The cardiac gap junction protein (Mr 47,000) has a tissue-specific cytoplasmic domain of Mr 17,000 at its carboxy-terminus.

The molecular weight of the heart gap junctional protein subunit was, until recently, believed to be about Mr 28,000-30,000, similar to that of other previously characterized gap junctional proteins. A larger polypeptide of about Mr 44,000-47,000, which undergoes proteolysis during isolation, has recently been proposed as the form of the heart junction protein in vivo. We show here that this entity has the same amino-terminal sequence as the previously characterized Mr 29,000-30,000 component. Thus, the cardiac junctional protein has, at its carboxy-terminus, cytoplasmic domain of Mr 17,000; this domain is absent in the liver protein. These observations provide further evidence that gap junction proteins form a highly diversified family.