CFTR
entrez
1080
canonical
uniprot
P13569
canonical
ensembl
ENSG00000001626
resolver
ensp
ENSP00000003084
resolver
genesymbol
CFTR
resolver
genesymbol_syn
ABCC7
resolver
hgnc
HGNC:1884
resolver
uniprot
Q20BG8
resolver
uniprot
Q20BH2
resolver
uniprot
Q2I0A1
resolver
uniprot
Q2I102
resolver
uniprot_entry
CFTR_HUMAN
resolver
uniprot_sec
Q20BG8
resolver
uniprot_sec
Q20BH2
resolver
uniprot_sec
Q2I0A1
resolver
uniprot_sec
Q2I102
resolver
amino_acid_sequence
MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
uniprot
proteins
disease_involvement
DISEASE: Cystic fibrosis (CF) [MIM:219700]: A common generalized disorder of the exocrine glands which impairs clearance of secretions in a variety of organs. It is characterized by the triad of chronic bronchopulmonary disease (with recurrent respiratory infections), pancreatic insufficiency (which leads to malabsorption and growth retardation) and elevated sweat electrolytes. It is the most common genetic disease in Caucasians, with a prevalence of about 1 in 2'000 live births. Inheritance is autosomal recessive. {ECO:0000269|PubMed:10094564, ECO:0000269|PubMed:10869121, ECO:0000269|PubMed:10923036, ECO:0000269|PubMed:11242048, ECO:0000269|PubMed:12167682, ECO:0000269|PubMed:12394343, ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:1284466, ECO:0000269|PubMed:1284468, ECO:0000269|PubMed:1284529, ECO:0000269|PubMed:1284530, ECO:0000269|PubMed:1284548, ECO:0000269|PubMed:1379210, ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:15716351, ECO:0000269|PubMed:16822950, ECO:0000269|PubMed:1695717, ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:17098864, ECO:0000269|PubMed:1710600, ECO:0000269|PubMed:1712898, ECO:0000269|PubMed:17182731, ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:20150177, ECO:0000269|PubMed:20691141, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:2236053, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:27241308, ECO:0000269|PubMed:28001373, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:32026723, ECO:0000269|PubMed:33572515, ECO:0000269|PubMed:7504969, ECO:0000269|PubMed:7505694, ECO:0000269|PubMed:7505767, ECO:0000269|PubMed:7508414, ECO:0000269|PubMed:7513296, ECO:0000269|PubMed:7517264, ECO:0000269|PubMed:7520022, ECO:0000269|PubMed:7522211, ECO:0000269|PubMed:7524909, ECO:0000269|PubMed:7524913, ECO:0000269|PubMed:7525450, ECO:0000269|PubMed:7537150, ECO:0000269|PubMed:7541273, ECO:0000269|PubMed:7541510, ECO:0000269|PubMed:7543567, ECO:0000269|PubMed:7544319, ECO:0000269|PubMed:7581407, ECO:0000269|PubMed:7606851, ECO:0000269|PubMed:7680525, ECO:0000269|PubMed:7683628, ECO:0000269|PubMed:7683954, ECO:0000269|PubMed:8081395, ECO:0000269|PubMed:8406518, ECO:0000269|PubMed:8522333, ECO:0000269|PubMed:8723693, ECO:0000269|PubMed:8723695, ECO:0000269|PubMed:8800923, ECO:0000269|PubMed:8829633, ECO:0000269|PubMed:8910473, ECO:0000269|PubMed:8956039, ECO:0000269|PubMed:9101301, ECO:0000269|PubMed:9222768, ECO:0000269|PubMed:9375855, ECO:0000269|PubMed:9401006, ECO:0000269|PubMed:9443874, ECO:0000269|PubMed:9452048, ECO:0000269|PubMed:9452054, ECO:0000269|PubMed:9452073, ECO:0000269|PubMed:9482579, ECO:0000269|PubMed:9507391, ECO:0000269|PubMed:9521595, ECO:0000269|PubMed:9554753, ECO:0000269|PubMed:9736778, ECO:0000269|PubMed:9804160, ECO:0000269|PubMed:9921909}. Note=The disease is caused by variants affecting the gene represented in this entry. There is some evidence that the functional defect caused by the most common variant Phe-508 DEL can be corrected by the binding to the snake phospholipase A2 crotoxin basic subunit CB. This toxin both disrupts the Phe-508 DEL-cytokeratin 8 complex, allowing for the escape from degradation, and increases the chloride channel current (PubMed:27241308). {ECO:0000269|PubMed:27241308}.; DISEASE: Congenital bilateral absence of the vas deferens (CBAVD) [MIM:277180]: An autosomal recessive disease characterized by vas deferens aplasia resulting in azoospermia and male infertility. CBAVD may occur in isolation or as a manifestation of cystic fibrosis. {ECO:0000269|PubMed:10066035, ECO:0000269|PubMed:10651488, ECO:0000269|PubMed:17329263, ECO:0000269|PubMed:7529962, ECO:0000269|PubMed:7539342, ECO:0000269|PubMed:9067761, ECO:0000269|PubMed:9736778, ECO:0000269|Ref.118}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.1.6
uniprot
proteins
function
FUNCTION: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:12529365, PubMed:12588899, PubMed:12727866, PubMed:15010471, PubMed:17036051, PubMed:1712898, PubMed:17182731, PubMed:19398555, PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:26846474, PubMed:28087700, PubMed:8910473, PubMed:9804160). Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (PubMed:11524016, PubMed:15284228, PubMed:26627831, PubMed:8910473). The ion channel is also permeable to HCO(3)(-); selectivity depends on the extracellular chloride concentration (PubMed:15010471, PubMed:19019741). In vitro, mediates ATP-dependent glutathione flux (PubMed:12727866). Exerts its function also by modulating the activity of other ion channels and transporters (PubMed:12403779, PubMed:22121115, PubMed:22178883, PubMed:27941075). Plays an important role in airway fluid homeostasis (PubMed:16645176, PubMed:19621064, PubMed:26823428). Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens (PubMed:14668433, PubMed:16645176, PubMed:26823428). Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex (PubMed:17182731, PubMed:17434346, PubMed:27941075). Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731). Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731, PubMed:27941075). May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7 (PubMed:12403779). Can inhibit the chloride channel activity of ANO1 (PubMed:22178883). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:19923167, PubMed:27714810, PubMed:29393851). {ECO:0000269|PubMed:10792060, ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:12403779, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:12588899, ECO:0000269|PubMed:12727866, ECO:0000269|PubMed:14668433, ECO:0000269|PubMed:15010471, ECO:0000269|PubMed:15284228, ECO:0000269|PubMed:16645176, ECO:0000269|PubMed:17036051, ECO:0000269|PubMed:1712898, ECO:0000269|PubMed:17182731, ECO:0000269|PubMed:19019741, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:19621064, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:26627831, ECO:0000269|PubMed:26823428, ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:27714810, ECO:0000269|PubMed:27941075, ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:29393851, ECO:0000269|PubMed:8910473, ECO:0000269|PubMed:9804160, ECO:0000305|PubMed:19923167}.
uniprot
proteins
mass_dalton
168142
uniprot
proteins
mutagenesis
MUTAGEN 347; /note="R->D: Decreases glutathione uptake. Increases affinity for glutathione."; /evidence="ECO:0000269|PubMed:12727866"; MUTAGEN 464; /note="K->A: Decreases glutathione uptake."; /evidence="ECO:0000269|PubMed:12727866"; MUTAGEN 464; /note="K->M: Impaired maturation of glycan chains indicating impaired trafficking from the endoplasmic reticulum to the cell membrane."; /evidence="ECO:0000269|PubMed:1699669"; MUTAGEN 508; /note="F->R: Impaired maturation of glycan chains indicating impaired trafficking from the endoplasmic reticulum to the cell membrane."; /evidence="ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:1712898"; MUTAGEN 539; /note="I->T: Enhances trafficking from the endoplasmic reticulum to the cell membrane."; /evidence="ECO:0000269|PubMed:28001373"; MUTAGEN 894; /note="N->D: Abolishes N-glycosylation, enhances endocytosis and impairs subsequent recycling to the cell surface; when associated with D-900."; /evidence="ECO:0000269|PubMed:20008117"; MUTAGEN 900; /note="N->D: Abolishes N-glycosylation, enhances endocytosis and impairs subsequent recycling to the cell surface; when associated with D-894."; /evidence="ECO:0000269|PubMed:20008117"; MUTAGEN 1137; /note="M->R: Abolishes channel activity. Impairs protein maturation, suggesting the protein is retained in the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:9804160"; MUTAGEN 1139; /note="I->V: Decreases channel activity, no visible effect on protein maturation."; /evidence="ECO:0000269|PubMed:9804160"; MUTAGEN 1154; /note="D->G: Decreases channel activity, no visible effect on protein maturation."; /evidence="ECO:0000269|PubMed:9804160"; MUTAGEN 1250; /note="K->A: Decreases glutathione uptake."; /evidence="ECO:0000269|PubMed:12727866"; MUTAGEN 1250; /note="K->M: No effect on maturation of glycans, suggesting that trafficking to the plasma membrane is not altered."; /evidence="ECO:0000269|PubMed:1699669"; MUTAGEN 1478..1480; /note="Missing: Reduces interaction with MARCHF2 and abolishes subsequent MARCHF2-mediated degradation. No effect on localization to the Golgi."; /evidence="ECO:0000269|PubMed:23818989
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:28067262}.; PTM: Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel (PubMed:12588899, PubMed:17036051, PubMed:8910473). Dephosphorylation decreases the ATPase activity (in vitro) (PubMed:8910473). Phosphorylation at PKA sites activates the channel (PubMed:10792060, PubMed:12519745, PubMed:12588899, PubMed:25330774). Phosphorylation at PKC sites enhances the response to phosphorylation by PKA (PubMed:12588899). Phosphorylated by AMPK; this inhibits channel activity (PubMed:12519745). {ECO:0000269|PubMed:10792060, ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:12588899, ECO:0000269|PubMed:1377674, ECO:0000269|PubMed:17036051, ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:8910473, ECO:0000269|PubMed:9385646}.; PTM: Ubiquitinated, leading to its degradation in the lysosome (PubMed:19398555, PubMed:23818989). Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane (PubMed:19398555). Ubiquitinated by RNF185 during ER stress (PubMed:24019521). Ubiquitinated by MARCHF2 (PubMed:23818989). {ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:23818989, ECO:0000269|PubMed:24019521}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCC family
uniprot
proteins
protein_family
CFTR transporter (TC 3.A.1.202) subfamily
uniprot
proteins
pubmed
10066035
uniprot
proteins
pubmed
10094564
uniprot
proteins
pubmed
10651488
uniprot
proteins
pubmed
10766763
uniprot
proteins
pubmed
10792060
uniprot
proteins
pubmed
10869121
uniprot
proteins
pubmed
10923036
uniprot
proteins
pubmed
11242048
uniprot
proteins
pubmed
11304524
uniprot
proteins
pubmed
11524016
uniprot
proteins
pubmed
11707463
uniprot
proteins
pubmed
12167682
uniprot
proteins
pubmed
12394343
uniprot
proteins
pubmed
12403779
uniprot
proteins
pubmed
12519745
uniprot
proteins
pubmed
12529365
uniprot
proteins
pubmed
12588899
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12727866
uniprot
proteins
pubmed
1284466
uniprot
proteins
pubmed
1284468
uniprot
proteins
pubmed
1284529
uniprot
proteins
pubmed
1284530
uniprot
proteins
pubmed
1284534
uniprot
proteins
pubmed
1284548
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
12913074
uniprot
proteins
pubmed
1377674
uniprot
proteins
pubmed
1378801
uniprot
proteins
pubmed
1379210
uniprot
proteins
pubmed
14668433
uniprot
proteins
pubmed
15010471
uniprot
proteins
pubmed
15247260
uniprot
proteins
pubmed
15284228
uniprot
proteins
pubmed
15528182
uniprot
proteins
pubmed
15716351
uniprot
proteins
pubmed
16331976
uniprot
proteins
pubmed
16645176
uniprot
proteins
pubmed
16822950
uniprot
proteins
pubmed
1695717
uniprot
proteins
pubmed
1699669
uniprot
proteins
pubmed
17036051
uniprot
proteins
pubmed
17098864
uniprot
proteins
pubmed
1710598
uniprot
proteins
pubmed
1710600
uniprot
proteins
pubmed
1712898
uniprot
proteins
pubmed
17182731
uniprot
proteins
pubmed
17329263
uniprot
proteins
pubmed
17434346
uniprot
proteins
pubmed
17462998
uniprot
proteins
pubmed
17660831
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
19019741
uniprot
proteins
pubmed
19398555
uniprot
proteins
pubmed
19621064
uniprot
proteins
pubmed
19923167
uniprot
proteins
pubmed
19944699
uniprot
proteins
pubmed
20008117
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20150177
uniprot
proteins
pubmed
20691141
uniprot
proteins
pubmed
20933420
uniprot
proteins
pubmed
21884936
uniprot
proteins
pubmed
21931164
uniprot
proteins
pubmed
22119790
uniprot
proteins
pubmed
22121115
uniprot
proteins
pubmed
22178883
uniprot
proteins
pubmed
22207244
uniprot
proteins
pubmed
2236053
uniprot
proteins
pubmed
23818989
uniprot
proteins
pubmed
24019521
uniprot
proteins
pubmed
2475911
uniprot
proteins
pubmed
25330774
uniprot
proteins
pubmed
26444971
uniprot
proteins
pubmed
26627831
uniprot
proteins
pubmed
26823428
uniprot
proteins
pubmed
26846474
uniprot
proteins
pubmed
27241308
uniprot
proteins
pubmed
27714810
uniprot
proteins
pubmed
27941075
uniprot
proteins
pubmed
28001373
uniprot
proteins
pubmed
28067262
uniprot
proteins
pubmed
28087700
uniprot
proteins
pubmed
28130590
uniprot
proteins
pubmed
29393851
uniprot
proteins
pubmed
32026723
uniprot
proteins
pubmed
33572515
uniprot
proteins
pubmed
7504969
uniprot
proteins
pubmed
7505694
uniprot
proteins
pubmed
7505767
uniprot
proteins
pubmed
7508414
uniprot
proteins
pubmed
7513296
uniprot
proteins
pubmed
7517264
uniprot
proteins
pubmed
7518437
uniprot
proteins
pubmed
7520022
uniprot
proteins
pubmed
7522211
uniprot
proteins
pubmed
7524909
uniprot
proteins
pubmed
7524913
uniprot
proteins
pubmed
7525450
uniprot
proteins
pubmed
7529962
uniprot
proteins
pubmed
7537150
uniprot
proteins
pubmed
7539342
uniprot
proteins
pubmed
7541273
uniprot
proteins
pubmed
7541510
uniprot
proteins
pubmed
7543567
uniprot
proteins
pubmed
7544319
uniprot
proteins
pubmed
7581407
uniprot
proteins
pubmed
7606851
uniprot
proteins
pubmed
7680525
uniprot
proteins
pubmed
7683628
uniprot
proteins
pubmed
7683954
uniprot
proteins
pubmed
8081395
uniprot
proteins
pubmed
8406518
uniprot
proteins
pubmed
8522333
uniprot
proteins
pubmed
8723693
uniprot
proteins
pubmed
8723695
uniprot
proteins
pubmed
8800923
uniprot
proteins
pubmed
8829633
uniprot
proteins
pubmed
8910473
uniprot
proteins
pubmed
8956039
uniprot
proteins
pubmed
9067761
uniprot
proteins
pubmed
9101301
uniprot
proteins
pubmed
9222768
uniprot
proteins
pubmed
9375855
uniprot
proteins
pubmed
9385646
uniprot
proteins
pubmed
9401006
uniprot
proteins
pubmed
9443874
uniprot
proteins
pubmed
9452048
uniprot
proteins
pubmed
9452054
uniprot
proteins
pubmed
9452073
uniprot
proteins
pubmed
9482579
uniprot
proteins
pubmed
9507391
uniprot
proteins
pubmed
9517543
uniprot
proteins
pubmed
9521595
uniprot
proteins
pubmed
9554753
uniprot
proteins
pubmed
9736778
uniprot
proteins
pubmed
9804160
uniprot
proteins
pubmed
9921909
uniprot
proteins
sequence_length
1480
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:1284548, ECO:0000269|PubMed:15247260, ECO:0000269|PubMed:15716351, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:19621064, ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:28130590}; Multi-pass membrane protein {ECO:0000269|Ref.57}. Early endosome membrane {ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20008117}; Multi-pass membrane protein {ECO:0000269|Ref.57}. Cell membrane {ECO:0000269|PubMed:10792060, ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:12588899, ECO:0000269|PubMed:15010471, ECO:0000269|PubMed:17036051, ECO:0000269|PubMed:1712898, ECO:0000269|PubMed:17182731, ECO:0000269|PubMed:19019741, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:22178883, ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:28001373, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:28130590, ECO:0000269|PubMed:9804160, ECO:0000305|PubMed:8910473}; Multi-pass membrane protein {ECO:0000269|Ref.57}. Recycling endosome membrane {ECO:0000305|PubMed:17462998}; Multi-pass membrane protein {ECO:0000269|Ref.57}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:25330774}; Multi-pass membrane protein {ECO:0000269|Ref.57}. Nucleus {ECO:0000250|UniProtKB:P34158}. Note=The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (PubMed:17462998, PubMed:19398555, PubMed:20008117). In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (PubMed:22207244). In Sertoli cells, a processed product is detected in the nucleus (By similarity). ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936). {ECO:0000250|UniProtKB:P34158, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:22207244, ECO:0000305|PubMed:17462998}.
uniprot
proteins
transmembrane_region
TRANSMEM 78..98; /note="Helical; Name=1"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 123..146; /note="Helical; Name=2"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 196..216; /note="Helical; Name=3"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 223..243; /note="Helical; Name=4"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 299..319; /note="Helical; Name=5"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 340..358; /note="Helical; Name=6"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 859..879; /note="Helical; Name=7"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 919..939; /note="Discontinuously helical; Name=8"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 991..1011; /note="Helical; Name=9"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 1014..1034; /note="Helical; Name=10"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 1096..1116; /note="Helical; Name=11"; /evidence="ECO:0000269|Ref.57"; TRANSMEM 1131..1151; /note="Helical; Name=12"; /evidence="ECO:0000269|Ref.57
uniprot
proteins