Structure of the Gene Encoding Mouse Reticulocalbin, a Novel Endoplasmic Reticulum-Resident Ca2+-Binding Protein with Multiple EF-Hand Motifs.

Ozawa Masayuki

Reticulocalbin, an endoplasmic reticulum (ER)-resident Ca²⁺-binding protein, is a member of the EF-hand Ca²⁺-binding protein superfamily [Ozawa, M. and Muramatsu, T. (1993) J. Biol. Chem. 268, 699-705]. Reticulocalbin has six repeats of a domain containing the EF-hand motif. In addition, the protein has an amino-terminal leader sequence which serves as a signal for transfer of the protein into the lumen of the ER, and a His-Asp-Glu-Leu sequence at its carboxy terminus which functions as a signal to retain the protein in the ER. In this paper, we describe the genomic structure of this unique Ca²⁺-binding protein. Southern blot analysis of mouse genomic DNA revealed that there is a single copy of the reticulocalbin gene per haploid genome. The gene spans over 13 kilobase pairs and encodes six separate exons. Thus, reticulocalbin differs from the cytosolic Ca²⁺-binding protein calbindin D28 which also has six EF-hand motif domains, but the gene for which is divided into 11 exons. While there is some correlation between exon division and protein domain structure, these relationships are not as clear as they are in other genes. Comparison of the gene organization of reticulocalbin with that of other EF-hand proteins revealed that reticulocalbin diverged very early from other members of the EF-hand protein superfamily.

Structure of the Gene Encoding Mouse Reticulocalbin, a Novel Endoplasmic Reticulum-Resident Ca2+-Binding Protein with Multiple EF-Hand Motifs.

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Structure of the Gene Encoding Mouse Reticulocalbin, a Novel Endoplasmic Reticulum-Resident Ca2+-Binding Protein with Multiple EF-Hand Motifs.

この論文をさがす

説明

収録刊行物

キーワード

詳細情報 詳細情報について

書き出し

問題の指摘

詳細情報詳細情報について