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TRPV5

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TRPV5
Identifiers
AliasesTRPV5, CAT2, ECAC1, OTRPC3, transient receptor potential cation channel subfamily V member 5
External IDsOMIM: 606679; MGI: 2429764; HomoloGene: 10520; GeneCards: TRPV5; OMA:TRPV5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

56302

194352

Ensembl

ENSG00000274348
ENSG00000127412

ENSMUSG00000036899

UniProt

Q9NQA5

P69744

RefSeq (mRNA)

NM_019841

NM_001007572

RefSeq (protein)

NP_062815

NP_001007573

Location (UCSC)Chr 7: 142.91 – 142.93 MbChr 6: 41.63 – 41.66 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transient receptor potential cation channel subfamily V member 5 is a calcium channel protein that in humans is encoded by the TRPV5 gene.[5][6][7]

Function

The TRPV5 gene is a member of the transient receptor family and the TRPV subfamily. The calcium-selective channel, TRPV5, encoded by this gene has 6 transmembrane-spanning domains, multiple potential phosphorylation sites, an N-linked glycosylation site, and 5 ANK repeats. This protein forms homotetramers or heterotetramers and is activated by a low internal calcium level.[8]

Both TRPV5 and TRPV6 are expressed in kidney and intestinal epithelial cells.[9] TRPV5 is mainly expressed in kidney epithelial cells, where it plays an important role in the reabsorption of Ca2+,[10] whereas TRPV6 is mainly expressed in the intestine.[9] The enzyme α-klotho increases kidney calcium reabsorption by stabilizing TPRV5.[9] Klotho is a beta-glucuronidase-like enzyme that activates TRPV5 by removal of sialic acid.[11]

Clinical significance

Normally, about 95% to 98% of Ca2+ filtered from the blood by the kidney is reabsorbed by the kidney's renal tubule, mediated by TRPV5.[12] Genetic deletion of TRPV5 in mice leads to Ca2+ loss in the urine, and consequential hyperparathyroidism, and bone loss.[13]

Interactions

TRPV5 has been shown to interact with S100A10.[14]

See also

References

  1. ^ a b c ENSG00000127412 GRCh38: Ensembl release 89: ENSG00000274348, ENSG00000127412 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036899 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Müller D, Hoenderop JG, Merkx GF, van Os CH, Bindels RJ (Sep 2000). "Gene structure and chromosomal mapping of human epithelial calcium channel". Biochem. Biophys. Res. Commun. 275 (1): 47–52. doi:10.1006/bbrc.2000.3227. PMID 10944439.
  6. ^ Müller D, Hoenderop JG, Meij IC, van den Heuvel LP, Knoers NV, den Hollander AI, Eggert P, García-Nieto V, Claverie-Martín F, Bindels RJ (Nov 2000). "Molecular cloning, tissue distribution, and chromosomal mapping of the human epithelial Ca2+ channel (ECAC1)". Genomics. 67 (1): 48–53. doi:10.1006/geno.2000.6203. PMID 10945469.
  7. ^ Clapham DE, Julius D, Montell C, Schultz G (Dec 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID 16382100.
  8. ^ "Entrez Gene: TRPV5 transient receptor potential cation channel, subfamily V, member 5".
  9. ^ a b c van Goor MK, Hoenderop JG, van der Wijst J (2017). "TRP channels in calcium homeostasis: from hormonal control to structure-function relationship of TRPV5 and TRPV6". Biochimica et Biophysica Acta. 1864 (6): 883–893. doi:10.1016/j.bbamcr.2016.11.027. PMID 27913205.
  10. ^ Hoenderop JG, Nilius B, Bindels RJ (2002). "Molecular mechanism of active Ca2+ reabsorption in the distal nephron". Annu. Rev. Physiol. 64: 529–49. doi:10.1146/annurev.physiol.64.081501.155921. PMID 11826278.
  11. ^ Cha SK, Ortega B, Kurosu H, Rosenblatt KP, Kuro-O M, Huang CL (2008). "Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1". Proceedings of the National Academy of Sciences of the United States of America. 105 (28): 9805–9810. doi:10.1073/pnas.0803223105. PMC 2474477. PMID 18606998.
  12. ^ Wolf MT, An SW, Nie M, Bal MS, Huang CL (2014). "Klotho up-regulates renal calcium channel transient receptor potential vanilloid 5 (TRPV5) by intra- and extracellular N-glycosylation-dependent mechanisms". Journal of Biological Chemistry. 289 (52): 35849–57. doi:10.1074/jbc.M114.616649. PMC 4276853. PMID 25378396.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  13. ^ Hoenderop JG, van Leeuwen JP, van der Eerden BC, Kersten FF, van der Kemp AW, Mérillat AM, Waarsing JH, Rossier BC, Vallon V, Hummler E, Bindels RJ (2003). "Renal Ca2+ wasting, hyperabsorption, and reduced bone thickness in mice lacking TRPV5". J. Clin. Invest. 112 (12): 1906–14. doi:10.1172/JCI19826. PMC 297001. PMID 14679186.
  14. ^ van de Graaf SF, Hoenderop JG, Gkika D, Lamers D, Prenen J, Rescher U, Gerke V, Staub O, Nilius B, Bindels RJ (Apr 2003). "Functional expression of the epithelial Ca(2+) channels (TRPV5 and TRPV6) requires association of the S100A10-annexin 2 complex". EMBO J. 22 (7): 1478–87. doi:10.1093/emboj/cdg162. PMC 152906. PMID 12660155.

Further reading

  • Vennekens R, Droogmans G, Nilius B (2001). "Functional properties of the epithelial Ca2+ channel, ECaC". Gen. Physiol. Biophys. 20 (3): 239–53. PMID 11765215.
  • Heiner I, Eisfeld J, Lückhoff A (2004). "Role and regulation of TRP channels in neutrophil granulocytes". Cell Calcium. 33 (5–6): 533–40. doi:10.1016/S0143-4160(03)00058-7. PMID 12765698.
  • Nijenhuis T, Hoenderop JG, Bindels RJ (2005). "TRPV5 and TRPV6 in Ca(2+) (re)absorption: regulating Ca(2+) entry at the gate". Pflügers Arch. 451 (1): 181–92. doi:10.1007/s00424-005-1430-6. PMID 16044309.
  • Mensenkamp AR, Hoenderop JG, Bindels RJ (2007). "TRPV5, the gateway to Ca2+ homeostasis". Handb Exp Pharmacol. Handbook of Experimental Pharmacology. 179 (179): 207–20. doi:10.1007/978-3-540-34891-7_12. ISBN 978-3-540-34889-4. PMID 17217059.
  • Schoeber JP, Hoenderop JG, Bindels RJ (2007). "Concerted action of associated proteins in the regulation of TRPV5 and TRPV6". Biochem. Soc. Trans. 35 (Pt 1): 115–9. doi:10.1042/BST0350115. PMID 17233615.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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