EC Number |
Protein Variants |
Reference |
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3.4.21.93 | more |
identification of polymorphisms of the PC1 gene in 447 individuals from three breeds. Only the P1, P2, P3, P9, and P10 loci show polymorphisms, and 12 SNPs in the PC1 gene have been identified. The polymorphisms are significantly associated with caprine body height and chest circumference |
717206 |
3.4.21.93 | more |
PC1/3 null mutant mice show C-terminally impaired but not completely blocked proIAPP processing, overview |
668377 |
3.4.21.93 | more |
PC1/3-deficient cells do not show preproGIP processing |
669436 |
3.4.21.93 | more |
PC1/3DELTA significantly decreases prohormone convertase 1/3 promoter activity by more than 60%. A 50% reduction when both E-boxes are mutated, even though the STAT3 sites remain intact (PC1/3DELTAE12). Mutation of both STAT3 sites (PC1/3DELTAS12) does not affect basal prohormone convertase 1/3 promoter activity, but leptin stimulation is lost. Mutating the E-box furthest from the start site (E-box 1, PC1/3DELTAE1) only has a significant effect on prohormone convertase 1/3 promoter activity under leptin stimulation, whereas mutating the E-box closest to the start site (E-box 2, PC1/3DELTAE2) has a more pronounced effect on luciferase expression with a loss of approximately 50% prohormone convertase 1/3 promoter activity levels in both leptin-stimulated and unstimulated cells |
700215 |
3.4.21.93 | more |
single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme |
669518 |
3.4.21.93 | N222D |
autocatalytic and neuropeptide processing is impaired |
687032 |
3.4.21.93 | N222D |
leads to obesity, abnormal proinsulin processing, reduced fecundity, impaired autocatalysis and multiple endocrinological defects in mice homozygous for the mutation. Increased energy intake, a more efficient metabolism and reduced alpha-MSH signaling contribute to the obesity. Heterozygous littermates exhibit an intermediate phenotype for both sexes, thus this mutation results in a semi-dominant phenotype |
-, 687032 |
3.4.21.93 | N309K |
naturally occuring mutation identified in four siblings presenting with congenital diarrhea and various endocrinopathies. The mutation affects the oxyanion hole transition state-stabilizing amino acid within the active site, which is critical for appropriate proprotein maturation and enzyme activity. The N309K mutant protein exhibits normal, though slowed, prodomain removal and is secreted from both HEK-293 and Neuro-2A cells. The secreted enzyme shows no catalytic activity, and is not processed into the 66 kDa form |
732772 |
3.4.21.93 | R50A |
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 | R51A |
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 |