Calumenin, a Ca2+-binding Protein Retained in the Endoplasmic Reticulum with a Novel Carboxyl-terminal Sequence, HDEF*
Calumenin, a Ca2+-binding Protein Retained in the Endoplasmic Reticulum with a Novel Carboxyl-terminal Sequence, HDEF*
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Calumenin,一种保留在内质网中的 Ca2 结合蛋白,具有新型羧基末端序列,HDEF*
DOI:
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发表时间:
1997
影响因子:
4.8
通讯作者:
T. Honjo
中科院分区:
文献类型:
--
作者:
D. Yabe;Tomoyuki Nakamura;N. Kanazawa;K. Tashiro;T. Honjo
We have identified and characterized a cDNA encoding a novel Ca2+-binding protein named calumenin from mouse heart by the signal sequence trap method. The deduced amino acid sequence (315 residues) of calumenin contains an amino-terminal signal sequence and six Ca2+-binding (EF-hand) motifs and shows homology with reticulocalbin, Erc-55, and Cab45. These proteins seem to form a new subset of the EF-hand protein family expressed in the lumen of the endoplasmic reticulum (ER) and Golgi apparatus. Purified calumenin had Ca2+-binding ability. The carboxyl-terminal tetrapeptide His-Asp-Glu-Phe was shown to be responsible for retention of calumenin in ER by the retention assay, immunostaining with a confocal laser microscope, and the deglycosylation assay. This is the first report indicating that the Phe residue is included in the ER retention signal. Calumenin is expressed most strongly in heart of adult and 18.5-day embryos. The calumenin gene (Calu) was mapped at the proximal portion of mouse chromosome 7.
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DOI:
--
发表时间:
1991
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Andres,DA;Rhodes,JD;Meisel,RL;Dixon,JE
通讯作者:
Dixon,JE
DOI:
10.1016/s0021-9258(19)39273-7
发表时间:
1990-04
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
D. Andres;I. Dickerson;J. Dixon
通讯作者:
D. Andres;I. Dickerson;J. Dixon
DOI:
--
发表时间:
1991
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Wileman,T;Kane,LP;Carson,GR;Terhorst,C
通讯作者:
Terhorst,C
DOI:
--
发表时间:
1993
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Wikström,L;Lodish,HF
通讯作者:
Lodish,HF
影响因子:
56.9
作者:
CHEN, JJ;REID, CE;ANDROPHY, EJ
通讯作者:
ANDROPHY, EJ