A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.

Annotation

general or unspecified; prefer specifics

obecné nebo nevymezené, dej přednost přesnějšímu deskriptoru

DUI

D009218 MeSH Browser

CUI

M0014361

Previous indexing

Muscle Proteins (1966-1970); Adenosine Triphosphatase (1966-1968)

History note

2002(1971); use ADENOSINE TRIPHOSPHATASE 1963-1968; for MYOSIN ATPASE use ADENOSINETRIPHOSPHATASE 1984-1988; for ACTOMYOSIN ATPASE use ADENOSINETRIPHOSPHATASE 1985-1988

Public note

2002; see MYOSIN 1973-2001, see MUSCLE PROTEINS 1969-1972; see ADENOSINE TRIPHOSPHATASE 1963-1968; for MYOSIN ATPASE see MYOSIN ATPASE 1993-2001, see ADENOSINE TRIPHOSPHATASE, MYOSIN 1989-1992, see ADENOSINE TRIPHOSPHATASE 1984-1988; for ADENOSINE TRIPHOSPHATASE, MYOSIN & MYOSIN ADENOSINETRIPHOSPHATASE see MYOSIN ATPASE 1993-2001; for ACTOMYOSIN ADENOSINETRIPHOSPHATASE & ADENOSINETRIPHOSPHATASE, ACTOMYOSIN see MYOSIN ATPASE 1993-2001, see ADENOSINE TRIPHOSPHATASE, MYOSIN 1989-92; for ACTOMYOSIN ATPASE see MYOSIN ATPASE 1993-2001, see ADENOSINE TRIPHOSPHATASE, MYOSIN 1989-1992, see ADENOSINE TRIPHOSPHATASE 1985-1988