TABLE 1.
1———————9—————————————23———-30 | |
Human (b) | FVNQHLCGSHLVEALYLVCGERGFFYTPKT |
Mouse I | FVKQHLCGPHLVEALYLVCGERGFFYTPKS |
Mouse II | FVNQHLCGSHLVEALYLVCGERGFFYTPMS |
31————————————-47——49———————————61 | |
Human (C) | RREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKR |
Mouse I | RREVEDPQVEQLELGGSP GDLQTLALEVARQKR |
Mouse II | RREVEDPQVAQLELGGGPGAGDLQTLALEVAQQKR |
64————————————————-86 | |
Human (a) | GIVEQCCTSICSLYQLENYCN |
Mouse I | GIVDQCCTSICSLYQLENYCN |
Mouse II | GIVDQCCTSICSLYQLENYCN |
The sequences of the human, mouse-1, and mouse-2 proinsulin molecules are shown. The amino acid residues in bold are cleaved off during the physiological processing of the prohormone, and C-peptide is secreted in equimolar amount with the mature insulin heterodimer. The amino acid residue numbering refers to the mouse proinsulin-1 sequence, and the PI-1(47–64) segment is underlined.