Calbindin-D28k was first shown to be present in the intestine in birds and then found in the mammalian kidney. It is also expressed in a number of neuroendocrine cells, particularly in the cerebellum. It is encoded in humans by the CALB1 gene.
Calbindin-D28k contains 4 active calcium-binding domains, and 2 modified domains that have lost their calcium-binding capacity. Calbindin-D28k acts as a calcium buffer and calcium sensor and can hold four Ca2+ in the EF-hands of loops EF1, EF3, EF4 and EF5. The structure was solved using high-resolution NMR and which was one of the largest proteins then to be determined. The sequence of Calbindin is 263 residues in length and has only one chain. The sequence consists mostly of alpha helicies but beta sheets are not absent. According to the PDB it is 44% helical with 14 helices containing 117 residues, and 4% beta sheet with 9 strands containing 13 residues.
Calbindin-D28k is a vitamin D responsive gene in many tissues, in particular the chick intestine, where it has a clear function in mediating calcium absorption. In the brain, its synthesis is independent of vitamin-D.
There is no homology between calbindin-D28k and calbindin-D9k, apart from their calcium binding domains (EF-hands): calbindin-D9k has two EF-hands, and calbindin-D28k has six.
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