A C2 domain is a protein structural domain involved in targeting proteins to cell membranes. The typical version (PKC-C2) has a beta-sandwich composed of 8 β-strands that co-ordinates two or three calcium ions, which bind in a cavity formed by the first and final loops of the domain, on the membrane binding face.

The C2 domain is a Ca(2+)-binding motif of approximately 130 residues in length originally identified in the Ca(2+)-dependent isoforms of protein kinase C. Single and multiple copies of C2 domains have been identified in a growing number of …

The C2 domain is a protein module of ∼120 aminoacids present in different enzymes such as PKCs cPLA 2 and PLCs. C2 domains possess 8 antiparallel β-sheets, which define three loops essential for calcium binding.

Most studies have concentrated on C2 domains prototyped by those in protein kinase C (PKC-C2) isoforms that bind lipid in a calcium-dependent manner. While two other distinct families of C2 domains, namely those in PI3K-C2 and PTEN-C2 are also recognized, a complete picture of evolutionary relationships within the C2 domain superfamily is lacking.

The C2 domain is a region containing approximately 130 residues that is found in proteins that bind phospholipids in either a calcium-dependent or calcium-independent manner. C2 domains are found in over 100 different proteins with functions ranging from …

C2 domain proteins are proteins containing the second conserved domain of protein kinase C. The C2 domain is an all-beta domain, consisting of a beta-sandwich of two antiparallel four-stranded beta sheets. C2 domains are found in a wide range of both enzymatic and non-enzymatic proteins involved in signal transduction and membrane trafficking.

Jun 1, 2014 · C2 domains are membrane-binding modules that share a common overall fold: a single compact Greek-key motif organized as an eight-stranded anti-parallel β-sandwich consisting of a pair of four-stranded β-sheets.

The C2-domain, originally identified from the a, b, and c isoforms of mammalian Ca 2+-dependent PKC1, contains approximately 130–145 amino acid residues. 3 C2 domain of PKCs is involved in the relocation of PKCs from the cytosol to the membrane …

C 2-domains have diverged evolutionarily into Ca 2+-dependent and Ca 2+-independent forms that interact with multiple targets. Thus, although most C 2-domains are probably Ca 2+-binding domains, they represent a family of versatile protein modules with diverse functions.

SMART detects C2 domains using one or both of two profiles. The C2 domain is a Ca 2+ -dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking.