The human Na,K-ATPase beta-subunit is anchored to the membrane by a single stretch of 28 hydrophobic amino acids; the hydrophilic amino terminus faces the cytoplasm and the carboxyl terminus is exoplasmic. Glycosylation and insertion of the Na,K-ATPase beta-subunit into the endoplasmic reticulum membrane are shown to be co-translational and SRP-dependent. The hydrophilic amino terminus is not required for the membrane insertion. The membrane-anchor domain is necessary for membrane insertion, and a 16 amino acid stretch has been identified as an element sufficient for the insertion.
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Kawakami et al. (1988) studied this question.