TY - JOUR
T1 - Isolation and sequence of rat testis cdna for a calcium binding polypeptide similar to the regulatory subunit of calcineurin
AU - Sugimoto, Mikio
AU - Matsui, Hideki
AU - Etoh, Seiji
AU - Shimizu, Tohru
AU - Nishio, Hajime
AU - Moia, Lizomar J.M.P.
AU - Tokuda, Masaaki
AU - Itano, Toshifumi
AU - Takenaka, Ikumasa
AU - Hatase, Osamu
N1 - Funding Information:
We wish to thank Dr. Akinobu Okabe for technical instruction and advice. We are grateful to Dr. Najma Janjua for reviewing the English of this manuscript. This work was supported by a Grant-in-aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
PY - 1991/11/14
Y1 - 1991/11/14
N2 - We have cloned and sequenced rat testis cDNAs coding for a calcium binding polypeptide similar to calcineurin β subunit, the Ca2+-binding subunit of the Ca2+/calmodulin stimulated protein phosphatase. Rat testis cDNA library was screened with a monoclonal antibody Va1 raised against bovine brain calcineurin β subunit. The deduced amino acid sequence is similar to that of human brain calcineurin β subunit with respect to containing four putative calcium binding sites. However, distinct differences were found: 1) The cloned cDNA had six amino acids polypeptide tail at carboxy-terminal which is absent in human brain calcineurin β subunit. This amino acids tail makes the carboxy-terminal highly hydrophilic in contrast to the human brain β subunit which is hydrophobic at carboxy-terminal; 2) eleven amino acids at the N-terminal of the cloned cDNA were completely different from the corresponding region of the brain calcineurin β subunit.
AB - We have cloned and sequenced rat testis cDNAs coding for a calcium binding polypeptide similar to calcineurin β subunit, the Ca2+-binding subunit of the Ca2+/calmodulin stimulated protein phosphatase. Rat testis cDNA library was screened with a monoclonal antibody Va1 raised against bovine brain calcineurin β subunit. The deduced amino acid sequence is similar to that of human brain calcineurin β subunit with respect to containing four putative calcium binding sites. However, distinct differences were found: 1) The cloned cDNA had six amino acids polypeptide tail at carboxy-terminal which is absent in human brain calcineurin β subunit. This amino acids tail makes the carboxy-terminal highly hydrophilic in contrast to the human brain β subunit which is hydrophobic at carboxy-terminal; 2) eleven amino acids at the N-terminal of the cloned cDNA were completely different from the corresponding region of the brain calcineurin β subunit.
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U2 - 10.1016/S0006-291X(05)81362-2
DO - 10.1016/S0006-291X(05)81362-2
M3 - Article
C2 - 1659420
AN - SCOPUS:0025718490
SN - 0006-291X
VL - 180
SP - 1476
EP - 1482
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -