The cystic fibrosis transmembrane conductance regulator (CFTR) is a 1480 amino acid membrane bound glycoprotein with
a molecular mass of 170,000. It is a member of the ATP binding cassette (ABC)superfamily of proteins. The protein is
comprised of two, six span membrane bound regions each connected to a nuclear binding factor which binds ATP.
Between these two units is an R-domain which is comprised of many charged amino acids. The R-domain is a unique
feature of CFTR within the ABC superfamily.
Put your mouse over the domain region in the following graph to view the summary of that domain, click to view the
details.
19 % of the CFTR protein make up the twelve transmembrane domains (M1 - M12). These domains have been shown to be comprised of typical a-helical secondary structure. Many of the residues within these regions form the channel lining residues and have a major role in the regulation of pore function. Six positively charged residues within the transmembrane domains [K95 (M1), R134 (M2), R334 (M6), K335 (M6), R347 (M6) and R1030 (M10] that are well conserved across species. Two of these are associated with mutations causing CF, R334Q/W and R347C/H/L/P.
The mutations happenning in MSD9 domain:
cDNA Name
|
Protein Name
|
Legacy Name
|
Region
|
Description
|
Consequence
|
c.3199G>C
|
p.Ala1067Pro
|
A1067P
|
exon 20
|
G to C at 3331
|
Ala en Pro at 1067
|
c.3199G>A
|
p.Ala1067Thr
|
A1067T
|
exon 20
|
G to A at 3331
|
Ala to Thr at 1067
|
c.3199_3200delinsA
|
p.Ala1067ThrfsX16
|
|
exon 20
|
|
|
c.3200C>A
|
p.Ala1067Asp
|
A1067D
|
exon 20
|
C to A at 3332
|
Ala to Asp at 1067
|
c.3200C>G
|
p.Ala1067Gly
|
A1067G
|
exon 20
|
C to G at 3332
|
Ala to Gly at 1067
|
c.3200C>T
|
p.Ala1067Val
|
A1067V
|
exon 20
|
C to T at 3332
|
Ala to Val at 1067
|
c.3201C>T
|
|
3333C/T
|
exon 20
|
C or T at 3333
|
sequence variation
|
c.3204C>T
|
|
3336C/T
|
exon 20
|
C or T at 3336
|
sequence variation
|
c.3205G>A
|
p.Gly1069Arg
|
G1069R
|
exon 20
|
G to A at 3337
|
Gly to Arg at 1069
|
c.3208C>T
|
p.Arg1070Trp
|
R1070W
|
exon 20
|
C to T at 3340
|
Arg to Trp at 1070
|
c.3209G>C
|
p.Arg1070Pro
|
R1070P
|
exon 20
|
G to C at 3341
|
Arg to Pro at 1070
|
c.3209G>A
|
p.Arg1070Gln
|
R1070Q
|
exon 20
|
G to A at 3341
|
Arg to Gln at 1070
|
c.3211C>T
|
p.Gln1071X
|
Q1071X
|
exon 20
|
C to T at 3343
|
Gln to Stop at 1071
|
c.3212A>C
|
p.Gln1071Pro
|
Q1071P
|
exon 20
|
A to C at 3344
|
Gln to Pro at 1071
|
c.3213G>T
|
p.Gln1071His
|
Q1071H
|
exon 20
|
G to T at 3345
|
Gln to His at 1071
|
c.3215C>T
|
p.Pro1072Leu
|
P1072L
|
exon 20
|
C to T at 3347
|
Pro to Leu at 1072
|
c.3218A>G
|
p.Tyr1073Cys
|
Y1073C
|
exon 20
|
A to G at 3350
|
Tyr to Cys at 1073
|
c.3220T>C
|
p.Phe1074Leu
|
|
|
|
|
c.3222T>A
|
p.Phe1074Leu
|
F1074L
|
exon 20
|
T to A at 3354
|
Phe to Leu at 1074
|
c.3229_3230delCT
|
p.Leu1077ValfsX78
|
3359delCT
|
exon 20
|
deletion of CT from 3359
|
frameshift
|
c.3230T>C
|
p.Leu1077Pro
|
L1077P
|
exon 20
|
T to C at 3362
|
Leu to Pro at 1077
|
c.3232T>A
|
p.Phe1078Ile
|
|
|
|
|
c.3233T>C
|
p.Phe1078Ser
|
|
exon 20
|
|
|
c.3236A>C
|
p.His1079Pro
|
H1079P
|
exon 20
|
A to C at 3368
|
His to Pro at 1079
|
c.3238A>C
|
p.Lys1080Gln
|
K1080Q
|
exon 20
|
3370A>C
|
|
c.3239A>G
|
p.Lys1080Arg
|
K1080R
|
exon 20
|
A to G at 3371
|
Lys to Arg
at 1080
|
c.3239A>T
|
p.Lys1080Ile
|
|
|
|
|
c.3241G>C
|
p.Ala1081Pro
|
A1081P
|
exon 20
|
G to C at 3373
|
Ala to Pro at 1081
|
c.3252A>G
|
|
3384A/G
|
exon 20
|
A or G at 3384
|
sequence variation
|
c.3254A>G
|
p.His1085Arg
|
H1085R
|
exon 20
|
A to G at 3386
|
His to Arg at 1085
|
c.3256A>G
|
p.Thr1086Ala
|
T1086A
|
exon 20
|
A to G at 3388
|
Thr to Ala at 1086
|
c.3257C>T
|
p.Thr1086Ile
|
T1086I
|
exon 20
|
C to T at 3389
|
Thr to Ile at 1086
|
c.3259G>C
|
p.Ala1087Pro
|
A1087P
|
exon 20
|
G to C at 3391
|
Ala to Pro at AS 1087
|