Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 0%
Model score: 0
No model available.

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VariantDescription
dbSNP:rs3813768
dbSNP:rs8071215

No binding partner found

The reference OMIM entry for this protein is 606676

Transient receptor potential cation channel, subfamily v, member 2; trpv2
Vanilloid receptor-like protein 1; vrl1

Pain-producing heat is detected by nociceptive sensory neurons that differ in their thermal response thresholds. Capsaicin, the main pungent ingredient in 'hot' chili peppers, is detected by the vanilloid receptor (VR1; 602076). VR1 is a heat-gated ion channel that mediates responses of small-diameter sensory neurons to moderate (43 degrees Celsius) thermal stimuli.

CLONING

By searching an EST database for sequences related to VR1, followed by probing a myeloid cell line, Caterina et al. (1999) isolated a cDNA encoding TRPV2, which they called VRL1. Sequence analysis predicted that the 764-amino acid VRL1 protein, which is 78% identical to the rat protein, contains 6 transmembrane domains, a putative pore-loop region, a cytoplasmic N terminus with 3 ankyrin-repeat domains, and a C-terminal cytoplasmic tail. Functional analysis showed that cells expressing VRL1 did not respond to capsaicin or low pH, but they did respond to heat over 53 degrees Celsius and to cations. Immunofluorescence microscopy demonstrated expression of Vrl1 in medium- to large-diameter rat dorsal root ganglion neurons and in spinal cord, specifically in Lissauer's tract and the dorsal horn. Northern blot analysis revealed expression of an approximately 2.5-kb Vrl1 transcript in rat sensory ganglia and spinal cord, as well as in lung, spleen, intestine, and multiple brain subregions. Caterina et al. (1999) suggested that nonneuronal tissues expressing VRL1 probably respond to stimuli other than high heat.

MAPPING

The International Radiation Hybrid Mapping Consortium mapped the TRPV2 gene to chromosome 17 (TMAP stSG44964).

ANIMAL MODEL

Muscular dystrophy (DMD; 310200) is a severe degenerative disorder of skeletal muscle characterized by progressive muscle weakness. One subgroup of this disease is caused by a defect in the genes encoding components of the dystrophin-glycoprotein complex (see dystrophin; 300337), resulting in a significant disruption of membrane integrity and/or stability and, consequently, a sustained increase in the cytosolic Ca(2+) concentration. Iwata et al. (2009) demonstrated that muscular dystrophy is ameliorated dystrophin-deficient mdx mice by dominant-negative inhibition of TRPV2. When transgenic (Tg) mice expressing a Trpv2 mutant in muscle were crossed with mdx mice, the cytosolic Ca(2+) concentration increase in muscle fibers was reduced. Histologic, biochemical, and physiologic indices characterizing dystrophic pathology, such as an increased number of central nuclei and fiber size variability/fibrosis/apoptosis, elevated serum creatine kinase levels, and reduced muscle performance, were all ameliorated in the mdx/Tg mice. Iwata et al. (2009) proposed that TRPV2 is a principal Ca(2+)-entry route leading to a sustained [Ca2+]i increase and muscle degeneration. ... More on the omim web site

Subscribe to this protein entry history

June 30, 2020: Protein entry updated
Automatic update: OMIM entry 606676 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).