Archives of Pharmacal Research
- Volume 21 Issue 6
- /
- Pages.712-717
- /
- 1998
- /
- 0253-6269(pISSN)
- /
- 1976-3786(eISSN)
Nucleotide and Deduced Amino Acid Sequences of Rat Myosin Binding Protein H (MyBP-H)
- Jung, Jae-Hoon (College of Pharmacy, Ewha Womans University) ;
- Oh, Ji-Hyun (College of Pharmacy, Ewha Womans University) ;
- Lee, Kyung-Lim (College of Pharmacy, Ewha Womans University)
- Published : 1998.12.01
Abstract
The complete nucleotide sequence of the cDNA clone encoding rat skeletal muscle myosin- binding protein H (MyBP-H) was determined and amino acid sequence was deduced from the nucleotide sequence (GenBank accession number AF077338). The full-length cDNA of 1782 base pairs(bp) contains a single open reading frame of 1454 bp encoding a rat MyBP-H protein of the predicted molecular mass 52.7kDa and includes the common consensus 1CA__TG' protein binding motif. The cDNA sequence of rat MyBP-H show 92%, 84% and 41% homology with those of mouse, human and chicken, respectively. The protein contains tandem internal motifs array (-FN III-Ig C2-FN III- Ig C2-) in the C-terminal region which resembles to the immunoglobulin superfamily C2 and fibronectin type III motifs. The amino acid sequence of the C-terminal Ig C2 was highly conserved among MyBPs family and other thick filament binding proteins, suggesting that the C-terminal Ig C2 might play an important role in its function. All proteins belonging to MyBP-H member contains `RKPS` sequence which is assumed to be cAMP- and cGMP-dependent protein kinase A phosphorylation site. Computer analysis of the primary sequence of rat MyBP-H predicted 11 protein kinase C (PKC)phosphorylation site, 7 casein kinase II (CK2) phosphorylation site and 4N-myristoylation site.