ABCMdb

ABCC7 p.Ile340Asn

CF databases:	c.1019T>A , p.Ile340Asn (CFTR1) ? ,
Predicted by SNAP2:	A: N (66%), C: N (53%), D: D (85%), E: D (75%), F: D (66%), G: D (80%), H: D (75%), K: D (85%), L: N (82%), M: N (82%), N: D (75%), P: D (85%), Q: D (59%), R: D (80%), S: D (71%), T: N (53%), V: N (87%), W: D (80%), Y: D (71%),
Predicted by PROVEAN:	A: N, C: D, D: D, E: D, F: N, G: D, H: D, K: D, L: N, M: N, N: D, P: D, Q: D, R: D, S: D, T: D, V: N, W: D, Y: D,

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Publications
[hide] Membrane-integration characteristics of two ABC tr... J Mol Biol. 2009 Apr 17;387(5):1153-64. Epub 2009 Feb 21. Enquist K, Fransson M, Boekel C, Bengtsson I, Geiger K, Lang L, Pettersson A, Johansson S, von Heijne G, Nilsson I
Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein.
J Mol Biol. 2009 Apr 17;387(5):1153-64. Epub 2009 Feb 21., [PMID:19236881]

Abstract [show]
To what extent do corresponding transmembrane helices in related integral membrane proteins have different membrane-insertion characteristics? Here, we compare, side-by-side, the membrane insertion characteristics of the 12 transmembrane helices in the adenosine triphosphate-binding cassette (ABC) transporters, P-glycoprotein (P-gp) and the cystic fibrosis transmembrane conductance regulator (CFTR). Our results show that 10 of the 12 CFTR transmembrane segments can insert independently into the ER membrane. In contrast, only three of the P-gp transmembrane segments are independently stable in the membrane, while the majority depend on the presence of neighboring loops and/or transmembrane segments for efficient insertion. Membrane-insertion characteristics can thus vary widely between related proteins.

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Sentences [show]
No. Sentence Comment
113 For CFTR, we chose mutations located in TM1CFTR (F87L, G91R), TM3CFTR (P205S, L206W), TM4CFTR (C225R), TM5CFTR (DF311, G314E), TM6CFTR (R334L/W, I336K/R/D, I340N/S, L346P, R347L/H), TM8CFTR (S909I, S912L), TM9CFTR (I1005R, A1006E), TM10CFTR (Y1032N), and TM12CFTR (M1137R, ΔM1140, M1140K), or close to the TM region of TM1CFTR (R74W, L102R/P), TMF2CFTR (R117P/L, L137P), and TM11CFTR (M1101K/R). Login to comment
115 As seen in Supplementary Data Table S2, only a few of the tested mutations in the 19 residue long CFTR TM segments alter the insertion efficiency significantly: TM4CFTR (C225R) (decrease from 88% to 34%), TM6CFTR (I336K/R/D) (decrease from 55% to 34%, 36% and 35%, respectively), TM6CFTR (I340N/S) (decrease from 55% to 32% and 35%, respectively), TM6CFTR (L346P) (decrease from 55% to 14%,), and TM12CFTR (ΔM1140) (decrease from 34% to 7%). Login to comment
116 One mutation, TM6CFTR (R334L), increased the insertion efficiency from 55% to 85%, as expected for a charged-to-hydrophobic replacement. Login to comment
120 Mutations TM6VCFTR (I336K), TM6VCFTR (I340N), and TM6VCFTR (L346P) still caused a large decrease in membrane insertion (from 81% to 39%, 35% and 14%, respectively). Login to comment
109 For CFTR, we chose mutations located in TM1CFTR (F87L, G91R), TM3CFTR (P205S, L206W), TM4CFTR (C225R), TM5CFTR (DF311, G314E), TM6CFTR (R334L/W, I336K/R/D, I340N/S, L346P, R347L/H), TM8CFTR (S909I, S912L), TM9CFTR (I1005R, A1006E), TM10CFTR (Y1032N), and TM12CFTR (M1137R, ƊM1140, M1140K), or close to the TM region of TM1CFTR (R74W, L102R/P), TMF2CFTR (R117P/L, L137P), and TM11CFTR (M1101K/R). Login to comment
111 As seen in Supplementary Data Table S2, only a few of the tested mutations in the 19 residue long CFTR TM segments alter the insertion efficiency significantly: TM4CFTR (C225R) (decrease from 88% to 34%), TM6CFTR (I336K/R/D) (decrease from 55% to 34%, 36% and 35%, respectively), TM6CFTR (I340N/S) (decrease from 55% to 32% and 35%, respectively), TM6CFTR (L346P) (decrease from 55% to 14%,), and TM12CFTR (ƊM1140) (decrease from 34% to 7%). Login to comment