Table 1.

Structure of the variable parts in the carboxyl terminal tail of α_1C subunits under investigation

α1C, 77	IKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFL-IQEYFRKFKKRKEQGLVGKPSQRNALSL	(1572–1651)
α1C, 77L	ETELSSQVQYQAKEASLLERRRKSSHP	(1572–1598)
α1C,77K	SSHPKSSTKPNKLLSSGGSTGWVEDARALEGQVLARGCGWLGSLEERERGPHHPPLGF	(1595–1652)
α1C,86	ETELSSQVQYQAKEASLLERRRKSSHPKSSTKPNKLLSSGGSTGWVEDARALEGQVLARGCGWLGSLEERERGPEHPPLGF	(1572–1652)

Amino acid sequences of α_1C,77 (1572–1651) and α_1C,86 (1572–1652) are shown in the top and bottom rows, respectively. Indicated amino acids of α_1C,86 replace the respective residues in the amino acid sequence of α_1C,77. In α_1C,77L and α_1C,77K subunits, indicated segments of α_1C,86 replace the respective motifs L (1572–1598) and K (1595–1651) of the α_1C,77 subunit. Note that the overlapping 4 amino acid segment SSHP has been proven not to contribute to the kinetics, voltage or Ca²⁺ dependence of inactivation (Soldatov et al. 1998). Residues in bold are located in identical positions between α_1C subunits.