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- W2007047797 abstract "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." @default.
- W2007047797 created "2016-06-24" @default.
- W2007047797 creator A5018938086 @default.
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- W2007047797 creator A5087139089 @default.
- W2007047797 date "2002-11-01" @default.
- W2007047797 modified "2023-10-03" @default.
- W2007047797 title "Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins" @default.
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- W2007047797 doi "https://doi.org/10.1016/s1570-9639(02)00444-2" @default.
- W2007047797 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12445459" @default.
- W2007047797 hasPublicationYear "2002" @default.
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