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Gene Review

LOC396520  -  calcium binding protein

Gallus gallus

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Disease relevance of LOC396520


High impact information on LOC396520


Biological context of LOC396520

  • The amino acid sequence reveals two Ca2+ binding sites, no internal repeats, 59% homology to the chicken visinin protein and 40% homology to calmodulin while Northern analysis demonstrated a single 1.0 kb mRNA species in bovine and mouse retina [4].
  • Cell survival and structural differentiation appeared normal, but one of the immunocytochemical markers studied (visinin) was less frequently observed in GP-treated cultures [5].

Anatomical context of LOC396520


Associations of LOC396520 with chemical compounds


Regulatory relationships of LOC396520


Other interactions of LOC396520

  • VILIP, a cognate protein of the retinal calcium binding proteins visinin and recoverin, is expressed in the developing chicken brain [11].

Analytical, diagnostic and therapeutic context of LOC396520

  • Hybridization of a northern blot of +/+, +/rd and rd/rd poly(A)+ RNA with a random-primer labelled visinin cDNA probe showed a single, equally labelled 1-Kbp band in each of the samples [2].
  • A 22kDa band, corresponding to purified visinin, was stained with equal intensity on Western blots of +/+, +/rd and rd/rd retinal protein probed with a visinin polyclonal antibody [2].
  • Conversely, Chx10 and Pax6 expression diminished the photoreceptor population to approximately 35% and 15% of control values, as determined by morphologic analysis, visinin immunocytochemistry, and peanut lectin binding [12].
  • In semi-quantitative, dot-immunoblotting analysis, the amount of visinin in the pineal organs of chicks kept under continuous light for 3 days was 4-8 fold more abundant than that under continuous darkness for the same duration [13].


  1. Visinin: a novel calcium binding protein expressed in retinal cone cells. Yamagata, K., Goto, K., Kuo, C.H., Kondo, H., Miki, N. Neuron (1990) [Pubmed]
  2. Visinin: biochemical and molecular comparisons in normal and rd chick retina. Semple-Rowland, S.L., van der Wel, H. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  3. A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase. Lambrecht, H.G., Koch, K.W. EMBO J. (1991) [Pubmed]
  4. Cloning and sequencing of the 23 kDa mouse photoreceptor cell-specific protein. McGinnis, J.F., Stepanik, P.L., Baehr, W., Subbaraya, I., Lerious, V. FEBS Lett. (1992) [Pubmed]
  5. Lipid-mediated gene transfection into chick embryo retinal cells in ovo and in vitro. Toy, J., Bradford, R.L., Adler, R. J. Neurosci. Methods (2000) [Pubmed]
  6. Localization of chick retinal 24,000 dalton protein (visinin)-like immunoreactivity in the rat lower brain stem. Kiyama, H., Takami, K., Hatakenaka, S., Nomura, I., Tohyama, M., Miki, N. Neuroscience (1985) [Pubmed]
  7. Localization of chick retinal visinin-like immunoreactivity in the rat forebrain and diencephalon. Takami, K., Kiyama, H., Hatakenaya, S., Tohyama, M., Miki, N. Neuroscience (1985) [Pubmed]
  8. Expression of an array of photoreceptor genes in chick embryonic retinal pigment epithelium cell cultures under the induction of neuroD. Yan, R.T., Wang, S.Z. Neurosci. Lett. (2000) [Pubmed]
  9. Bone morphogenetic protein 7 increases chick photoreceptor outer segment initiation. Sehgal, R., Andres, D.J., Adler, R., Belecky-Adams, T.L. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  10. NeuroD induces the expression of visinin and calretinin by proliferating cells derived from toxin-damaged chicken retina. Fischer, A.J., Wang, S.Z., Reh, T.A. Dev. Dyn. (2004) [Pubmed]
  11. VILIP, a cognate protein of the retinal calcium binding proteins visinin and recoverin, is expressed in the developing chicken brain. Lenz, S.E., Henschel, Y., Zopf, D., Voss, B., Gundelfinger, E.D. Brain Res. Mol. Brain Res. (1992) [Pubmed]
  12. Effects of homeobox genes on the differentiation of photoreceptor and nonphotoreceptor neurons. Toy, J., Norton, J.S., Jibodh, S.R., Adler, R. Invest. Ophthalmol. Vis. Sci. (2002) [Pubmed]
  13. Direct photosensitivity of chick pinealocytes as demonstrated by visinin immunoreactivity. Goto, K., Yamagata, K., Miki, N., Kondo, H. Cell Tissue Res. (1990) [Pubmed]
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