It is intriguing how the mechanics of molecular motors is regulated to perform the mechanical work in living systems. In sharp contrast to the conventional wisdom, recent experiments indicated that motor force maintains ∼6 pN upon a wide range of filament loads during skeletal muscle contraction at the steady state. Here we find that this rather precise regulation which takes place in an essentially chaotic system, can be due to that a “working” motor is arrested in a transitional state when the motor force is ∼6 pN. Our analysis suggests that the motor force can be self-regulated through chemomechanical coupling, and motor force homeostasis is a built-in feature at the level of a single motor, which provides insights to understanding the coordinated function of multiple molecular motors existing in various physiological processes. With a coupled stochastic-elastic numerical framework, the kinetic model for a Actin-myosin-ATP cycle constructed in this work might pave the way to decently investigate the transient behaviors of the skeletal muscle or other actomyosin complex structures.