|PROSITE documentation PDOC00535 [for PROSITE entry PS00613]|
The following extracellular proteins contain, in their C-terminal section, a domain of about 240 amino acids which is highly conserved . These proteins are:
This domain has a N-terminal section of about 90 residues that contains 11 conserved cysteines, a central section that is probably in an α-helical conformation, and a C-terminal section that contains two EF-hand type calcium-binding regions  and three conserved cysteines. This topology is schematically represented below.
+----+ | | xCxCxCxxCCxCxxxCxxCxCxxxxxCxCxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxx<Ca>xCxxC<Ca>Cxx *********** ***
'C' : conserved cysteines involved in disulfide bonds. 'Ca': EF-hand region (see <PDOC00018>). '*' : position of the patterns.
We developed two signature patterns for this domain. One is located in the C-terminal cysteine-rich section, the other consists in a highly conserved stretch of 11 residues in the central section.Expert(s) to contact by email:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Lane T.F. Sage E.H.|
|Title||The biology of SPARC, a protein that modulates cell-matrix interactions.|
|Source||FASEB J. 8:163-173(1994).|
|2||Authors||Hohenester E. Maurer P. Hohenadl C. Timpl R. Jansonius J.N. Engel J.|
|Title||Structure of a novel extracellular Ca(2+)-binding module in BM-40.|
|Source||Nat. Struct. Biol. 3:67-73(1996).|