cDNA cloning and predicted primary structure of scallop sarcoplasmic reticulum Ca2+-ATPase

Yoshiaki Nagata, Taibo Yamamoto, Masatsugu Ema, Junsei Mimura, Yoshiaki Fujii-Kuriyama, Tomohiko Suzuki, Takahiro Furukohri, Kazuhiko Konishi, Dai Sato, Genichi Tajima, Jun Nakamura

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6 Citations (Scopus)


Sarcoplasmic reticulum (SR) Ca2+-ATPase of the scallop cross-striated adductor muscle was purified with deoxycholate and digested with lysyl endopeptidase for sequencing of the digested fragments. Overlapping cDNA clones of the ATPase were isolated by screening the cDNA library with an RT-PCR product as a hybridization probe, which encodes the partial amino acid sequence of the ATPase. The predicted amino acid sequence of the ATPase contained all the partial sequences determined with the proteolytic fragments and consisted of the 993 residues with ~70% overall sequence similarity to those of the SR ATPases from rabbit fast-twitch and slow-twitch muscles. An outline of the structure of the scallop ATPase molecule is predicted to mainly consist of ten transmembrane and five 'stalk' domains with two large cytoplasmic regions as observed with the rabbit ATPase molecules. The sequence relationship between scallop and other sarco/endoplasmic reticulum-type Ca2+-ATPases is discussed. Copyright (C) 1998 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)777-785
Number of pages9
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number4
Publication statusPublished - 1998


  • Adductor muscle
  • Amino acid sequence
  • Ca-ATPase
  • Cross-striated muscle
  • Invertebrate
  • Molecular evolution
  • Mollusca
  • Nucleotide sequence
  • cDNA-cloning


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