3.4.21.93	D65A	site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide	669518	
3.4.21.93	D66A	site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide	669518	
3.4.21.93	D67A	site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide	669518	
3.4.21.93	K61A	site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide	669518	
3.4.21.93	additional information	carboxyl terminus-truncated PC3 (1-638) containing the transmembrane domain is associated with lipid rafts in Neuro2A cells, while PC3 (1-616) and PC3-deltaTM lacking the transmembrane domain are not. PC3 (1-638) undergoes stimulated secretion and is colocalized with the secretory granule marker, chromogranin A, by immunocytochemistry. In contrast, PC3 (1-616) and PC3-deltaTM are constitutively secreted and primarily localized in the Golgi	688980	
3.4.21.93	additional information	concentration of progastrin in the antrum of PC1/3-null mice is elevated 3fold. Progastrin molecule is only partly cleaved at the dibasic Arg36-Arg37 site and even less at the Lys53-Lys54 site in the PC1/3-null mice	696097	
3.4.21.93	additional information	construction of an PC3 containing a 19 amino-acid transmembrane sequence, and/or a C-terminal glycosylation tag, the C-terminal extension is exposed to the endoplasmic reticulum lumen, overview	667660	
3.4.21.93	additional information	construction of PC1 prosegment, amino acids 1-110, fused to the C-terminal PC1 tail, amino acids 619-753, termed proCT construct	668621	
3.4.21.93	additional information	design of prohormone convertase-2-specific mutations into the catalytic domain of PC1/3 in order to investigate the molecular contributions of these sequences to PC1/3-specific properties. The exchange of residues RQG314 with the SY sequence present in the same location within PC2 shifts the pH optimum of PC1/3 upward into the neutral range, other mutations in the catalytic domain had no effect. None of the full-length PC1/3 mutants examined exhibits increased specific activity, but the 66-kDa form of the RQG314SY mutant is 2 to 4 times more active than the 66-kDa form of wild-type PC1/3. Mutation of GIVTDA243–248 to QPFMTDI, a molecular determinant of 7B2 binding, results in increased zymogen expression but no propeptide cleavage or secretion, suggesting that this mutant is trapped in the endoplasmic reticulum. None of the mutations examined confers PC2-specific properties. No mutant exhibits altered calcium requirements	717543	
3.4.21.93	additional information	generation of chimeric PC1-propeptide/SAAS CT peptide constructs, effects on C-terminal PC1 processing are limited to the construct containing the PC1 propeptide alone when expressed in AtT20 cells, while both the PC1 propeptide and the SAAS CT propeptide are inhibitory on C-terminal PC1 zymogen processing when expressed in HEK293 cells, overview	669648