Aliases for TRPV6 Gene
- Transient Receptor Potential Cation Channel, Subfamily V, Member 6 2 3
- Epithelial Calcium Channel 2 2 3 4
- ECAC2 3 4 6
- CAT1 3 4 6
- Calcium Transport Protein 1 3 4
- CATL 3 6
- Transient Receptor Potential Cation Channel Subfamily V Member 6 3
- Epithelial Apical Membrane Calcium Transporter/Channel CaT1 3
- Alu-Binding Protein With Zinc Finger Domain 3
External Ids for TRPV6 Gene
Previous Symbols for TRPV6 Gene
This gene encodes a member of a family of multipass membrane proteins that functions as calcium channels. The encoded protein contains N-terminal ankyrin repeats, which are required for channel assembly and regulation. Translation initiation for this protein occurs at a non-AUG start codon that is decoded as methionine. This gene is situated next to a closely related gene for transient receptor potential cation channel subfamily V member 5 (TRPV5). This locus has experienced positive selection in non-African populations, resulting in several non-synonymous codon differences among individuals of different genetic backgrounds. [provided by RefSeq, Feb 2015]
GeneCards Summary for TRPV6 Gene
TRPV6 (Transient Receptor Potential Cation Channel, Subfamily V, Member 6) is a Protein Coding gene. Diseases associated with TRPV6 include cri-du-chat syndrome and prostate cancer. Among its related pathways are CREB Pathway and Signaling events mediated by PTP1B. GO annotations related to this gene include calmodulin binding and calcium channel activity. An important paralog of this gene is TRPV2.
UniProtKB/Swiss-Prot for TRPV6 Gene
Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).
Vanilloids are a group of compounds, structurally related to capsaicin, thought to exert their actions via vanilloid receptors. The vanilloid receptor family (TRPV) is a subgroup of the transient receptor potential (TRP) superfamily of ion channels, and six members (TRPV1-6) have so far been identified. The six vanilloid receptor members have been divided into four groups on the basis of structure and function: TRPV1/2, TRPV3, TRPV4 and TRPV5/6. TRPV1-4 are thermosensitive, non-selective cation channels that exist as tetrameric complexes. They are activated by a range of stimuli including heat, protons, lipids and changes in osmolarity or pressure. TRPV5-6 are calcium selective channels that are involved in the absorption and reabsorption of calcium across intestinal and renal epithelia. It has been proposed that cannabinoids are endogenous ligands for vanilloid receptors. Furthermore, adenosine has been shown to be an endogenous TRPV1 ligand and TRPV4 is activated by anandamide and arachidonic acid.