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Transient receptor potential cation channel, subfamily V, member 6
Symbols TRPV6; CAT1; CATL; ABP/ZF; ECAC2; HSA277909; LP6728; ZFAB
External IDs OMIM606680 MGI1927259 HomoloGene56812 IUPHAR: TRPV6 GeneCards: TRPV6 Gene
RNA expression pattern
PBB GE TRPV6 206827 s at tn.png
More reference expression data
Species Human Mouse
Entrez 55503 64177
Ensembl ENSG00000165125 ENSMUSG00000029868
UniProt Q9H1D0 Q91WD2
RefSeq (mRNA) XM_001126541 XM_977638
RefSeq (protein) XP_001126541 XP_982732
Location (UCSC) Chr 7:
142.28 - 142.29 Mb
Chr 6:
41.55 - 41.57 Mb
PubMed search [1] [2]

TRPV6 is a membrane calcium channel which is responsible for the first step in calcium absorption in the intestine. It was first named CAT1 [1], or ECaC2, and has been described in the intestine in several species, including humans [2]. It is located in the apical brush-border membrane of the intestinal enterocyte where is regulates calcium entry into the cell. It is most abundant in the proximal small intestine (duodenum and jejunum) where calbindin and the calcium-pumping ATPAse are also found. The TRPV6 calcium transporter also found in the human placenta, pancreas and prostate gland and in some species in the kidney where the related channel TRPV5 is strongly expressed.

TRPV6 is a member of the Transient receptor potential (TRP) family of membrane proteins. Unlike most TRP channels, TRPV6 is selective for Ca2+ ions, similarly to its close homologue, TRPV5, which is mainly expressed in the kidney, and plays a role in Ca2+ reabsorption.

Expression of TRPV6 appears to be vitamin D dependent as it is greatly reduced in animals that do not express the vitamin D receptor. Importantly, vitamin D treatment of colon cancer cells, Caco-2, also increases expression of TRPV6 gene. Vitamin D treatment of these cells also increases transport of calcium, probably via increasing TRPV6 expression.


See also


  1. ^ Peng JB, Chen XZ, Berger UV, et al. (1999). "Molecular cloning and characterization of a channel-like transporter mediating intestinal calcium absorption". J. Biol. Chem. 274 (32): 22739–46. doi:10.1074/jbc.274.32.22739. PMID 10428857.  
  2. ^ Barley NF, Howard A, O'Callaghan D, Legon S, Walters JR (2001). "Epithelial calcium transporter expression in human duodenum". Am. J. Physiol. Gastrointest. Liver Physiol. 280 (2): G285–90. PMID 11208552.  

Further reading

  • Taparia S, Fleet JC, Peng JB, Wang XD, Wood RJ (2006). "1,25-Dihydroxyvitamin D and 25-hydroxyvitamin D--mediated regulation of TRPV6 (a putative epithelial calcium channel) mRNA expression in Caco-2 cells". European journal of nutrition 45 (4): 196–204. doi:10.1007/s00394-005-0586-3. PMID 16362534.  
  • 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.  
  • Peng JB, Brown EM, Hediger MA (2004). "Epithelial Ca2+ entry channels: transcellular Ca2+ transport and beyond.". J. Physiol. (Lond.) 551 (Pt 3): 729–40. doi:10.1113/jphysiol.2003.043349. PMID 12869611.  
  • Clapham DE, Julius D, Montell C, Schultz G (2006). "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.  
  • Wissenbach U, Niemeyer BA (2007). "TRPV6.". Handb Exp Pharmacol 179 (179): 221–34. doi:10.1007/978-3-540-34891-7_13. PMID 17217060.  
  • 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.  

External links



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