The histidine-rich $Ca^{2+}$ binding protein (HRC) is a $Ca^{2+}$ binding protein in the sarcoplasmic reticulum (SR). In this study, we examined whether the HRC is involved in the regulation of cardiac contraction and $Ca^{2+}$ signaling using HRC knock-out (KO) mouse ventricular myocytes. In field-stimulated single mouse ventricular myocytes, cell shortenings and $Ca^{2+}$ transients were measured using a video edge detection and a confocal $Ca^{2+}$ imaging, respectively. Compared with the wide-type (WT) myocytes, the magnitudes of cell shortenings were significantly larger in HRC KO cells (P<0.01, WT vs. KO). The rate of contraction and relaxation was significantly accelerated in HRC KO myocytes (P<0.05 and P<0.01, respectively, WT vs. KO). The magnitudes of $Ca^{2+}$ transients were increased by HRC KO (P<0.01, WT vs. KO). In addition, the decay of the $Ca^{2+}$ transient was faster in HRC KO cells than in wild-type cells P<0.01, WT vs. KO). These results suggest that HRC may suppress SR $Ca^{2+}$ releases and decay of $Ca^{2+}$ transients during action potentials, thereby attenuating ventricular contraction and relaxation.