Posttranslational processing of a carboxy‐terminal propeptide containing a KDEL sequence of plant vacuolar cysteine endopeptidase (SH‐EP)

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Abstract
A plant cysteine endopeptidase, designated SH‐EP, is a major protease occurring in cotyledons of Vigna mungo seedlings, and acts to degrade seed globulin stored in protein bodies. Here we show that the 43 kDa intermediate of SH‐EP formed in the endoplasmic reticulum is transported to protein bodies and processed to the 33 kDa mature form during transport or thereafter, and that the COOH‐terminal propeptide of 10 amino acid residues containing a KDEL sequence, which is known as a retention signal for the endoplasmic reticulum lumen, is processed to form the mature SH‐EP.