Structural highlights
Function
[S10AD_MOUSE] Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Mandinova A, Soldi R, Graziani I, Bagala C, Bellum S, Landriscina M, Tarantini F, Prudovsky I, Maciag T. S100A13 mediates the copper-dependent stress-induced release of IL-1alpha from both human U937 and murine NIH 3T3 cells. J Cell Sci. 2003 Jul 1;116(Pt 13):2687-96. Epub 2003 May 13. PMID:12746488 doi:http://dx.doi.org/10.1242/jcs.00471
- ↑ Kathir KM, Ibrahim K, Rajalingam D, Prudovsky I, Yu C, Kumar TK. S100A13-lipid interactions-role in the non-classical release of the acidic fibroblast growth factor. Biochim Biophys Acta. 2007 Dec;1768(12):3080-9. Epub 2007 Sep 25. PMID:17991455 doi:http://dx.doi.org/10.1016/j.bbamem.2007.09.007
- ↑ Landriscina M, Bagala C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T. Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress. J Biol Chem. 2001 Jul 6;276(27):25549-57. Epub 2001 May 10. PMID:11432880 doi:http://dx.doi.org/10.1074/jbc.M102925200