ABCC7 p.Leu206Tyr
| ClinVar: |
c.617T>G
,
p.Leu206Trp
D
, Pathogenic
c.618G>T , p.Leu206Phe ? , not provided |
| CF databases: |
c.617T>G
,
p.Leu206Trp
D
, CF-causing ; CFTR1: This mutation was identified in two unrelated CF patient from Southern France.
c.618G>T , p.Leu206Phe (CFTR1) ? , We would like to report a novel mutation we have identified by DGGE and direct sequencing. |
| Predicted by SNAP2: | A: D (95%), C: D (91%), D: D (95%), E: D (95%), F: D (95%), G: D (95%), H: D (95%), I: D (91%), K: D (95%), M: D (91%), N: D (95%), P: D (95%), Q: D (95%), R: D (95%), S: D (95%), T: D (95%), V: D (85%), W: D (71%), Y: D (95%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: N, G: D, H: D, I: N, K: D, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, V: N, W: D, Y: N, |
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[hide] Misprocessing of the CFTR protein leads to mild cy... Hum Mutat. 2005 Apr;25(4):360-71. Clain J, Lehmann-Che J, Dugueperoux I, Arous N, Girodon E, Legendre M, Goossens M, Edelman A, de Braekeleer M, Teulon J, Fanen P
Misprocessing of the CFTR protein leads to mild cystic fibrosis phenotype.
Hum Mutat. 2005 Apr;25(4):360-71., [PMID:15776432]
Abstract [show]
Cystic fibrosis (CF) is mainly caused by mutations that interfere with the biosynthetic folding of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel. The aim of this study was to determine the mechanism of dysfunction of a disease-causing mutation associated with variable phenotypes. In order to attain these objectives, we studied the effect of the p.L206W mutation on CFTR protein production and function, and we examined the genotype-phenotype correlation of [p.L206W]+[p.F508del] patients. We showed that p.L206W is a processing (class II) mutation since the CFTR biosynthetic pathway was severely impaired, whereas single-channel measurements indicated ion conductance similar to the wild-type protein. These data raise the larger question of the phenotypic variability of class II mutants, including p.F508del. Since multiple potential partners could modify the processing of the CFTR protein during its course to the cell surface, environmental and other genetic factors might contribute to this variability.
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No. Sentence Comment
196 In contrast, CFTR misprocessing was induced specifically by different polar residues Glu (p.L206E), Arg (p.L206R), or Tyr (p.L206Y).
X
ABCC7 p.Leu206Tyr 15776432:196:125
status: NEW197 Notably, the substitution by Tyr (p.L206Y), which differs from Phe only by a hydroxyl group, significantly reduced the processing efficiency when compared to p.L206F.
X
ABCC7 p.Leu206Tyr 15776432:197:36
status: NEW