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Scallop DMT functions as a Ca 2+ transporter
Author(s) -
Toyohara Haruhiko,
Yamamoto Sayuri,
Hosoi Masatomi,
Takagi Masaya,
Hayashi Isao,
Nakao Kenji,
Kaneko Shuji
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.082
Subject(s) - scallop , transporter , extracellular , dmt1 , chemistry , biochemistry , complementary dna , patinopecten yessoensis , intracellular , divalent , amino acid , microbiology and biotechnology , biology , biophysics , gene , fishery , organic chemistry
We identified a DMT (divalent metal transporter) homologous protein that functions as a Ca 2+ transporter. Scallop DMT cDNA encodes a 539‐amino‐acid protein with 12 putative membrane‐spanning domains and has a consensus transport motif in the fourth extracellular loop. Since its mRNA is significantly expressed in the gill and intestine, it is assumed that scallop DMT transports Ca 2+ from seawater by the gill and from food by the intestine. Scallop DMT lacks the iron‐responsive element commonly found in iron‐regulatory proteins, suggesting that it is free of the post‐transcriptional regulation from intracellular Fe 2+ concentration. Scallop DMT distinctly functions as a Ca 2+ transporter unlike other DMTs, however, it also transports Fe 2+ and Cd 2+ similar to them.