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Gene Review:

Scp2 - Sarcoplasmic calcium-binding protein 2

Drosophila melanogaster

Synonyms: CE, CG14904, Cex, Dcabp-A.2, Dmel\CG14904, ...

Maxwell, R.A. et al., Nelson, T.J. et al., Lan, Q. et al.

Nelson, Quattrone, Kim, Pacini, Cesati, Alkon, Lan, Wessely,

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High impact information on Scp2

JHDK and dSCP2 are similar to G-proteins with three conserved sequence elements involved in purine nucleotide binding [1].
The results indicate that AeSCP-x is proteolytically cleaved after translation to produce a smaller protein that contains only the SCP-2 domain, which is similar to post-translational modification of the vertebrate's SCP-x to produce multiple products [2].
These results establish that, in the absence of calcium, both squid and Drosophila CE bind GTP at near-physiological concentrations and hydrolyze GTP at rates comparable to unactivated ras [3].
GTPase activity in Drosophila CE was also strongly regulated by Ca(2+), exhibiting over 23-fold higher activity in the presence of 0.3 microM calcium [3].

Biological context of Scp2

Substrate docking to three-dimensional models of JHDK has shown that the three conserved nucleotide-binding elements surround the putative substrate-binding site and align with conserved sequence elements of p21(Ras) and adenylate kinase [1].

References

Juvenile hormone diol kinase. II. Sequencing, cloning, and molecular modeling of juvenile hormone-selective diol kinase from Manduca sexta. Maxwell, R.A., Welch, W.H., Horodyski, F.M., Schegg, K.M., Schooley, D.A. J. Biol. Chem. (2002) [Pubmed]
Expression of a sterol carrier protein-x gene in the yellow fever mosquito, Aedes aegypti. Lan, Q., Wessely, V. Insect Mol. Biol. (2004) [Pubmed]
Calcium-regulated GTPase activity in the calcium-binding protein calexcitin. Nelson, T.J., Quattrone, A., Kim, J., Pacini, A., Cesati, V., Alkon, D.L. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2003) [Pubmed]

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