MINDY3

All mammalian species compared share a 95-99% homology similarity to Homo sapiens MINDY3. The reasons behind this are unknown, but it can be inferred that MINDY3 must play an important role in proper cellular function in mammals, as even small changes over time in important genes can drastically alter their function.

Avians, Fish, and Insects also shared a similarity in the 30-40% range with Homo sapiens' MINDY3. Even though there are several hundred million years of divergence from Humans and insects, the fact that there is still a 40% similarity in insects seems to suggest that this gene hasn't changed extremely over such long timespans, and must have been important for other species as well long ago. The splice patterns in these other species aren't known, but in humans there are at least 19 different isoforms but with only 1 major paralog: Fam188b.^[8] This paralog differs structurally in 3 exons with MINDY3.

MINDY3 is a 445-Amino Acid chain. Structurally, it doesn't show many interesting regions that could easily set it apart from other proteins. MINDY3 has no transmembrane domains, it has no sequence repeats.

The I-TASSER^[9] protein folding results show that MINDY3's protein product has a similar structure to 1CFF,^[10] a Calmodulin binding peptide. Calmodulin is involved in cell apoptosis as well, so this can shed light on the theorized function of MINDY3 as well.

The protein fold is most functionally similar to 3LEW,^[11] a “SusD-like carbohydrate binding protein from Bacteroides vulgatus” (Joint Center for Structural Genomics). 3LEW shares a 90% similarity with MINDY3, and although not enough to make a concrete connection, it is enough to establish a base idea of related structures. Another protein that is functionally similar (81%) is 3SNX, a “putative SusD-like carbohydrate binding protein from Bacteroides thetaiotaomicron VPI-5482”.^[12] The function of MINDY3 can be assumed to play a role in cell apoptosis, and that is because it shares structural similarities with other proteins that are involved in this process. Although there is no CARD-domain as would normally be found in an apoptotic peptide, MINDY3 does share a similar function with 1cffA, a “calmodulin binding peptide of the Ca2+ pump”.^[10] Since Calmodulin is known to cause apoptosis throughout various body tissues via the Ca2+ pump^[13][14] and 1cffA shares a 26% similarity with MINDY3, I can hypothesize that apoptosis truly is the function of MINDY3. Other molecules similar to MINDY3 are 1linA,^[15] and 1qx7M, which share 23% and 18% structure similarity respectively, and both of these molecules deal with either the Ca2+ pump or Calmodulin expression as well.