TRPV5

This gene is a member of the transient receptor family and the TrpV subfamily. The calcium-selective channel 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. [provided by RefSeq]

transient receptor potential cation channel, subfamily V, member 5

Constitutively active calcium selective cation channel thought to be involved in Ca2+ reabsorption in kidney and intestine (PubMed:11549322, PubMed:18768590).
Required for normal Ca2+ reabsorption in the kidney distal convoluted tubules (By similarity).
The channel is activated by low internal calcium level and the current exhibits an inward rectification (PubMed:11549322, PubMed:18768590).
A Ca2+-dependent feedback regulation includes fast channel inactivation and slow current decay (By similarity).
Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).

Biological Process calcium ion homeostasis Source:UniProtKB
Biological Process calcium ion import across plasma membrane Source:UniProtKB1 Publication
Biological Process calcium ion transmembrane transport Source:UniProtKB1 Publication
Biological Process calcium ion transport Source:UniProtKB
Biological Process protein homotetramerization Source:UniProtKB
Biological Process regulation of urine volume Source:UniProtKB

Apical cell membrane
Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells (By similarity).
The expression of the glycosylated form in the cell membrane is increased in the presence of WNK3 (PubMed:18768590).

Cytoplasmic: 1-327
Helical: 328-348
Extracellular: 349-385
Helical: 386-408
Cytoplasmic: 409-419
Helical: 420-442
Extracellular: 443-448
Helical: 449-469
Cytoplasmic: 470-492
Helical: 493-513
Pore-forming: 524-544
Helical: 557-577
Cytoplasmic: 578-729

Glycosylated.