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6327167 
Journal Article 
Review 
Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins 
Maki, M; Kitaura, Y; Satoh, H; Ohkouchi, S; Shibata, H 
2002 
1 
Biochimica et Biophysica Acta
ISSN: 0006-3002
EISSN: 1878-2434 
1600 
1-2 
51-60 
English 
12445459 
WOS:000179517500008 
Penta-EF-hand (PEF) proteins comprise a family of Ca(2+)-binding proteins that have five repetitive EF-hand motifs. Among the eight alpha-helices (alpha1-alpha8), alpha4 and alpha7 link EF2-EF3 and EF4-EF5, respectively. In addition to the structural similarities in the EF-hand regions, the PEF protein family members have common features: (i) dimerization through unpaired C-terminal EF5s, (ii) possession of hydrophobic Gly/Pro-rich N-terminal domains, and (iii) Ca(2+)-dependent translocation to membranes. Based on comparison of amino acid sequences, mammalian PEF proteins are classified into two groups: Group I PEF proteins (ALG-2 and peflin) and Group II PEF proteins (Ca(2+)-dependent protease calpain subfamily members, sorcin and grancalcin). The Group I genes have also been found in lower animals, plants, fungi and protists. Recent findings of specific interacting proteins have started to gradually unveil the functions of the noncatalytic mammalian PEF proteins. 
penta-EF-hand; Ca2+-binding protein; ALG-2; peflin; sorcin; calpain