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Cystic fibrosis transmembrane conductance regulator (CFTR) (ATP-binding cassette sub-family C member 7) (Channel conductance-controlling ATPase) (EC 3.6.3.49) (cAMP-dependent chloride channel)

 CFTR_HUMAN              Reviewed;        1480 AA.
P13569; Q20BG8; Q20BH2; Q2I0A1; Q2I102;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 3.
30-AUG-2017, entry version 229.
RecName: Full=Cystic fibrosis transmembrane conductance regulator;
Short=CFTR;
AltName: Full=ATP-binding cassette sub-family C member 7;
AltName: Full=Channel conductance-controlling ATPase;
EC=3.6.3.49 {ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:15284228, ECO:0000269|PubMed:26627831, ECO:0000269|PubMed:8910473};
AltName: Full=cAMP-dependent chloride channel;
Name=CFTR; Synonyms=ABCC7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-470.
PubMed=2475911; DOI=10.1126/science.2475911;
Riordan J.R., Rommens J.M., Kerem B., Alon N., Rozmahel R.,
Grzelczak Z., Zielenski J., Lok S., Plavsic N., Chou J.-L.,
Drumm M.L., Iannuzzi M.C., Collins F.S., Tsui L.-C.;
"Identification of the cystic fibrosis gene: cloning and
characterization of complementary DNA.";
Science 245:1066-1073(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-470.
PubMed=1710598; DOI=10.1016/0888-7543(91)90503-7;
Zielenski J., Rozmahel R., Bozon D., Kerem B., Grzelczak Z.,
Riordan J.R., Rommens J., Tsui L.-C.;
"Genomic DNA sequence of the cystic fibrosis transmembrane conductance
regulator (CFTR) gene.";
Genomics 10:214-228(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-470 AND TRP-1453.
Stacy R., Subramanian S., Deodato C., Burkhardt P., Song Y.,
Paddock M., Chang J., Zhou Y., Haugen E., Waring D., Chapman P.,
Hayden H., Levy R., Wu Z., Rouse G., James R., Phelps K., Olson M.V.,
Kaul R.;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-737; SER-768;
SER-790; SER-795 AND SER-813.
PubMed=1377674;
Picciotto M.R., Cohn J.A., Bertuzzi G., Greenguard P., Nairn A.C.;
"Phosphorylation of the cystic fibrosis transmembrane conductance
regulator.";
J. Biol. Chem. 267:12742-12752(1992).
[7]
GLYCOSYLATION AT ASN-894 AND ASN-900, AND TOPOLOGY.
PubMed=7518437;
Chang X.-B., Hou Y.-X., Jensen T.J., Riordan J.R.;
"Mapping of cystic fibrosis transmembrane conductance regulator
membrane topology by glycosylation site insertion.";
J. Biol. Chem. 269:18572-18575(1994).
[8]
PHOSPHORYLATION AT SER-660; SER-700; SER-712; SER-737; SER-753;
SER-768; SER-795 AND SER-813.
PubMed=9385646; DOI=10.1002/pro.5560061117;
Neville D.C.A., Rozanas C.R., Rice E.M., Gruis D.B., Verkman A.S.,
Townsend R.R.;
"Evidence for phosphorylation of serine 753 in CFTR using a novel
metal-ion affinity resin and matrix-assisted laser desorption mass
spectrometry.";
Protein Sci. 6:2436-2445(1997).
[9]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=10766763; DOI=10.1074/jbc.M910165199;
Pagani F., Buratti E., Stuani C., Romano M., Zuccato E., Niksic M.,
Giglio L., Faraguna D., Baralle F.E.;
"Splicing factors induce cystic fibrosis transmembrane regulator exon
9 skipping through a nonevolutionary conserved intronic element.";
J. Biol. Chem. 275:21041-21047(2000).
[10]
DOMAIN, FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=10792060; DOI=10.1073/pnas.100588797;
Ostedgaard L.S., Baldursson O., Vermeer D.W., Welsh M.J.,
Robertson A.D.;
"A functional R domain from cystic fibrosis transmembrane conductance
regulator is predominantly unstructured in solution.";
Proc. Natl. Acad. Sci. U.S.A. 97:5657-5662(2000).
[11]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=11524016; DOI=10.1021/bi0108195;
Ramjeesingh M., Li C., Kogan I., Wang Y., Huan L.J., Bear C.E.;
"A monomer is the minimum functional unit required for channel and
ATPase activity of the cystic fibrosis transmembrane conductance
regulator.";
Biochemistry 40:10700-10706(2001).
[12]
INTERACTION WITH GOPC, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11707463; DOI=10.1074/jbc.M110177200;
Cheng J., Moyer B.D., Milewski M., Loffing J., Ikeda M., Mickle J.E.,
Cutting G.R., Li M., Stanton B.A., Guggino W.B.;
"A Golgi-associated PDZ domain protein modulates cystic fibrosis
transmembrane regulator plasma membrane expression.";
J. Biol. Chem. 277:3520-3529(2002).
[13]
INTERACTION WITH SLC4A7 AND SLC9A3R1, AND FUNCTION.
PubMed=12403779; DOI=10.1074/jbc.M201862200;
Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A.,
Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.;
"The cystic fibrosis transmembrane conductance regulator interacts
with and regulates the activity of the HCO3- salvage transporter human
Na+-HCO3-cotransport isoform 3.";
J. Biol. Chem. 277:50503-50509(2002).
[14]
PHOSPHORYLATION BY AMPK, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12519745; DOI=10.1152/ajpcell.00227.2002;
Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.;
"Physiological modulation of CFTR activity by AMP-activated protein
kinase in polarized T84 cells.";
Am. J. Physiol. 284:C1297-C1308(2003).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15010471; DOI=10.1074/jbc.M313323200;
Shcheynikov N., Kim K.H., Kim K.M., Dorwart M.R., Ko S.B., Goto H.,
Naruse S., Thomas P.J., Muallem S.;
"Dynamic control of cystic fibrosis transmembrane conductance
regulator Cl(-)/HCO3(-) selectivity by external Cl(-).";
J. Biol. Chem. 279:21857-21865(2004).
[16]
INTERACTION WITH MYO6, AND SUBCELLULAR LOCATION.
PubMed=15247260; DOI=10.1074/jbc.M403141200;
Swiatecka-Urban A., Boyd C., Coutermarsh B., Karlson K.H., Barnaby R.,
Aschenbrenner L., Langford G.M., Hasson T., Stanton B.A.;
"Myosin VI regulates endocytosis of the cystic fibrosis transmembrane
conductance regulator.";
J. Biol. Chem. 279:38025-38031(2004).
[17]
REVIEW.
PubMed=1378801;
McIntosh I., Cutting G.R.;
"Cystic fibrosis transmembrane conductance regulator and the etiology
and pathogenesis of cystic fibrosis.";
FASEB J. 6:2775-2782(1992).
[18]
ALTERNATIVE SPLICING (ISOFORM 3).
PubMed=12913074; DOI=10.1093/hmg/ddg215;
Aznarez I., Chan E.M., Zielenski J., Blencowe B.J., Tsui L.-C.;
"Characterization of disease-associated mutations affecting an exonic
splicing enhancer and two cryptic splice sites in exon 13 of the
cystic fibrosis transmembrane conductance regulator gene.";
Hum. Mol. Genet. 12:2031-2040(2003).
[19]
CHANNEL GATING REGULATION, PHOSPHORYLATION, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=12588899; DOI=10.1113/jphysiol.2002.035790;
Chappe V., Hinkson D.A., Zhu T., Chang X.B., Riordan J.R.,
Hanrahan J.W.;
"Phosphorylation of protein kinase C sites in NBD1 and the R domain
control CFTR channel activation by PKA.";
J. Physiol. (Lond.) 548:39-52(2003).
[20]
FUNCTION.
PubMed=14668433; DOI=10.1073/pnas.2634339100;
Coakley R.D., Grubb B.R., Paradiso A.M., Gatzy J.T., Johnson L.G.,
Kreda S.M., O'Neal W.K., Boucher R.C.;
"Abnormal surface liquid pH regulation by cultured cystic fibrosis
bronchial epithelium.";
Proc. Natl. Acad. Sci. U.S.A. 100:16083-16088(2003).
[21]
CATALYTIC ACTIVITY, AND DOMAIN.
PubMed=15284228; DOI=10.1074/jbc.M407666200;
Kidd J.F., Ramjeesingh M., Stratford F., Huan L.J., Bear C.E.;
"A heteromeric complex of the two nucleotide binding domains of cystic
fibrosis transmembrane conductance regulator (CFTR) mediates ATPase
activity.";
J. Biol. Chem. 279:41664-41669(2004).
[22]
FUNCTION.
PubMed=16645176; DOI=10.1164/rccm.200506-987OC;
Blouquit S., Regnier A., Dannhoffer L., Fermanian C., Naline E.,
Boucher R., Chinet T.;
"Ion and fluid transport properties of small airways in cystic
fibrosis.";
Am. J. Respir. Crit. Care Med. 174:299-305(2006).
[23]
DOMAIN, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17036051; DOI=10.1038/sj.emboj.7601373;
Mense M., Vergani P., White D.M., Altberg G., Nairn A.C., Gadsby D.C.;
"In vivo phosphorylation of CFTR promotes formation of a nucleotide-
binding domain heterodimer.";
EMBO J. 25:4728-4739(2006).
[24]
IDENTIFICATION IN A COMPLEX WITH RAB11A AND MYO5B, AND SUBCELLULAR
LOCATION.
PubMed=17462998; DOI=10.1074/jbc.M608531200;
Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S.,
Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E.,
Langford G.M., Fukuda M., Stanton B.A.;
"Myosin Vb is required for trafficking of the cystic fibrosis
transmembrane conductance regulator in Rab11a-specific apical
recycling endosomes in polarized human airway epithelial cells.";
J. Biol. Chem. 282:23725-23736(2007).
[25]
FUNCTION.
PubMed=17434346; DOI=10.1016/j.jcf.2007.03.001;
Lu C., Jiang C., Pribanic S., Rotin D.;
"CFTR stabilizes ENaC at the plasma membrane.";
J. Cyst. Fibros. 6:419-422(2007).
[26]
DOMAIN.
PubMed=17660831; DOI=10.1038/nsmb1278;
Baker J.M., Hudson R.P., Kanelis V., Choy W.Y., Thibodeau P.H.,
Thomas P.J., Forman-Kay J.D.;
"CFTR regulatory region interacts with NBD1 predominantly via multiple
transient helices.";
Nat. Struct. Mol. Biol. 14:738-745(2007).
[27]
UBIQUITINATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19398555; DOI=10.1074/jbc.M109.001685;
Bomberger J.M., Barnaby R.L., Stanton B.A.;
"The deubiquitinating enzyme USP10 regulates the post-endocytic
sorting of cystic fibrosis transmembrane conductance regulator in
airway epithelial cells.";
J. Biol. Chem. 284:18778-18789(2009).
[28]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19019741; DOI=10.1016/j.jcf.2008.10.004;
Tang L., Fatehi M., Linsdell P.;
"Mechanism of direct bicarbonate transport by the CFTR anion
channel.";
J. Cyst. Fibros. 8:115-121(2009).
[29]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19621064; DOI=10.1371/journal.pbio.1000155;
Zhang L., Button B., Gabriel S.E., Burkett S., Yan Y.,
Skiadopoulos M.H., Dang Y.L., Vogel L.N., McKay T., Mengos A.,
Boucher R.C., Collins P.L., Pickles R.J.;
"CFTR delivery to 25% of surface epithelial cells restores normal
rates of mucus transport to human cystic fibrosis airway epithelium.";
PLoS Biol. 7:E1000155-E1000155(2009).
[30]
INTERACTION WITH CSE1L.
PubMed=20933420; DOI=10.1016/j.cub.2010.09.012;
Bagnat M., Navis A., Herbstreith S., Brand-Arzamendi K., Curado S.,
Gabriel S., Mostov K., Huisken J., Stainier D.Y.;
"Cse1l is a negative regulator of CFTR-dependent fluid secretion.";
Curr. Biol. 20:1840-1845(2010).
[31]
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT CF PHE-508 DEL,
MUTAGENESIS OF ASN-894 AND ASN-900, AND GLYCOSYLATION AT ASN-894 AND
ASN-900.
PubMed=20008117; DOI=10.1152/ajplung.00016.2009;
Cholon D.M., O'Neal W.K., Randell S.H., Riordan J.R., Gentzsch M.;
"Modulation of endocytic trafficking and apical stability of CFTR in
primary human airway epithelial cultures.";
Am. J. Physiol. 298:L304-L314(2010).
[32]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19923167; DOI=10.1093/humrep/dep406;
Li C.Y., Jiang L.Y., Chen W.Y., Li K., Sheng H.Q., Ni Y., Lu J.X.,
Xu W.X., Zhang S.Y., Shi Q.X.;
"CFTR is essential for sperm fertilizing capacity and is correlated
with sperm quality in humans.";
Hum. Reprod. 25:317-327(2010).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ANO1.
PubMed=22178883; DOI=10.1159/000335765;
Ousingsawat J., Kongsuphol P., Schreiber R., Kunzelmann K.;
"CFTR and TMEM16A are separate but functionally related Cl-channels.";
Cell. Physiol. Biochem. 28:715-724(2011).
[35]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22207244; DOI=10.1007/s00418-011-0904-1;
Enuka Y., Hanukoglu I., Edelheit O., Vaknine H., Hanukoglu A.;
"Epithelial sodium channels (ENaC) are uniformly distributed on motile
cilia in the oviduct and the respiratory airways.";
Histochem. Cell Biol. 137:339-353(2012).
[36]
INTERACTION WITH SLC26A8.
PubMed=22121115; DOI=10.1093/hmg/ddr558;
Rode B., Dirami T., Bakouh N., Rizk-Rabin M., Norez C., Lhuillier P.,
Lores P., Jollivet M., Melin P., Zvetkova I., Bienvenu T., Becq F.,
Planelles G., Edelman A., Gacon G., Toure A.;
"The testis anion transporter TAT1 (SLC26A8) physically and
functionally interacts with the cystic fibrosis transmembrane
conductance regulator channel: a potential role during sperm
capacitation.";
Hum. Mol. Genet. 21:1287-1298(2012).
[37]
PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;
SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,
PALMITOYLATION AT CYS-524 AND CYS-1395, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=22119790; DOI=10.1093/protein/gzr054;
McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,
Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.;
"Purification of CFTR for mass spectrometry analysis: identification
of palmitoylation and other post-translational modifications.";
Protein Eng. Des. Sel. 25:7-14(2012).
[38]
UBIQUITINATION BY RNF185.
PubMed=24019521; DOI=10.1074/jbc.M113.470500;
El Khouri E., Le Pavec G., Toledano M.B., Delaunay-Moisan A.;
"RNF185 is a novel E3 ligase of endoplasmic reticulum-associated
degradation (ERAD) that targets cystic fibrosis transmembrane
conductance regulator (CFTR).";
J. Biol. Chem. 288:31177-31191(2013).
[39]
FUNCTION, CHARACTERIZATION OF CF VARIANT PHE-508 DEL, SUBCELLULAR
LOCATION, PHOSPHORYLATION AT SER-660; SER-670; SER-700; SER-712;
SER-737; SER-753; SER-768; SER-795 AND SER-813, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=25330774; DOI=10.1002/pmic.201400218;
Pasyk S., Molinski S., Ahmadi S., Ramjeesingh M., Huan L.J., Chin S.,
Du K., Yeger H., Taylor P., Moran M.F., Bear C.E.;
"The major cystic fibrosis causing mutation exhibits defective
propensity for phosphorylation.";
Proteomics 15:447-461(2015).
[40]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=26627831; DOI=10.1074/jbc.M115.704809;
Ehrhardt A., Chung W.J., Pyle L.C., Wang W., Nowotarski K.,
Mulvihill C.M., Ramjeesingh M., Hong J., Velu S.E., Lewis H.A.,
Atwell S., Aller S., Bear C.E., Lukacs G.L., Kirk K.L., Sorscher E.J.;
"Channel gating regulation by the cystic fibrosis transmembrane
conductance regulator (CFTR) first cytosolic loop.";
J. Biol. Chem. 291:1854-1865(2016).
[41]
FUNCTION.
PubMed=26823428; DOI=10.1126/science.aad5589;
Shah V.S., Meyerholz D.K., Tang X.X., Reznikov L., Abou Alaiwa M.,
Ernst S.E., Karp P.H., Wohlford-Lenane C.L., Heilmann K.P.,
Leidinger M.R., Allen P.D., Zabner J., McCray P.B. Jr.,
Ostedgaard L.S., Stoltz D.A., Randak C.O., Welsh M.J.;
"Airway acidification initiates host defense abnormalities in cystic
fibrosis mice.";
Science 351:503-507(2016).
[42]
FUNCTION.
PubMed=27941075; DOI=10.1152/ajplung.00375.2016;
Rauh R., Hoerner C., Korbmacher C.;
"deltabetagamma-ENaC is inhibited by CFTR but stimulated by cAMP in
Xenopus laevis oocytes.";
Am. J. Physiol. 312:L277-L287(2017).
[43]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=28130590; DOI=10.1007/s00418-016-1535-3;
Hanukoglu I., Boggula V.R., Vaknine H., Sharma S., Kleyman T.,
Hanukoglu A.;
"Expression of epithelial sodium channel (ENaC) and CFTR in the human
epidermis and epidermal appendages.";
Histochem. Cell Biol. 147:733-748(2017).
[44]
FUNCTION.
PubMed=27714810; DOI=10.1002/jcp.25634;
Puga Molina L.C., Pinto N.A., Torres Rodriguez P., Romarowski A.,
Vicens Sanchez A., Visconti P.E., Darszon A., Trevino C.L.,
Buffone M.G.;
"Essential role of CFTR in PKA-dependent phosphorylation,
alkalinization, and hyperpolarization during human sperm
capacitation.";
J. Cell. Physiol. 232:1404-1414(2017).
[45]
3D-STRUCTURE MODELING OF 425-638.
PubMed=9517543;
DOI=10.1002/(SICI)1097-0134(19980215)30:3<275::AID-PROT7>3.3.CO;2-L;
Hoedemaeker F.J., Davidson A.R., Rose D.R.;
"A model for the nucleotide-binding domains of ABC transporters based
on the large domain of aspartate aminotransferase.";
Proteins 30:275-286(1998).
[46]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1476-1480 IN COMPLEX WITH
SLC9A3R1.
PubMed=11304524; DOI=10.1074/jbc.C100154200;
Karthikeyan S., Leung T., Ladias J.A.A.;
"Structural basis of the Na+/H+ exchanger regulatory factor PDZ1
interaction with the carboxyl-terminal region of the cystic fibrosis
transmembrane conductance regulator.";
J. Biol. Chem. 276:19683-19686(2001).
[47] {ECO:0000244|PDB:2LOB}
STRUCTURE BY NMR OF 1473-1480 IN COMPLEX WITH GOPC.
PubMed=16331976; DOI=10.1021/bi0516475;
Piserchio A., Fellows A., Madden D.R., Mierke D.F.;
"Association of the cystic fibrosis transmembrane regulator with CAL:
structural features and molecular dynamics.";
Biochemistry 44:16158-16166(2005).
[48] {ECO:0000244|PDB:1XMI, ECO:0000244|PDB:1XMJ}
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 389-678 OF WILD-TYPE AND
VARIANT CF PHE-508 DEL IN COMPLEX WITH ATP, AND CHARACTERIZATION OF
VARIANT CF PHE-508 DEL.
PubMed=15528182; DOI=10.1074/jbc.M410968200;
Lewis H.A., Zhao X., Wang C., Sauder J.M., Rooney I., Noland B.W.,
Lorimer D., Kearins M.C., Conners K., Condon B., Maloney P.C.,
Guggino W.B., Hunt J.F., Emtage S.;
"Impact of the deltaF508 mutation in first nucleotide-binding domain
of human cystic fibrosis transmembrane conductance regulator on domain
folding and structure.";
J. Biol. Chem. 280:1346-1353(2005).
[49] {ECO:0000244|PDB:3GD7}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1193-1435 AND 1458-1470 IN
COMPLEX WITH ATP ANALOG.
Atwell S., Antonysamy S., Guggino W.B., Conners K., Emtage S.,
Gheyi T., Hunt J.F., Lewis H.A., Lu F., Sauder J.M., Weber P.C.,
Wetmore D., Zhao X.;
"Crystal structure of human NBD2 complexed with N6-phenylethyl-ATP (P-
ATP).";
Submitted (FEB-2009) to the PDB data bank.
[50] {ECO:0000244|PDB:2BBO, ECO:0000244|PDB:2BBS, ECO:0000244|PDB:2BBT}
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 389-677 IN COMPLEX WITH ATP.
PubMed=19944699; DOI=10.1016/j.jmb.2009.11.051;
Lewis H.A., Wang C., Zhao X., Hamuro Y., Conners K., Kearins M.C.,
Lu F., Sauder J.M., Molnar K.S., Coales S.J., Maloney P.C.,
Guggino W.B., Wetmore D.R., Weber P.C., Hunt J.F.;
"Structure and dynamics of NBD1 from CFTR characterized using
crystallography and hydrogen/deuterium exchange mass spectrometry.";
J. Mol. Biol. 396:406-430(2010).
[51] {ECO:0000244|PDB:2PZE, ECO:0000244|PDB:2PZF, ECO:0000244|PDB:2PZG}
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 387-646 IN COMPLEX WITH ATP,
AND CHARACTERIZATION OF VARIANT CF PHE-508 DEL.
PubMed=20150177; DOI=10.1093/protein/gzq004;
Atwell S., Brouillette C.G., Conners K., Emtage S., Gheyi T.,
Guggino W.B., Hendle J., Hunt J.F., Lewis H.A., Lu F.,
Protasevich I.I., Rodgers L.A., Romero R., Wasserman S.R., Weber P.C.,
Wetmore D., Zhang F.F., Zhao X.;
"Structures of a minimal human CFTR first nucleotide-binding domain as
a monomer, head-to-tail homodimer, and pathogenic mutant.";
Protein Eng. Des. Sel. 23:375-384(2010).
[52]
STRUCTURE BY ELECTRON MICROSCOPY (9 ANGSTROMS).
PubMed=21931164; DOI=10.1074/jbc.M111.292268;
Rosenberg M.F., O'Ryan L.P., Hughes G., Zhao Z., Aleksandrov L.A.,
Riordan J.R., Ford R.C.;
"The cystic fibrosis transmembrane conductance regulator (CFTR):
three-dimensional structure and localization of a channel gate.";
J. Biol. Chem. 286:42647-42654(2011).
[53] {ECO:0000244|PDB:4WZ6}
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 389-678.
PubMed=26444971; DOI=10.1002/pro.2821;
Hall J.D., Wang H., Byrnes L.J., Shanker S., Wang K., Efremov I.V.,
Chong P.A., Forman-Kay J.D., Aulabaugh A.E.;
"Binding screen for cystic fibrosis transmembrane conductance
regulator correctors finds new chemical matter and yields insights
into cystic fibrosis therapeutic strategy.";
Protein Sci. 25:360-373(2016).
[54] {ECO:0000244|PDB:5UAK}
STRUCTURE BY ELECTRON MICROSCOPY (3.87 ANGSTROMS), AND TOPOLOGY.
Liu F., Zhang Z., Chen J.;
"Structure of human cystic fibrosis transmembrane conductance
regulator (CFTR).";
Submitted (DEC-2016) to the PDB data bank.
[55]
REVIEW ON VARIANTS.
PubMed=1284534; DOI=10.1002/humu.1380010304;
Tsui L.-C.;
"Mutations and sequence variations detected in the cystic fibrosis
transmembrane conductance regulator (CFTR) gene: a report from the
Cystic Fibrosis Genetic Analysis Consortium.";
Hum. Mutat. 1:197-203(1992).
[56]
CHARACTERIZATION OF VARIANT CF TRP-334; ILE-507 DEL; PHE-508 DEL;
ASP-551 AND ILE-549, MUTAGENESIS OF LYS-464; PHE-508 AND LYS-1250, AND
GLYCOSYLATION.
PubMed=1699669; DOI=10.1016/0092-8674(90)90148-8;
Cheng S.H., Gregory R.J., Marshall J., Paul S., Souza D.W.,
White G.A., O'Riordan C.R., Smith A.E.;
"Defective intracellular transport and processing of CFTR is the
molecular basis of most cystic fibrosis.";
Cell 63:827-834(1990).
[57]
VARIANTS CF.
PubMed=1695717; DOI=10.1038/346366a0;
Cutting G.R., Kasch L.M., Rosenstein B.J., Zielenski J., Tsui L.-C.,
Antonarakis S.E., Kazazian H.H. Jr.;
"A cluster of cystic fibrosis mutations in the first nucleotide-
binding fold of the cystic fibrosis conductance regulator protein.";
Nature 346:366-369(1990).
[58]
VARIANTS CF.
PubMed=2236053; DOI=10.1073/pnas.87.21.8447;
Kerem B.-S., Zielenski J., Markiewicz D., Bozon D., Gazit E.,
Yahav J., Kennedy D., Riordan J.R., Collins F.S., Rommens J.M.,
Tsui L.-C.;
"Identification of mutations in regions corresponding to the two
putative nucleotide (ATP)-binding folds of the cystic fibrosis gene.";
Proc. Natl. Acad. Sci. U.S.A. 87:8447-8451(1990).
[59]
VARIANTS CF.
PubMed=1710600; DOI=10.1016/0888-7543(91)90510-L;
White M.B., Krueger L.J., Holsclaw D.S. Jr., Gerrard B.C., Stewart C.,
Quittell L., Dolganov G., Baranov V., Ivaschenko T., Kapronov N.I.,
Sebastio G., Castiglione O., Dean M.;
"Detection of three rare frameshift mutations in the cystic fibrosis
gene in an African-American (CF444delA), an Italian (CF2522insC), and
a Soviet (CF3821delT).";
Genomics 10:266-269(1991).
[60]
CHARACTERIZATION OF CF VARIANTS ILE-507 DEL; PHE-508 DEL; ILE-549;
ARG-549; ASP-551; THR-559; ASN-572; LYS-1303 AND ASP-1349, FUNCTION,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-508.
PubMed=1712898; DOI=10.1128/MCB.11.8.3886;
Gregory R.J., Rich D.P., Cheng S.H., Souza D.W., Paul S.,
Manavalan P., Anderson M.P., Welsh M.J., Smith A.E.;
"Maturation and function of cystic fibrosis transmembrane conductance
regulator variants bearing mutations in putative nucleotide-binding
domains 1 and 2.";
Mol. Cell. Biol. 11:3886-3893(1991).
[61]
VARIANTS CF PHE-520 AND HIS-1291.
PubMed=1284466; DOI=10.1093/hmg/1.1.11;
Jones C.T., McIntosh I., Keston M., Ferguson A., Brock D.J.H.;
"Three novel mutations in the cystic fibrosis gene detected by
chemical cleavage: analysis of variant splicing and a nonsense
mutation.";
Hum. Mol. Genet. 1:11-17(1992).
[62]
VARIANT CF MET-1283.
PubMed=1284468; DOI=10.1093/hmg/1.2.123;
Cheadle J.P., Meredith A.L., Al-Jader L.N.;
"A new missense mutation (R1283M) in exon 20 of the cystic fibrosis
transmembrane conductance regulator gene.";
Hum. Mol. Genet. 1:123-125(1992).
[63]
VARIANT CF PRO-1255.
PubMed=1284530; DOI=10.1093/hmg/1.6.441;
Lissens W., Bonduelle M., Malfroot A., Dab I., Liebaers I.;
"A serine to proline substitution (S1255P) in the second nucleotide
binding fold of the cystic fibrosis gene.";
Hum. Mol. Genet. 1:441-442(1992).
[64]
VARIANTS CF LYS-92 AND CYS-117.
PubMed=1284529; DOI=10.1093/hmg/1.6.439;
Shackleton S., Beards F., Harris A.;
"Detection of novel and rare mutations in exon 4 of the cystic
fibrosis gene by SSCP.";
Hum. Mol. Genet. 1:439-440(1992).
[65]
CHARACTERIZATION OF VARIANT CF PHE-508 DEL AND ASP-551, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=1284548; DOI=10.1038/ng0892-321;
Kartner N., Augustinas O., Jensen T.J., Naismith A.L., Riordan J.R.;
"Mislocalization of delta F508 CFTR in cystic fibrosis sweat gland.";
Nat. Genet. 1:321-327(1992).
[66]
VARIANT CF LYS-1101.
PubMed=7680525;
Zielenski J., Fugiwara T.M., Markiewicz D., Paradis A.J.,
Anacleto A.I., Richards B., Schwartz R.H., Klinger K.W., Tsui L.-C.,
Morgan K.;
"Identification of the M1101K mutation in the cystic fibrosis
transmembrane conductance regulator (CFTR) gene and complete detection
of cystic fibrosis mutations in the Hutterite population.";
Am. J. Hum. Genet. 52:609-615(1993).
[67]
VARIANTS CF VAL-1052; ARG-1061; LEU-1066; GLN-1070; ARG-1085 AND
ARG-1101.
PubMed=7683628; DOI=10.1006/geno.1993.1183;
Mercier B., Lissens W., Novelli G., Kalaydjieva L., De Arce M.,
Kapranov N., Klain N.C., Lenoir G., Chauveau P., Lenaerts C.,
Rault G., Cashman S., Sangiuolo F., Audrezet M.-P., Dallapiccola B.,
Guillermit H., Bonduelle M., Liebaers I., Quere I., Verlingue C.,
Ferec C.;
"Identification of eight novel mutations in a collaborative analysis
of a part of the second transmembrane domain of the CFTR gene.";
Genomics 16:296-297(1993).
[68]
VARIANT CF LEU-693.
PubMed=8406518;
Audrezet M.P., Novelli G., Mercier B., Sangiuolo F., Maceratesi P.,
Ferec C., Dallapiccola B.;
"Identification of three novel cystic fibrosis mutations in a sample
of Italian cystic fibrosis patients.";
Hum. Hered. 43:295-300(1993).
[69]
VARIANT CF LYS-92.
PubMed=7683954; DOI=10.1093/hmg/2.1.79;
Nunes V., Chillon M., Doerk T., Tuemmler B., Casals T., Estivill X.;
"A new missense mutation (E92K) in the first transmembrane domain of
the CFTR gene causes a benign cystic fibrosis phenotype.";
Hum. Mol. Genet. 2:79-80(1993).
[70]
VARIANT CF SER-205.
PubMed=7505694; DOI=10.1093/hmg/2.10.1741;
Chillon M., Casals T., Nunes V., Gimenez J., Ruiz E.P., Estivill X.;
"Identification of a new missense mutation (P205S) in the first
transmembrane domain of the CFTR gene associated with a mild cystic
fibrosis phenotype.";
Hum. Mol. Genet. 2:1741-1742(1993).
[71]
VARIANTS CF.
PubMed=7504969; DOI=10.1002/humu.1380020511;
Gasparini P., Marigo C., Bisceglia G., Nicolis E., Zelante L.,
Bombieri C., Borgo G., Pignatti P.F., Cabrini G.;
"Screening of 62 mutations in a cohort of cystic fibrosis patients
from north eastern Italy: their incidence and clinical features of
defined genotypes.";
Hum. Mutat. 2:389-394(1993).
[72]
VARIANTS CYS-31 AND ILE-1220, AND VARIANTS CF LEU-912; TYR-949;
PRO-1065 AND PRO-1071.
PubMed=7522211; DOI=10.1006/geno.1994.1290;
Ghaneb N., Costes B., Girodon E., Martin J., Fanen P., Goossens M.;
"Identification of eight mutations and three sequence variations in
the cystic fibrosis transmembrane conductance regulator (CFTR) gene.";
Genomics 21:434-436(1994).
[73]
VARIANT CF PRO-346.
PubMed=7513296; DOI=10.1007/BF00202817;
Boteva K., Papageorgiou E., Georgiou C., Angastiniotis M.,
Middleton L.T., Constantinou-Deltas C.D.;
"Novel cystic fibrosis mutation associated with mild disease in
Cypriot patients.";
Hum. Genet. 93:529-532(1994).
[74]
VARIANTS CF TYR-199; SER-619; ARG-1005 AND ARG-1291.
PubMed=7525450; DOI=10.1007/BF00211022;
Doerk T., Mekus F., Schmidt K., Bosshammer J., Fislage R., Heuer T.,
Dziadek V., Neumann T., Kaelin N., Wulbrand U., Wulf B.,
von der Hardt H., Maass G., Tuemmler B.;
"Detection of more than 50 different CFTR mutations in a large group
of German cystic fibrosis patients.";
Hum. Genet. 94:533-542(1994).
[75]
VARIANT CF GLU-1249.
PubMed=7520022; DOI=10.1159/000154223;
Greil I., Wagner K., Rosenkranz W.;
"A new missense mutation G1249E in exon 20 of the cystic fibrosis
transmembrane conductance regulator (CFTR) gene.";
Hum. Hered. 44:238-240(1994).
[76]
VARIANT CF GLU-1397.
PubMed=7524913; DOI=10.1093/hmg/3.6.999;
Petreska L., Koceva S., Gordova-Muratovska A., Nestorov R.,
Efremov G.D.;
"Identification of two new mutations (711 +3A-->G and V1397E) in CF
chromosomes of Albanian and Macedonian origin.";
Hum. Mol. Genet. 3:999-1000(1994).
[77]
VARIANT CF CYS-109.
PubMed=7524909; DOI=10.1093/hmg/3.6.1001;
Schaedel C., Kristoffersson A.-C., Kornfaelt R., Holmberg L.;
"A novel cystic fibrosis mutation, Y109C, in the first transmembrane
domain of CFTR.";
Hum. Mol. Genet. 3:1001-1002(1994).
[78]
VARIANT CF THR-120.
PubMed=7517264; DOI=10.1002/humu.1380030308;
Chillon M., Casals T., Gimenez J., Nunes V., Estivill X.;
"Analysis of the CFTR gene in the Spanish population: SSCP-screening
for 60 known mutations and identification of four new mutations (Q30X,
A120T, 1812-1 G-->A, and 3667del4).";
Hum. Mutat. 3:223-230(1994).
[79]
VARIANT CF LEU-87.
PubMed=8081395; DOI=10.1002/humu.1380030412;
Bienvenu T., Petitpretz P., Beldjord C., Kaplan J.C.;
"A missense mutation (F87L) in exon 3 of the cystic fibrosis
transmembrane conductance regulator gene.";
Hum. Mutat. 3:395-396(1994).
[80]
VARIANTS CBAVD ARG-149; LYS-193; GLY-258 AND GLY-800.
PubMed=7529962;
Mercier B., Verlingue C., Lissens W., Silber S.J., Novelli G.,
Bonduelle M., Audrezet M.-P., Ferec C.;
"Is congenital bilateral absence of vas deferens a primary form of
cystic fibrosis? Analyses of the CFTR gene in 67 patients.";
Am. J. Hum. Genet. 56:272-277(1995).
[81]
VARIANTS CBAVD.
PubMed=7539342;
Jezequel P., Dorval I., Fergelot P., Chauvel B., Le Treut A.,
Le Gall J.-Y., Le Lannou D., Blayau M.;
"Structural analysis of CFTR gene in congenital bilateral absence of
vas deferens.";
Clin. Chem. 41:833-835(1995).
[82]
VARIANT CF SER-551.
PubMed=7606851;
Orozco L., Lezana J.L., Villarreal M.T., Chavez M., Carnevale A.;
"Mild cystic fibrosis disease in three Mexican delta-F508/G551S
compound heterozygous siblings.";
Clin. Genet. 47:96-98(1995).
[83]
VARIANTS CF GLY-57; LYS-193 AND GLY-579.
PubMed=7544319; DOI=10.1007/BF00210414;
Brancolini V., Cremonesi L., Belloni E., Pappalardo E., Bordoni R.,
Seia M., Russo S., Padoan R., Giunta A., Ferrari M.;
"Search for mutations in pancreatic sufficient cystic fibrosis Italian
patients: detection of 90% of molecular defects and identification of
three novel mutations.";
Hum. Genet. 96:312-318(1995).
[84]
VARIANT CF TRP-206.
PubMed=8522333; DOI=10.1007/BF00210305;
Desgeorges M., Rodier M., Piot M., Demaille J., Claustres M.;
"Four adult patients with the missense mutation L206W and a mild
cystic fibrosis phenotype.";
Hum. Genet. 96:717-720(1995).
[85]
VARIANTS CF LEU-31 AND ARG-1098.
PubMed=7537150; DOI=10.1002/humu.1380050106;
Zielenski J., Markiewicz D., Chen H.S., Schappert K.T., Seller A.,
Durie P., Corey M., Tsui L.-C.;
"Identification of six mutations (R31L, 441delA, 681delC, 1461ins4,
W1089R, E1104X) in the cystic fibrosis transmembrane conductance
regulator (CFTR) gene.";
Hum. Mutat. 5:43-47(1995).
[86]
VARIANT CF ASN-572.
PubMed=7541273; DOI=10.1002/humu.1380050304;
Verlingue C., Kapranov N.I., Mercier B., Ginter E.K., Petrova N.V.,
Audrezet M.P., Ferec C.;
"Complete screening of mutations in the coding sequence of the CFTR
gene in a sample of CF patients from Russia: identification of three
novel alleles.";
Hum. Mutat. 5:205-209(1995).
[87]
VARIANT CF ARG-98.
PubMed=7581407; DOI=10.1002/humu.1380060216;
Romey M.-C., Desgeorges M., Ray P., Godard P., Demaille J.,
Claustres M.;
"Novel missense mutation in the first transmembrane segment of the
CFTR gene (Q98R) identified in a male adult.";
Hum. Mutat. 6:190-191(1995).
[88]
VARIANT CF ILE-338.
PubMed=7543567; DOI=10.1016/S0022-3476(95)70310-1;
Leoni G.B., Pitzalis S., Podda R., Zanda M., Silvetti M., Caocci L.,
Cao A., Rosatelli M.C.;
"A specific cystic fibrosis mutation (T338I) associated with the
phenotype of isolated hypotonic dehydration.";
J. Pediatr. 127:281-283(1995).
[89]
VARIANTS CF PHE-42; LEU-117; ARG-139 AND GLU-1006.
PubMed=7541510; DOI=10.1016/S0890-8508(95)80038-7;
Ferec C., Novelli G., Verlingue C., Quere I., Dallapiccola B.,
Audrezet M.P., Mercier B.;
"Identification of six novel CFTR mutations in a sample of Italian
cystic fibrosis patients.";
Mol. Cell. Probes 9:135-137(1995).
[90]
VARIANT CF SER-665.
PubMed=8800923;
Messaoud T., Verlingue C., Denamur E., Pascaud O., Quere I.,
Fattoum S., Elion J., Ferec C.;
"Distribution of CFTR mutations in cystic fibrosis patients of
Tunisian origin: identification of two novel mutations.";
Eur. J. Hum. Genet. 4:20-24(1996).
[91]
VARIANT CF ARG-314.
PubMed=8829633;
DOI=10.1002/(SICI)1098-1004(1996)7:2<151::AID-HUMU10>3.0.CO;2-1;
Nasr S.Z., Strong T.V., Mansoura M.K., Dawson D.C., Collins F.S.;
"Novel missense mutation (G314R) in a cystic fibrosis patient with
hepatic failure.";
Hum. Mutat. 7:151-154(1996).
[92]
VARIANT CF CYS-569.
PubMed=8723693;
DOI=10.1002/(SICI)1098-1004(1996)7:4<375::AID-HUMU17>3.3.CO;2-K;
Petreska L., Plaseska D., Koseva S., Stavljenic-Rukavina A.,
Efremov G.D.;
"A novel mutation in exon 12 (Y569C) of the CFTR gene identified in a
patient of Croatian origin.";
Hum. Mutat. 7:374-375(1996).
[93]
VARIANT CF ARG-1061.
PubMed=8723695;
DOI=10.1002/(SICI)1098-1004(1996)7:4<376::AID-HUMU18>3.3.CO;2-E;
Bienvenu T., Chertkoff L., Beldjord C., Segal E., Carniglia L.,
Barreiro C., Kaplan J.-C.;
"Identification of three novel mutations in the cystic fibrosis
transmembrane conductance regulator gene in Argentinian CF patients.";
Hum. Mutat. 7:376-377(1996).
[94]
VARIANT CF LEU-562.
PubMed=8956039;
DOI=10.1002/(SICI)1098-1004(1996)8:4<340::AID-HUMU7>3.3.CO;2-K;
Hughes D.J., Hill A.J.M., Macek M. Jr., Redmond A.O., Nevin N.C.,
Graham C.A.;
"Mutation characterization of CFTR gene in 206 Northern Irish CF
families: thirty mutations, including two novel, account for
approximately 94% of CF chromosomes.";
Hum. Mutat. 8:340-347(1996).
[95]
CHARACTERIZATION OF VARIANT CF ASP-551, CATALYTIC ACTIVITY, FUNCTION,
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=8910473; DOI=10.1074/jbc.271.45.28463;
Li C., Ramjeesingh M., Wang W., Garami E., Hewryk M., Lee D.,
Rommens J.M., Galley K., Bear C.E.;
"ATPase activity of the cystic fibrosis transmembrane conductance
regulator.";
J. Biol. Chem. 271:28463-28468(1996).
[96]
VARIANT CBAVD TYR-50.
PubMed=9067761;
DOI=10.1002/(SICI)1098-1004(1997)9:2<183::AID-HUMU13>3.0.CO;2-Z;
Zielenski J., Patrizio P., Markiewicz D., Asch R.H., Tsui L.-C.;
"Identification of two mutations (S50Y and 4173delC) in the CFTR gene
from patients with congenital bilateral absence of vas deferens
(CBAVD).";
Hum. Mutat. 9:183-184(1997).
[97]
VARIANT CF MET-1140 DEL.
PubMed=9101301;
DOI=10.1002/(SICI)1098-1004(1997)9:4<368::AID-HUMU13>3.3.CO;2-F;
Clavel C., Pennaforte F., Pigeon F., Verlingue C., Birembaut P.,
Ferec C.;
"Identification of four novel mutations in the cystic fibrosis
transmembrane conductance regulator gene: E664X, 2113delA, 306delTAGA,
and delta M1140.";
Hum. Mutat. 9:368-369(1997).
[98]
VARIANT CF ASP-141.
PubMed=9222768;
DOI=10.1002/(SICI)1098-1004(1997)10:1<86::AID-HUMU15>3.0.CO;2-W;
Gouya L., Pascaud O., Munck A., Elion J., Denamur E.;
"Novel mutation (A141D) in exon 4 of the CFTR gene identified in an
Algerian patient.";
Hum. Mutat. 10:86-87(1997).
[99]
VARIANT CF CYS-1066.
PubMed=9375855;
DOI=10.1002/(SICI)1098-1004(1997)10:5<387::AID-HUMU9>3.3.CO;2-V;
Casals T., Pacheco P., Barreto C., Gimenez J., Ramos M.D., Pereira S.,
Pinheiro J.A., Cobos N., Curvelo A., Vazquez C., Rocha H.,
Seculi J.L., Perez E., Dapena J., Carrilho E., Duarte A.,
Palacio A.M., Nunes V., Lavinha J., Estivill X.;
"Missense mutation R1066C in the second transmembrane domain of CFTR
causes a severe cystic fibrosis phenotype: study of 19 heterozygous
and 2 homozygous patients.";
Hum. Mutat. 10:387-392(1997).
[100]
VARIANTS CF GLU-85; HIS-117; TYR-287; GLU-455; ASP-551; PRO-1070 AND
LYS-1303.
PubMed=9401006;
DOI=10.1002/(SICI)1098-1004(1997)10:6<436::AID-HUMU4>3.0.CO;2-B;
Shrimpton A.E., Borowitz D., Swender P.;
"Cystic fibrosis mutation frequencies in upstate New York.";
Hum. Mutat. 10:436-442(1997).
[101]
VARIANT CF PHE-311 DEL.
PubMed=9443874; DOI=10.1086/301681;
Friedman K.J., Leigh M.W., Czarnecki P., Feldman G.L.;
"Cystic fibrosis transmembrane-conductance regulator mutations among
African Americans.";
Am. J. Hum. Genet. 62:195-196(1998).
[102]
CHARACTERIZATION OF VARIANTS CF VAL-1137; MET-1140 DEL AND HIS-1152,
MUTAGENESIS OF MET-1137; ILE-1139 AND ASP-1154, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=9804160; DOI=10.1016/S0014-5793(98)01042-4;
Vankeerberghen A., Wei L., Teng H., Jaspers M., Cassiman J.J.,
Nilius B., Cuppens H.;
"Characterization of mutations located in exon 18 of the CFTR gene.";
FEBS Lett. 437:1-4(1998).
[103]
VARIANTS CF LEU-1013 AND ILE-1028.
PubMed=9521595; DOI=10.1007/s004390050683;
Onay T., Topaloglu O., Zielenski J., Gokgoz N., Kayserili H.,
Camcioglu Y., Cokugras H., Akcakaya N., Apak M., Tsui L.-C.,
Kirdar B.;
"Analysis of the CFTR gene in Turkish cystic fibrosis patients:
identification of three novel mutations (3172delAC, P1013L and
M1028I).";
Hum. Genet. 102:224-230(1998).
[104]
VARIANTS CF, AND VARIANTS CYS-31; GLN-75; VAL-506 AND CYS-668.
PubMed=9921909; DOI=10.1007/s004390050897;
Bombieri C., Benetazzo M., Saccomani A., Belpinati F., Gile L.S.,
Luisetti M., Pignatti P.F.;
"Complete mutational screening of the CFTR gene in 120 patients with
pulmonary disease.";
Hum. Genet. 103:718-722(1998).
[105]
CHARACTERIZATION OF VARIANTS CF PHE-601; SER-610; THR-613; GLY-614;
THR-618; SER-619; GLN-620; PRO-620; ARG-628; PRO-633 AND SER-665,
CHARACTERIZATION OF VARIANT OLIGOSPERMIA ASP-622, CHARACTERIZATION OF
VARIANTS CBAVD GLY-792 AND GLY-800, AND CHARACTERIZATION OF VARIANT
THORACIC SARCOIDOSIS LYS-828.
PubMed=9736778; DOI=10.1093/hmg/7.11.1761;
Vankeerberghen A., Wei L., Jaspers M., Cassiman J.-J., Nilius B.,
Cuppens H.;
"Characterization of 19 disease-associated missense mutations in the
regulatory domain of the cystic fibrosis transmembrane conductance
regulator.";
Hum. Mol. Genet. 7:1761-1769(1998).
[106]
VARIANTS CF SER-560 AND ASP-569.
PubMed=9482579;
DOI=10.1002/(SICI)1098-1004(1998)11:2<152::AID-HUMU8>3.0.CO;2-L;
Malone G., Haworth A., Schwarz M.J., Cuppens H., Super M.;
"Detection of five novel mutations of the cystic fibrosis
transmembrane regulator (CFTR) gene in Pakistani patients with cystic
fibrosis: Y569D, Q98X, 296+12(T>C), 1161delC and 621+2(T>C).";
Hum. Mutat. 11:152-157(1998).
[107]
VARIANTS CF PHE-13 AND ILE-338.
PubMed=9554753;
Leoni G.B., Pitzalis S., Tonelli R., Cao A.;
"Identification of a novel mutation (S13F) in the CFTR gene in a CF
patient of Sardinian origin.";
Hum. Mutat. 11:337-337(1998).
[108]
VARIANTS CF PRO-117 AND ASP-192 DEL.
PubMed=9452048;
Feldmann D., Sardet A., Cougoureux E., Plouvier E., Fontaine J.-L.,
Tournier G., Aymard P.;
"Identification of three novel mutations in the CFTR gene, R117P,
deltaD192, and 3121+1G-->A in four French patients.";
Hum. Mutat. Suppl. 1:S78-S80(1998).
[109]
VARIANT CF ARG-1065.
PubMed=9452054;
Casals T., Ramos M.D., Gimenez J., Nadal M., Nunes V., Estivill X.;
"Paternal origin of a de novo novel CFTR mutation (L1065R) causing
cystic fibrosis.";
Hum. Mutat. Suppl. 1:S99-S102(1998).
[110]
VARIANT CF ASN-LYS-370 INS.
PubMed=9452073;
Shackleton S., Harris A.;
"A 2-amino acid insertion mutation (1243insACAAAA) in exon 7 of the
CFTR gene.";
Hum. Mutat. Suppl. 1:S156-S157(1998).
[111]
VARIANT CBAVD GLY-513, AND VARIANT MET-470.
PubMed=10651488;
Bienvenu T., Bousquet S., Vidaud D., Hubert D., Francoual C.,
Beldjord C., Kaplan J.-C.;
"A novel missense mutation D513G in exon 10 of the cystic fibrosis
transmembrane conductance regulator (CFTR) gene identified in a French
CBAVD patient.";
Hum. Mutat. 12:213-214(1998).
[112]
VARIANTS CBAVD LEU-111; LYS-244; VAL-544 AND VAL-1364.
de Meeus A., Guittard C., Desgeorges M., Carles S., Demaille J.,
Claustres M.;
"Genetic findings in congenital bilateral aplasia of vas deferens
patients and identification of six novel mutations.";
Hum. Mutat. 12:480-480(1998).
[113]
VARIANT CF GLY-579.
PubMed=10094564;
DOI=10.1002/(SICI)1098-1004(1999)13:2<173::AID-HUMU20>3.0.CO;2-3;
Picci L., Cameran M., Olante P., Zacchello F., Scarpa M.;
"Identification of a D579G homozygote cystic fibrosis patient with
pancreatic sufficiency and minor lung involvement.";
Hum. Mutat. 13:173-173(1999).
[114]
VARIANT CF LEU-693.
PubMed=12167682; DOI=10.1056/NEJMoa011899;
Groman J.D., Meyer M.E., Wilmott R.W., Zeitlin P.L., Cutting G.R.;
"Variant cystic fibrosis phenotypes in the absence of CFTR
mutations.";
N. Engl. J. Med. 347:401-407(2002).
[115]
CHARACTERIZATION OF VARIANT CF TYR-287 AND PHE-508 DEL, SUBCELLULAR
LOCATION, FUNCTION, AND GLYCOSYLATION.
PubMed=12529365; DOI=10.1074/jbc.M212843200;
Silvis M.R., Picciano J.A., Bertrand C., Weixel K., Bridges R.J.,
Bradbury N.A.;
"A mutation in the cystic fibrosis transmembrane conductance regulator
generates a novel internalization sequence and enhances endocytic
rates.";
J. Biol. Chem. 278:11554-11560(2003).
[116]
CHARACTERIZATION OF VARIANT CF PHE-508 DEL, SUBCELLULAR LOCATION,
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15716351; DOI=10.1091/mbc.E04-11-1010;
Kreda S.M., Mall M., Mengos A., Rochelle L., Yankaskas J.,
Riordan J.R., Boucher R.C.;
"Characterization of wild-type and deltaF508 cystic fibrosis
transmembrane regulator in human respiratory epithelia.";
Mol. Biol. Cell 16:2154-2167(2005).
[117]
CHARACTERIZATION OF CF VARIANT LYS-1303, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=17182731; DOI=10.1152/ajpcell.00064.2006;
Suaud L., Yan W., Carattino M.D., Robay A., Kleyman T.R.,
Rubenstein R.C.;
"Regulatory interactions of N1303K-CFTR and ENaC in Xenopus oocytes:
evidence that chloride transport is not necessary for inhibition of
ENaC.";
Am. J. Physiol. 292:C1553-C1561(2007).
[118]
VARIANT [LARGE SCALE ANALYSIS] MET-470.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[119]
CHARACTERIZATION OF VARIANT CF HIS-117, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=26846474; DOI=10.1113/JP271723;
Yu Y.C., Sohma Y., Hwang T.C.;
"On the mechanism of gating defects caused by the R117H mutation in
cystic fibrosis transmembrane conductance regulator.";
J. Physiol. (Lond.) 594:3227-3244(2016).
[120]
CHARACTERIZATION OF VARIANT CF PHE-508 DEL, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ILE-539.
PubMed=28001373; DOI=10.1021/acs.biochem.6b00853;
Zhang Z., Baksh M.M., Finn M.G., Heidary D.K., Richards C.I.;
"Direct measurement of trafficking of the cystic fibrosis
transmembrane conductance regulator to the cell surface and binding to
a chemical chaperone.";
Biochemistry 56:240-249(2017).
[121]
CHARACTERIZATION OF VARIANTS CF PHE-508 DEL AND ASP-551, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=28087700; DOI=10.1074/jbc.M116.751537;
Meng X., Wang Y., Wang X., Wrennall J.A., Rimington T.L., Li H.,
Cai Z., Ford R.C., Sheppard D.N.;
"Two small molecules restore stability to a sub-population of the
cystic fibrosis transmembrane conductance regulator with the
predominant disease-causing mutation.";
J. Biol. Chem. 292:3706-3719(2017).
-!- 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:15010471,
PubMed:12588899, PubMed:17036051, PubMed:19398555,
PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:1712898,
PubMed:8910473, PubMed:9804160, PubMed:12529365, PubMed:17182731,
PubMed:26846474, PubMed:28087700). Channel activity is coupled to
ATP hydrolysis (PubMed:8910473). The ion channel is also permeable
to HCO(3-); selectivity depends on the extracellular chloride
concentration (PubMed:15010471, PubMed:19019741). Exerts its
function also by modulating the activity of other ion channels and
transporters (PubMed:12403779, PubMed:22178883, PubMed:22121115,
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:17434346, PubMed:27941075,
PubMed:17182731). 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: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). {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:14668433, ECO:0000269|PubMed:15010471,
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:8910473,
ECO:0000269|PubMed:9804160, ECO:0000305|PubMed:19923167}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:15284228,
ECO:0000269|PubMed:26627831, ECO:0000269|PubMed:8910473}.
-!- SUBUNIT: Monomer; does not require oligomerization for channel
activity (PubMed:11524016). May form oligomers in the membrane
(PubMed:11524016). Interacts with SLC26A3, SLC26A6 and SHANK2 (By
similarity). Interacts with SLC9A3R1 and MYO6 (PubMed:12403779,
PubMed:15247260, PubMed:11304524). Interacts (via C-terminus) with
GOPC (via PDZ domain); this promotes CFTR internalization and
thereby decreases channel activity (PubMed:11707463,
PubMed:16331976). Interacts with SLC4A7 through SLC9A3R1
(PubMed:12403779). Found in a complex with MYO5B and RAB11A
(PubMed:17462998). Interacts with ANO1 (PubMed:22178883).
Interacts with SLC26A8 (PubMed:22121115). Interacts with AHCYL1;
the interaction increases CFTR activity (By similarity). Interacts
with CSE1L (PubMed:20933420). {ECO:0000250|UniProtKB:P26361,
ECO:0000250|UniProtKB:P34158, ECO:0000269|PubMed:11304524,
ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:11707463,
ECO:0000269|PubMed:12403779, ECO:0000269|PubMed:15247260,
ECO:0000269|PubMed:16331976, ECO:0000269|PubMed:17462998,
ECO:0000269|PubMed:20933420, ECO:0000269|PubMed:22121115,
ECO:0000269|PubMed:22178883}.
-!- INTERACTION:
P51572:BCAP31; NbExp=3; IntAct=EBI-349854, EBI-77683;
P27824:CANX; NbExp=3; IntAct=EBI-349854, EBI-355947;
Q9BUN8:DERL1; NbExp=2; IntAct=EBI-349854, EBI-398977;
Q9H8Y8:GORASP2; NbExp=3; IntAct=EBI-349854, EBI-739467;
P19120:HSPA8 (xeno); NbExp=2; IntAct=EBI-349854, EBI-907802;
O15554:KCNN4; NbExp=5; IntAct=EBI-349854, EBI-2924473;
P05787:KRT8; NbExp=7; IntAct=EBI-349854, EBI-297852;
Q9HBW0:LPAR2; NbExp=4; IntAct=EBI-349854, EBI-765995;
Q5T2W1:PDZK1; NbExp=2; IntAct=EBI-349854, EBI-349819;
Q99942:RNF5; NbExp=3; IntAct=EBI-349854, EBI-348482;
Q9QX74:Shank2 (xeno); NbExp=2; IntAct=EBI-349854, EBI-397902;
Q96RN1:SLC26A8; NbExp=2; IntAct=EBI-349854, EBI-1792052;
O14745:SLC9A3R1; NbExp=5; IntAct=EBI-349854, EBI-349787;
Q15599:SLC9A3R2; NbExp=7; IntAct=EBI-349854, EBI-1149760;
-!- 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.54}. Early endosome membrane
{ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20008117}; Multi-
pass membrane protein {ECO:0000269|Ref.54}. 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:22178883, ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:28001373,
ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:28130590,
ECO:0000269|PubMed:9804160, ECO:0000305|PubMed:8910473}; Multi-
pass membrane protein {ECO:0000269|Ref.54}. Recycling endosome
membrane {ECO:0000305|PubMed:17462998}; Multi-pass membrane
protein {ECO:0000269|Ref.54}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11707463, ECO:0000269|PubMed:25330774}; Multi-
pass membrane protein {ECO:0000269|Ref.54}. 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).
{ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20008117,
ECO:0000269|PubMed:22207244, ECO:0000305|PubMed:17462998}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P13569-1; Sequence=Displayed;
Name=2;
IsoId=P13569-2; Sequence=VSP_022123;
Note=Exon skipping favored by a high number of TG repeats and a
low number of T repeats at the intron-exon boundary. Causes
congenital bilateral absence of the vas deferens (CBAVD).;
Name=3;
IsoId=P13569-3; Sequence=VSP_022124, VSP_022125;
Note=Alternative acceptor site favored by mutation in an exonic
splicing enhancer (ESE). Causes cystic fibrosis (CF).;
-!- TISSUE SPECIFICITY: Expressed in the respiratory airway, including
bronchial epithelium, and in the female reproductive tract,
including oviduct (at protein level) (PubMed:22207244,
PubMed:15716351). Detected in pancreatic intercalated ducts in the
exocrine tissue, on epithelial cells in intralobular striated
ducts in sublingual salivary glands, on apical membranes of crypt
cells throughout the small and large intestine, and on the
reabsorptive duct in eccrine sweat glands (PubMed:1284548,
PubMed:28130590). Detected on the equatorial segment of the sperm
head (at protein level) (PubMed:19923167). Detected in nasal and
bronchial superficial epithelium (PubMed:15716351). Expressed by
the central cells on the cebaceous glands and, at lower levels, by
epithelial cells (PubMed:28130590). {ECO:0000269|PubMed:1284548,
ECO:0000269|PubMed:15716351, ECO:0000269|PubMed:19923167,
ECO:0000269|PubMed:22207244, ECO:0000269|PubMed:28130590}.
-!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
transporter nucleotide-binding domains (PubMed:15284228). The two
ATP-binding domains interact with each other, forming a head-to-
tail dimer (PubMed:17036051). Normal ATPase activity requires
interaction between the two domains (PubMed:15284228). The first
ABC transporter nucleotide-binding domain has no ATPase activity
by itself (By similarity). {ECO:0000250|UniProtKB:P26361,
ECO:0000269|PubMed:15284228, ECO:0000269|PubMed:17036051}.
-!- DOMAIN: The PDZ-binding motif mediates interactions with GOPC and
with the SLC4A7, SLC9A3R1/EBP50 complex.
{ECO:0000269|PubMed:11304524, ECO:0000269|PubMed:11707463,
ECO:0000269|PubMed:16331976}.
-!- DOMAIN: The R region is intrinsically disordered (PubMed:10792060,
PubMed:17660831). It mediates channel activation when it is
phosphorylated, but not in the absence of phosphorylation
(PubMed:10792060). {ECO:0000269|PubMed:10792060,
ECO:0000269|PubMed:17660831}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12529365,
ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:20008117}.
-!- 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). Deubiquitination by USP10 in early endosomes
enhances its endocytic recycling to the cell membrane
(PubMed:19398555). Ubiquitinated by RNF185 during ER stress
(PubMed:24019521). {ECO:0000269|PubMed:19398555,
ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:24019521}.
-!- 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:12167682, 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:15528182,
ECO:0000269|PubMed:15716351, ECO:0000269|PubMed:1695717,
ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:1710600,
ECO:0000269|PubMed:1712898, ECO:0000269|PubMed:17182731,
ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:20150177,
ECO:0000269|PubMed:2236053, ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:26846474, ECO:0000269|PubMed:28001373,
ECO:0000269|PubMed:28087700, ECO:0000269|PubMed:7504969,
ECO:0000269|PubMed:7505694, 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:9521595, ECO:0000269|PubMed:9554753,
ECO:0000269|PubMed:9736778, ECO:0000269|PubMed:9804160,
ECO:0000269|PubMed:9921909}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Congenital bilateral absence of the vas deferens (CBAVD)
[MIM:277180]: Important cause of sterility in men and could
represent an incomplete form of cystic fibrosis, as the majority
of men suffering from cystic fibrosis lack the vas deferens.
{ECO:0000269|PubMed:10651488, ECO:0000269|PubMed:7529962,
ECO:0000269|PubMed:7539342, ECO:0000269|PubMed:9067761,
ECO:0000269|PubMed:9736778, ECO:0000269|Ref.112}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=CFTR; Note=Cystic fibrosis mutation db;
URL="http://www.genet.sickkids.on.ca/app";
-!- WEB RESOURCE: Name=Wikipedia; Note=CFTR entry;
URL="https://en.wikipedia.org/wiki/Cystic_fibrosis_transmembrane_conductance_regulator";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P13569";
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EMBL; M28668; AAA35680.1; -; mRNA.
EMBL; M55131; AAC13657.1; -; Genomic_DNA.
EMBL; M55106; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55107; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55108; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55110; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55111; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55112; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55113; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55114; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55115; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55116; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55117; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55118; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55119; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55120; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55121; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55122; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55123; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55124; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55125; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55126; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55127; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55128; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55129; AAC13657.1; JOINED; Genomic_DNA.
EMBL; M55130; AAC13657.1; JOINED; Genomic_DNA.
EMBL; DQ354388; ABC79050.1; -; Genomic_DNA.
EMBL; DQ354389; ABC79052.1; -; Genomic_DNA.
EMBL; DQ354390; ABC79054.1; -; Genomic_DNA.
EMBL; DQ354391; ABC79056.1; -; Genomic_DNA.
EMBL; DQ356258; ABC87055.1; -; Genomic_DNA.
EMBL; DQ356259; ABC87057.1; -; Genomic_DNA.
EMBL; DQ356261; ABC87061.1; -; Genomic_DNA.
EMBL; DQ356262; ABC87063.1; -; Genomic_DNA.
EMBL; DQ356263; ABC87065.1; -; Genomic_DNA.
EMBL; DQ356264; ABC87067.1; -; Genomic_DNA.
EMBL; DQ388128; ABD72183.1; -; Genomic_DNA.
EMBL; DQ388129; ABD72185.1; -; Genomic_DNA.
EMBL; DQ388131; ABD72189.1; -; Genomic_DNA.
EMBL; DQ388132; ABD72191.1; -; Genomic_DNA.
EMBL; DQ388133; ABD72193.1; -; Genomic_DNA.
EMBL; DQ388134; ABD72195.1; -; Genomic_DNA.
EMBL; DQ388135; ABD72197.1; -; Genomic_DNA.
EMBL; DQ388138; ABD72203.1; -; Genomic_DNA.
EMBL; DQ388139; ABD72205.1; -; Genomic_DNA.
EMBL; DQ388140; ABD72207.1; -; Genomic_DNA.
EMBL; DQ388141; ABD72209.1; -; Genomic_DNA.
EMBL; DQ388142; ABD72211.1; -; Genomic_DNA.
EMBL; DQ388143; ABD72213.1; -; Genomic_DNA.
EMBL; DQ388145; ABD72217.1; -; Genomic_DNA.
EMBL; AC000061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC000111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236947; EAL24353.1; -; Genomic_DNA.
EMBL; M65196; AAA51979.1; -; Genomic_DNA.
EMBL; M65197; AAA51980.1; -; Genomic_DNA.
CCDS; CCDS5773.1; -. [P13569-1]
PIR; A39069; DVHUCF.
RefSeq; NP_000483.3; NM_000492.3. [P13569-1]
UniGene; Hs.489786; -.
UniGene; Hs.621460; -.
UniGene; Hs.661104; -.
PDB; 1NBD; Model; -; A=425-638.
PDB; 1XMI; X-ray; 2.25 A; A/B/C/D/E=389-678.
PDB; 1XMJ; X-ray; 2.30 A; A=389-677.
PDB; 2BBO; X-ray; 2.55 A; A=389-678.
PDB; 2BBS; X-ray; 2.05 A; A/B=389-677.
PDB; 2BBT; X-ray; 2.30 A; A/B=389-678.
PDB; 2LOB; NMR; -; B=1473-1480.
PDB; 2PZE; X-ray; 1.70 A; A/B=387-646.
PDB; 2PZF; X-ray; 2.00 A; A/B=387-646.
PDB; 2PZG; X-ray; 1.80 A; A/B=375-646.
PDB; 3GD7; X-ray; 2.70 A; A/B/C/D=1193-1427.
PDB; 3ISW; X-ray; 2.80 A; C=5-20.
PDB; 4WZ6; X-ray; 2.05 A; A=389-678.
PDB; 5D2D; X-ray; 2.10 A; C=747-774.
PDB; 5D3E; X-ray; 2.75 A; C/G/K=762-801.
PDB; 5D3F; X-ray; 2.74 A; C=747-774.
PDB; 5UAK; EM; 3.87 A; A=1-1480.
PDBsum; 1NBD; -.
PDBsum; 1XMI; -.
PDBsum; 1XMJ; -.
PDBsum; 2BBO; -.
PDBsum; 2BBS; -.
PDBsum; 2BBT; -.
PDBsum; 2LOB; -.
PDBsum; 2PZE; -.
PDBsum; 2PZF; -.
PDBsum; 2PZG; -.
PDBsum; 3GD7; -.
PDBsum; 3ISW; -.
PDBsum; 4WZ6; -.
PDBsum; 5D2D; -.
PDBsum; 5D3E; -.
PDBsum; 5D3F; -.
PDBsum; 5UAK; -.
DisProt; DP00012; -.
ProteinModelPortal; P13569; -.
SMR; P13569; -.
BioGrid; 107506; 275.
DIP; DIP-32788N; -.
IntAct; P13569; 140.
MINT; MINT-148539; -.
STRING; 9606.ENSP00000003084; -.
BindingDB; P13569; -.
ChEMBL; CHEMBL4051; -.
DrugBank; DB00887; Bumetanide.
DrugBank; DB04941; Crofelemer.
DrugBank; DB01016; Glyburide.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB08820; Ivacaftor.
DrugBank; DB09280; Lumacaftor.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB04522; Phosphonoserine.
GuidetoPHARMACOLOGY; 707; -.
MoonProt; P13569; -.
TCDB; 3.A.1.202.1; the atp-binding cassette (abc) superfamily.
iPTMnet; P13569; -.
PhosphoSitePlus; P13569; -.
SwissPalm; P13569; -.
BioMuta; CFTR; -.
DMDM; 147744553; -.
PaxDb; P13569; -.
PeptideAtlas; P13569; -.
PRIDE; P13569; -.
DNASU; 1080; -.
Ensembl; ENST00000003084; ENSP00000003084; ENSG00000001626. [P13569-1]
GeneID; 1080; -.
KEGG; hsa:1080; -.
UCSC; uc003vjd.4; human. [P13569-1]
CTD; 1080; -.
DisGeNET; 1080; -.
GeneCards; CFTR; -.
GeneReviews; CFTR; -.
HGNC; HGNC:1884; CFTR.
HPA; CAB001951; -.
HPA; HPA021939; -.
MalaCards; CFTR; -.
MIM; 219700; phenotype.
MIM; 277180; phenotype.
MIM; 602421; gene.
neXtProt; NX_P13569; -.
OpenTargets; ENSG00000001626; -.
Orphanet; 48; Congenital bilateral absence of vas deferens.
Orphanet; 586; Cystic fibrosis.
Orphanet; 676; Hereditary chronic pancreatitis.
Orphanet; 60033; Idiopathic bronchiectasis.
Orphanet; 399805; Male infertility with azoospermia or oligozoospermia due to single gene mutation.
PharmGKB; PA109; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00890000139450; -.
HOVERGEN; HBG004169; -.
InParanoid; P13569; -.
KO; K05031; -.
OMA; LAHFVWI; -.
OrthoDB; EOG091G00K4; -.
PhylomeDB; P13569; -.
TreeFam; TF105200; -.
BioCyc; MetaCyc:HS00075-MONOMER; -.
BRENDA; 3.6.3.49; 2681.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5627083; RHO GTPases regulate CFTR trafficking.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SIGNOR; P13569; -.
EvolutionaryTrace; P13569; -.
GenomeRNAi; 1080; -.
PRO; PR:P13569; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000001626; -.
CleanEx; HS_CFTR; -.
ExpressionAtlas; P13569; baseline and differential.
Genevisible; P13569; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0043225; F:ATPase-coupled anion transmembrane transporter activity; TAS:Reactome.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB.
GO; GO:0017081; F:chloride channel regulator activity; TAS:Reactome.
GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005260; F:intracellular ATPase-gated chloride channel activity; IMP:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IDA:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; IDA:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IDA:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
GO; GO:0051454; P:intracellular pH elevation; ISS:UniProtKB.
GO; GO:0060081; P:membrane hyperpolarization; ISS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:UniProtKB.
GO; GO:1902161; P:positive regulation of cyclic nucleotide-gated ion channel activity; IMP:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
GO; GO:0035377; P:transepithelial water transport; IMP:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:Ensembl.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR009147; CFTR/ABCC7.
InterPro; IPR025837; CFTR_reg_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24223:SF273; PTHR24223:SF273; 1.
Pfam; PF00664; ABC_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
Pfam; PF14396; CFTR_R; 1.
PRINTS; PR01851; CYSFIBREGLTR.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF90123; SSF90123; 2.
TIGRFAMs; TIGR01271; CFTR_protein; 1.
PROSITE; PS50929; ABC_TM1F; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Chloride; Chloride channel; Complete proteome; Disease mutation;
Endoplasmic reticulum; Endosome; Glycoprotein; Hydrolase; Ion channel;
Ion transport; Isopeptide bond; Lipoprotein; Membrane;
Nucleotide-binding; Palmitate; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 1480 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000093419.
TOPO_DOM 1 77 Cytoplasmic. {ECO:0000305}.
TRANSMEM 78 98 Helical; Name=1. {ECO:0000269|Ref.54}.
TOPO_DOM 99 122 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 123 146 Helical; Name=2. {ECO:0000269|Ref.54}.
TOPO_DOM 147 195 Cytoplasmic. {ECO:0000269|Ref.54}.
TRANSMEM 196 216 Helical; Name=3. {ECO:0000269|Ref.54}.
TOPO_DOM 217 222 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 223 243 Helical; Name=4. {ECO:0000269|Ref.54}.
TOPO_DOM 244 298 Cytoplasmic. {ECO:0000269|Ref.54}.
TRANSMEM 299 319 Helical; Name=5. {ECO:0000269|Ref.54}.
TOPO_DOM 320 339 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 340 358 Helical; Name=6. {ECO:0000269|Ref.54}.
TOPO_DOM 359 858 Cytoplasmic. {ECO:0000269|Ref.54}.
TRANSMEM 859 879 Helical; Name=7. {ECO:0000269|Ref.54}.
TOPO_DOM 880 918 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 919 939 Discontinuously helical; Name=8.
{ECO:0000269|Ref.54}.
TOPO_DOM 940 990 Cytoplasmic. {ECO:0000269|Ref.54}.
TRANSMEM 991 1011 Helical; Name=9. {ECO:0000269|Ref.54}.
TOPO_DOM 1012 1013 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 1014 1034 Helical; Name=10. {ECO:0000269|Ref.54}.
TOPO_DOM 1035 1095 Cytoplasmic. {ECO:0000269|Ref.54}.
TRANSMEM 1096 1116 Helical; Name=11. {ECO:0000269|Ref.54}.
TOPO_DOM 1117 1130 Extracellular. {ECO:0000269|Ref.54}.
TRANSMEM 1131 1151 Helical; Name=12. {ECO:0000269|Ref.54}.
TOPO_DOM 1152 1480 Cytoplasmic. {ECO:0000269|Ref.54}.
DOMAIN 81 365 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 423 646 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 859 1155 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1210 1443 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 458 465 ATP 1. {ECO:0000244|PDB:1XMI,
ECO:0000244|PDB:1XMJ,
ECO:0000244|PDB:2BBO,
ECO:0000244|PDB:2BBS,
ECO:0000244|PDB:2BBT,
ECO:0000255|PROSITE-ProRule:PRU00434,
ECO:0000269|PubMed:15528182}.
NP_BIND 1244 1251 ATP 2. {ECO:0000244|PDB:3GD7,
ECO:0000255|PROSITE-ProRule:PRU00434}.
REGION 654 831 Intrinsically disordered R region.
{ECO:0000269|PubMed:10792060}.
MOTIF 1478 1480 PDZ-binding.
{ECO:0000269|PubMed:11707463,
ECO:0000269|PubMed:16331976}.
BINDING 401 401 ATP 1. {ECO:0000244|PDB:1XMI,
ECO:0000244|PDB:1XMJ,
ECO:0000244|PDB:2BBO,
ECO:0000244|PDB:2BBS,
ECO:0000244|PDB:2BBT,
ECO:0000244|PDB:2PZE,
ECO:0000244|PDB:2PZF,
ECO:0000244|PDB:2PZG,
ECO:0000269|PubMed:15528182,
ECO:0000269|PubMed:20150177}.
BINDING 434 434 ATP 1. {ECO:0000244|PDB:2PZE,
ECO:0000244|PDB:2PZF,
ECO:0000244|PDB:2PZG,
ECO:0000269|PubMed:20150177}.
BINDING 493 493 ATP 1. {ECO:0000244|PDB:1XMI,
ECO:0000244|PDB:2BBO,
ECO:0000244|PDB:2BBS,
ECO:0000269|PubMed:15528182}.
BINDING 1219 1219 ATP 2. {ECO:0000244|PDB:3GD7}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 660 660 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:22119790,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 670 670 Phosphoserine; by PKA.
{ECO:0000269|PubMed:25330774}.
MOD_RES 686 686 Phosphoserine; by PKC.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:22119790}.
MOD_RES 700 700 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:22119790,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 712 712 Phosphoserine; by PKA.
{ECO:0000269|PubMed:22119790,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 717 717 Phosphothreonine.
{ECO:0000269|PubMed:22119790}.
MOD_RES 737 737 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:22119790,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 753 753 Phosphoserine; by PKA.
{ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 768 768 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 790 790 Phosphoserine; by PKC.
{ECO:0000269|PubMed:1377674}.
MOD_RES 795 795 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:22119790,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 813 813 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1377674,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:9385646}.
MOD_RES 1444 1444 Phosphoserine.
{ECO:0000269|PubMed:22119790}.
MOD_RES 1456 1456 Phosphoserine.
{ECO:0000269|PubMed:22119790}.
LIPID 524 524 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22119790}.
LIPID 1395 1395 S-palmitoyl cysteine.
{ECO:0000269|PubMed:22119790}.
CARBOHYD 894 894 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7518437,
ECO:0000305|PubMed:20008117}.
CARBOHYD 900 900 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:7518437,
ECO:0000305|PubMed:20008117}.
CROSSLNK 688 688 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:22119790}.
VAR_SEQ 404 464 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_022123.
VAR_SEQ 589 605 SCVCKLMANKTRILVTS -> RRRCSCLLDRNKKTIF (in
isoform 3). {ECO:0000305}.
/FTId=VSP_022124.
VAR_SEQ 606 1480 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_022125.
VARIANT 13 13 S -> F (in CF; dbSNP:rs397508635).
{ECO:0000269|PubMed:9554753}.
/FTId=VAR_000101.
VARIANT 31 31 R -> C (in dbSNP:rs1800073).
{ECO:0000269|PubMed:7522211,
ECO:0000269|PubMed:9921909}.
/FTId=VAR_000102.
VARIANT 31 31 R -> L (in CF; dbSNP:rs149353983).
{ECO:0000269|PubMed:7537150}.
/FTId=VAR_000103.
VARIANT 42 42 S -> F (in CF; dbSNP:rs143456784).
{ECO:0000269|PubMed:7541510}.
/FTId=VAR_000104.
VARIANT 44 44 D -> G (in CF; dbSNP:rs1800074).
/FTId=VAR_000105.
VARIANT 44 44 D -> V (in dbSNP:rs1800074).
/FTId=VAR_000106.
VARIANT 50 50 S -> Y (in CBAVD; dbSNP:rs397508220).
{ECO:0000269|PubMed:9067761}.
/FTId=VAR_000107.
VARIANT 57 57 W -> G (in CF; dbSNP:rs397508272).
{ECO:0000269|PubMed:7544319}.
/FTId=VAR_000108.
VARIANT 67 67 P -> L (in CF; dbSNP:rs368505753).
/FTId=VAR_000109.
VARIANT 74 74 R -> W (in CF; dbSNP:rs115545701).
/FTId=VAR_000110.
VARIANT 75 75 R -> Q (in dbSNP:rs1800076).
{ECO:0000269|PubMed:9921909}.
/FTId=VAR_000111.
VARIANT 85 85 G -> E (in CF; dbSNP:rs75961395).
{ECO:0000269|PubMed:9401006}.
/FTId=VAR_000112.
VARIANT 87 87 F -> L (in CF; dbSNP:rs397508403).
{ECO:0000269|PubMed:8081395}.
/FTId=VAR_000113.
VARIANT 91 91 G -> R (in CF; dbSNP:rs121908750).
/FTId=VAR_000114.
VARIANT 92 92 E -> K (in CF; dbSNP:rs121908751).
{ECO:0000269|PubMed:1284529,
ECO:0000269|PubMed:7683954}.
/FTId=VAR_000115.
VARIANT 98 98 Q -> R (in CF; dbSNP:rs397508464).
{ECO:0000269|PubMed:7581407}.
/FTId=VAR_000116.
VARIANT 105 105 I -> S (in CF).
/FTId=VAR_000117.
VARIANT 109 109 Y -> C (in CF; dbSNP:rs121909031).
{ECO:0000269|PubMed:7524909}.
/FTId=VAR_000118.
VARIANT 110 110 D -> H (in CF; dbSNP:rs113993958).
/FTId=VAR_000119.
VARIANT 111 111 P -> L (in CBAVD; dbSNP:rs140502196).
{ECO:0000269|Ref.112}.
/FTId=VAR_000120.
VARIANT 117 117 R -> C (in CF; dbSNP:rs77834169).
{ECO:0000269|PubMed:1284529}.
/FTId=VAR_000121.
VARIANT 117 117 R -> H (in CF and CBAVD; decreases single
channel conductance; promotes rapid
return to the closed state of the
channel; dbSNP:rs78655421).
{ECO:0000269|PubMed:26846474,
ECO:0000269|PubMed:9401006}.
/FTId=VAR_000122.
VARIANT 117 117 R -> L (in CF; dbSNP:rs78655421).
{ECO:0000269|PubMed:7541510}.
/FTId=VAR_000123.
VARIANT 117 117 R -> P (in CF; dbSNP:rs78655421).
{ECO:0000269|PubMed:9452048}.
/FTId=VAR_000124.
VARIANT 120 120 A -> T (in CF; dbSNP:rs201958172).
{ECO:0000269|PubMed:7517264}.
/FTId=VAR_000125.
VARIANT 138 138 L -> P (in dbSNP:rs1800078).
/FTId=VAR_009895.
VARIANT 139 139 H -> R (in CF; dbSNP:rs76371115).
{ECO:0000269|PubMed:7541510}.
/FTId=VAR_000126.
VARIANT 141 141 A -> D (in CF; dbSNP:rs397508700).
{ECO:0000269|PubMed:9222768}.
/FTId=VAR_000127.
VARIANT 148 148 I -> T (in CF; dbSNP:rs35516286).
/FTId=VAR_000128.
VARIANT 149 149 G -> R (in CBAVD; dbSNP:rs397508718).
{ECO:0000269|PubMed:7529962}.
/FTId=VAR_000129.
VARIANT 170 170 R -> H (in dbSNP:rs1800079).
/FTId=VAR_009896.
VARIANT 178 178 G -> R (in CF; dbSNP:rs80282562).
/FTId=VAR_000130.
VARIANT 182 182 S -> G (in dbSNP:rs1800080).
/FTId=VAR_009897.
VARIANT 192 192 Missing (in CF).
{ECO:0000269|PubMed:9452048}.
/FTId=VAR_000131.
VARIANT 193 193 E -> K (in CBAVD and CF;
dbSNP:rs397508759).
{ECO:0000269|PubMed:7529962,
ECO:0000269|PubMed:7544319}.
/FTId=VAR_000132.
VARIANT 199 199 H -> Q (in CF; dbSNP:rs397508765).
/FTId=VAR_000133.
VARIANT 199 199 H -> Y (in CF; dbSNP:rs121908802).
{ECO:0000269|PubMed:7525450}.
/FTId=VAR_000134.
VARIANT 205 205 P -> S (in CF; dbSNP:rs121908803).
{ECO:0000269|PubMed:7505694}.
/FTId=VAR_000135.
VARIANT 206 206 L -> W (in CF; dbSNP:rs121908752).
{ECO:0000269|PubMed:8522333}.
/FTId=VAR_000136.
VARIANT 225 225 C -> R (in CF; dbSNP:rs397508780).
/FTId=VAR_000137.
VARIANT 244 244 M -> K (in CBAVD; dbSNP:rs397508790).
{ECO:0000269|Ref.112}.
/FTId=VAR_000138.
VARIANT 258 258 R -> G (in CBAVD; dbSNP:rs191456345).
{ECO:0000269|PubMed:7529962}.
/FTId=VAR_000139.
VARIANT 287 287 N -> Y (in CF; decreased presence at the
cell membrane due to increased
internalization from the apical cell
membrane; no effect on single channel
gating and conductance;
dbSNP:rs397508804).
{ECO:0000269|PubMed:12529365,
ECO:0000269|PubMed:9401006}.
/FTId=VAR_000140.
VARIANT 297 297 R -> Q (in CF; dbSNP:rs143486492).
/FTId=VAR_000141.
VARIANT 301 301 Y -> C (in CF; dbSNP:rs150691494).
/FTId=VAR_000142.
VARIANT 307 307 S -> N (in CF; dbSNP:rs397508817).
/FTId=VAR_000143.
VARIANT 311 311 F -> L (in CF; dbSNP:rs121909016).
/FTId=VAR_000144.
VARIANT 311 311 Missing (in CF).
{ECO:0000269|PubMed:9443874}.
/FTId=VAR_000145.
VARIANT 314 314 G -> E (in CF; dbSNP:rs75763344).
/FTId=VAR_000146.
VARIANT 314 314 G -> R (in CF; dbSNP:rs397508819).
{ECO:0000269|PubMed:8829633}.
/FTId=VAR_000147.
VARIANT 322 322 V -> M (in dbSNP:rs1800085).
/FTId=VAR_009898.
VARIANT 334 334 R -> W (in CF; mild; does not prevent
maturation of glycans;
dbSNP:rs121909011).
{ECO:0000269|PubMed:1699669}.
/FTId=VAR_000148.
VARIANT 336 336 I -> K (in CF; dbSNP:rs397508139).
/FTId=VAR_000150.
VARIANT 338 338 T -> I (in CF; mild; isolated hypotonic
dehydration; dbSNP:rs77409459).
{ECO:0000269|PubMed:7543567,
ECO:0000269|PubMed:9554753}.
/FTId=VAR_000151.
VARIANT 346 346 L -> P (in CF; dominant mutation but mild
phenotype; dbSNP:rs397508146).
{ECO:0000269|PubMed:7513296}.
/FTId=VAR_000152.
VARIANT 347 347 R -> H (in CF; dbSNP:rs77932196).
/FTId=VAR_000153.
VARIANT 347 347 R -> L (in CF; dbSNP:rs77932196).
/FTId=VAR_000154.
VARIANT 347 347 R -> P (in CF; MILD; dbSNP:rs77932196).
/FTId=VAR_000155.
VARIANT 351 351 T -> S (in dbSNP:rs1800086).
/FTId=VAR_009899.
VARIANT 352 352 R -> Q (in CF; dbSNP:rs121908753).
/FTId=VAR_000156.
VARIANT 353 353 Q -> H (in dbSNP:rs1800087).
/FTId=VAR_009900.
VARIANT 359 360 QT -> KK (in CF; dbSNP:rs397508152).
/FTId=VAR_000158.
VARIANT 359 359 Q -> K (in CF; dbSNP:rs76879328).
/FTId=VAR_000157.
VARIANT 370 370 K -> KNK (in CF).
{ECO:0000269|PubMed:9452073}.
/FTId=VAR_000159.
VARIANT 455 455 A -> E (in CF; dbSNP:rs74551128).
{ECO:0000269|PubMed:9401006}.
/FTId=VAR_000160.
VARIANT 456 456 V -> F (in CF; dbSNP:rs397508195).
/FTId=VAR_000161.
VARIANT 458 458 G -> V (in CF; dbSNP:rs121909009).
/FTId=VAR_000162.
VARIANT 467 467 L -> F (in dbSNP:rs1800089).
/FTId=VAR_000163.
VARIANT 470 470 V -> M (in dbSNP:rs213950).
{ECO:0000269|PubMed:10651488,
ECO:0000269|PubMed:1710598,
ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:2475911,
ECO:0000269|Ref.3}.
/FTId=VAR_000164.
VARIANT 480 480 G -> C (in CF; dbSNP:rs79282516).
/FTId=VAR_000165.
VARIANT 492 492 S -> F (in CF; dbSNP:rs121909017).
/FTId=VAR_000166.
VARIANT 504 504 E -> Q (in CF; dbSNP:rs397508223).
/FTId=VAR_000167.
VARIANT 506 506 I -> M (in dbSNP:rs1800092).
/FTId=VAR_009901.
VARIANT 506 506 I -> V (in dbSNP:rs1800091).
{ECO:0000269|PubMed:9921909}.
/FTId=VAR_000168.
VARIANT 507 507 I -> V (in dbSNP:rs1800091).
/FTId=VAR_000169.
VARIANT 507 507 Missing (in CF; impaired maturation of
glycan chains).
{ECO:0000269|PubMed:1699669,
ECO:0000269|PubMed:1710600}.
/FTId=VAR_000170.
VARIANT 508 508 F -> C (in dbSNP:rs1800093).
/FTId=VAR_000172.
VARIANT 508 508 Missing (in CF and CBAVD; most common
mutation; impairs protein folding and
stability; causes local changes to the
surface that mediates interactions
between domains; decreases frequency of
channel opening in vitro; decreases
presence at the cell membrane due to
retention in intracellular compartments;
impairs recycling to the cell membrane
after endocytosis).
{ECO:0000269|PubMed:12529365,
ECO:0000269|PubMed:1284548,
ECO:0000269|PubMed:15528182,
ECO:0000269|PubMed:15716351,
ECO:0000269|PubMed:1699669,
ECO:0000269|PubMed:1710600,
ECO:0000269|PubMed:20008117,
ECO:0000269|PubMed:20150177,
ECO:0000269|PubMed:25330774,
ECO:0000269|PubMed:28001373,
ECO:0000269|PubMed:28087700}.
/FTId=VAR_000171.
VARIANT 513 513 D -> G (in CBAVD; dbSNP:rs397508225).
{ECO:0000269|PubMed:10651488}.
/FTId=VAR_000173.
VARIANT 520 520 V -> F (in CF; dbSNP:rs77646904).
{ECO:0000269|PubMed:1284466}.
/FTId=VAR_000174.
VARIANT 532 532 K -> E (in dbSNP:rs35032490).
/FTId=VAR_048150.
VARIANT 544 544 G -> V (in CBAVD; dbSNP:rs397508241).
{ECO:0000269|Ref.112}.
/FTId=VAR_000175.
VARIANT 549 549 S -> I (in CF; impaired maturation of
glycan chains; dbSNP:rs121908755).
{ECO:0000269|PubMed:1699669,
ECO:0000269|PubMed:1712898}.
/FTId=VAR_000177.
VARIANT 549 549 S -> N (in CF; dbSNP:rs121908755).
/FTId=VAR_000176.
VARIANT 549 549 S -> R (in CF; impaired maturation of
glycan chains; dbSNP:rs121909005).
{ECO:0000269|PubMed:1712898}.
/FTId=VAR_000178.
VARIANT 551 551 G -> D (in CF; decreases frequency of
channel opening in vitro; decreases
channel activity and ATPase activity; no
effect on trafficking to the cell
membrane; no effect on protein stability;
no effect on maturation of glycans;
dbSNP:rs75527207).
{ECO:0000269|PubMed:1284548,
ECO:0000269|PubMed:1699669,
ECO:0000269|PubMed:1712898,
ECO:0000269|PubMed:28087700,
ECO:0000269|PubMed:8910473,
ECO:0000269|PubMed:9401006}.
/FTId=VAR_000179.
VARIANT 551 551 G -> S (in CF; dbSNP:rs121909013).
{ECO:0000269|PubMed:7606851}.
/FTId=VAR_000180.
VARIANT 553 553 R -> Q (in CF; dbSNP:rs121909044).
/FTId=VAR_000181.
VARIANT 558 558 L -> S (in CF; dbSNP:rs193922504).
/FTId=VAR_000182.
VARIANT 559 559 A -> T (in CF; impaired maturation of
glycan chains; dbSNP:rs75549581).
{ECO:0000269|PubMed:1712898}.
/FTId=VAR_000183.
VARIANT 560 560 R -> K (in CF; dbSNP:rs80055610).
/FTId=VAR_000184.
VARIANT 560 560 R -> S (in CF; dbSNP:rs397508267).
{ECO:0000269|PubMed:9482579}.
/FTId=VAR_000185.
VARIANT 560 560 R -> T (in CF; dbSNP:rs80055610).
/FTId=VAR_000186.
VARIANT 562 562 V -> I (in dbSNP:rs1800097).
/FTId=VAR_000187.
VARIANT 562 562 V -> L (in CF; dbSNP:rs1800097).
{ECO:0000269|PubMed:8956039}.
/FTId=VAR_000188.
VARIANT 563 563 Y -> N (in CF; dbSNP:rs121909006).
/FTId=VAR_000189.
VARIANT 569 569 Y -> C (in CF; dbSNP:rs397508277).
{ECO:0000269|PubMed:8723693}.
/FTId=VAR_000190.
VARIANT 569 569 Y -> D (in CF; dbSNP:rs397508276).
{ECO:0000269|PubMed:9482579}.
/FTId=VAR_000191.
VARIANT 569 569 Y -> H (in CF; dbSNP:rs397508276).
/FTId=VAR_000192.
VARIANT 571 571 L -> S (in CF; dbSNP:rs397508280).
/FTId=VAR_000193.
VARIANT 572 572 D -> N (in CF; impaired maturation of
glycan chains; dbSNP:rs397508282).
{ECO:0000269|PubMed:1712898,
ECO:0000269|PubMed:7541273}.
/FTId=VAR_000194.
VARIANT 574 574 P -> H (in CF; dbSNP:rs121908758).
/FTId=VAR_000195.
VARIANT 576 576 G -> A (in dbSNP:rs1800098).
/FTId=VAR_000196.
VARIANT 579 579 D -> G (in CF; dbSNP:rs397508288).
{ECO:0000269|PubMed:10094564,
ECO:0000269|PubMed:7544319}.
/FTId=VAR_000197.
VARIANT 601 601 I -> F (in CF; impaired maturation of
glycan chains; dbSNP:rs397508306).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000198.
VARIANT 605 605 S -> F (in dbSNP:rs766874).
/FTId=VAR_048151.
VARIANT 610 610 L -> S (in CF; impaired maturation of
glycan chains; dbSNP:rs397508311).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000199.
VARIANT 613 613 A -> T (in CF; impaired maturation of
glycan chains; dbSNP:rs201978662).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000200.
VARIANT 614 614 D -> G (in CF; impaired maturation of
glycan chains; dbSNP:rs201124247).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000201.
VARIANT 618 618 I -> T (in CF; impaired maturation of
glycan chains; dbSNP:rs139468767).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000202.
VARIANT 619 619 L -> S (in CF; impaired maturation of
glycan chains; dbSNP:rs397508313).
{ECO:0000269|PubMed:7525450,
ECO:0000269|PubMed:9736778}.
/FTId=VAR_000203.
VARIANT 620 620 H -> P (in CF; impaired maturation of
glycan chains; dbSNP:rs397508314).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000204.
VARIANT 620 620 H -> Q (in CF; no effect on glycan
maturation but strongly increased channel
activity; dbSNP:rs397508315).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000205.
VARIANT 622 622 G -> D (in oligospermia; no effect on
glycan maturation but decreased channel
activity; dbSNP:rs121908759).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000206.
VARIANT 628 628 G -> R (in CF; impaired maturation of
glycan chains; dbSNP:rs397508316).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000207.
VARIANT 633 633 L -> P (in CF; impaired maturation of
glycan chains; dbSNP:rs397508318).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000208.
VARIANT 648 648 D -> V (in CF; dbSNP:rs121909033).
/FTId=VAR_000209.
VARIANT 651 651 D -> N (in CF; dbSNP:rs780526529).
/FTId=VAR_000210.
VARIANT 654 654 S -> G (in dbSNP:rs1800099).
/FTId=VAR_009902.
VARIANT 665 665 T -> S (in CF; no effect on glycan
maturation and channel activity).
{ECO:0000269|PubMed:8800923,
ECO:0000269|PubMed:9736778}.
/FTId=VAR_000211.
VARIANT 668 668 R -> C (in dbSNP:rs1800100).
{ECO:0000269|PubMed:9921909}.
/FTId=VAR_000212.
VARIANT 693 693 F -> L (in CF; unknown pathological
significance; dbSNP:rs145540754 and
dbSNP:rs397508338).
{ECO:0000269|PubMed:12167682,
ECO:0000269|PubMed:8406518}.
/FTId=VAR_000213.
VARIANT 754 754 V -> M (in CF; dbSNP:rs150157202).
/FTId=VAR_000214.
VARIANT 766 766 R -> M (in CBAVD; dbSNP:rs397508363).
/FTId=VAR_000215.
VARIANT 792 792 R -> G (in CBAVD; no effect on glycan
maturation but decreased channel
activity; dbSNP:rs145449046).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000216.
VARIANT 800 800 A -> G (in CBAVD; no effect on glycan
maturation but strongly increased channel
activity; dbSNP:rs397508373).
{ECO:0000269|PubMed:7529962,
ECO:0000269|PubMed:9736778}.
/FTId=VAR_000217.
VARIANT 807 807 I -> M (in CBAVD; dbSNP:rs1800103).
/FTId=VAR_000218.
VARIANT 822 822 E -> K (in CF; dbSNP:rs397508378).
/FTId=VAR_000219.
VARIANT 826 826 E -> K (in thoracic sarcoidosis; no
effect on glycan maturation and channel
activity; dbSNP:rs397508381).
{ECO:0000269|PubMed:9736778}.
/FTId=VAR_000220.
VARIANT 866 866 C -> Y (in CF; dbSNP:rs193922506).
/FTId=VAR_000221.
VARIANT 903 903 Y -> H (in dbSNP:rs1800106).
/FTId=VAR_009903.
VARIANT 909 909 S -> I (in dbSNP:rs1800107).
/FTId=VAR_009904.
VARIANT 912 912 S -> L (in dbSNP:rs121909034).
{ECO:0000269|PubMed:7522211}.
/FTId=VAR_000222.
VARIANT 913 913 Y -> C (in CF; dbSNP:rs121909008).
/FTId=VAR_000223.
VARIANT 917 917 Y -> C (in CF; dbSNP:rs397508428).
/FTId=VAR_000224.
VARIANT 949 949 H -> Y (in CF; dbSNP:rs121909035).
{ECO:0000269|PubMed:7522211}.
/FTId=VAR_000225.
VARIANT 952 952 M -> I (in CF; dbSNP:rs151048781).
/FTId=VAR_000226.
VARIANT 967 967 L -> S (in dbSNP:rs1800110).
/FTId=VAR_009905.
VARIANT 997 997 L -> F (in CF; dbSNP:rs1800111).
/FTId=VAR_000227.
VARIANT 1005 1005 I -> R (in CF; dbSNP:rs397508479).
{ECO:0000269|PubMed:7525450}.
/FTId=VAR_000228.
VARIANT 1006 1006 A -> E (in CF; dbSNP:rs397508480).
{ECO:0000269|PubMed:7541510}.
/FTId=VAR_000229.
VARIANT 1013 1013 P -> L (in CF; dbSNP:rs193922516).
{ECO:0000269|PubMed:9521595}.
/FTId=VAR_000230.
VARIANT 1028 1028 M -> I (in CF; dbSNP:rs200553511).
{ECO:0000269|PubMed:9521595}.
/FTId=VAR_000231.
VARIANT 1052 1052 F -> V (in CF; dbSNP:rs150212784).
{ECO:0000269|PubMed:7683628}.
/FTId=VAR_000232.
VARIANT 1061 1061 G -> R (in CF; dbSNP:rs142394380).
{ECO:0000269|PubMed:7683628,
ECO:0000269|PubMed:8723695}.
/FTId=VAR_000233.
VARIANT 1065 1065 L -> P (in CF; dbSNP:rs121909036).
{ECO:0000269|PubMed:7522211}.
/FTId=VAR_000234.
VARIANT 1065 1065 L -> R (in CF; dbSNP:rs121909036).
{ECO:0000269|PubMed:9452054}.
/FTId=VAR_000235.
VARIANT 1066 1066 R -> C (in CF; dbSNP:rs78194216).
{ECO:0000269|PubMed:9375855}.
/FTId=VAR_000236.
VARIANT 1066 1066 R -> H (in CF; dbSNP:rs121909019).
/FTId=VAR_000237.
VARIANT 1066 1066 R -> L (in CF; dbSNP:rs121909019).
{ECO:0000269|PubMed:7683628}.
/FTId=VAR_000238.
VARIANT 1067 1067 A -> T (in CF; dbSNP:rs121909020).
/FTId=VAR_000239.
VARIANT 1067 1067 A -> V (in dbSNP:rs1800114).
/FTId=VAR_000240.
VARIANT 1070 1070 R -> P (in CF; dbSNP:rs78769542).
{ECO:0000269|PubMed:9401006}.
/FTId=VAR_000242.
VARIANT 1070 1070 R -> Q (in CF; dbSNP:rs78769542).
{ECO:0000269|PubMed:7683628}.
/FTId=VAR_000241.
VARIANT 1070 1070 R -> W (in CBAVD; dbSNP:rs202179988).
/FTId=VAR_011564.
VARIANT 1071 1071 Q -> P (in CF; dbSNP:rs121909037).
{ECO:0000269|PubMed:7522211}.
/FTId=VAR_000243.
VARIANT 1072 1072 P -> L (in CF).
/FTId=VAR_000244.
VARIANT 1077 1077 L -> P (in CF; dbSNP:rs139304906).
/FTId=VAR_000245.
VARIANT 1085 1085 H -> R (in CF; dbSNP:rs79635528).
{ECO:0000269|PubMed:7683628}.
/FTId=VAR_000246.
VARIANT 1098 1098 W -> R (in CF; dbSNP:rs397508531).
{ECO:0000269|PubMed:7537150}.
/FTId=VAR_000247.
VARIANT 1101 1101 M -> K (in CF; dbSNP:rs36210737).
{ECO:0000269|PubMed:7680525}.
/FTId=VAR_000248.
VARIANT 1101 1101 M -> R (in CF; dbSNP:rs36210737).
{ECO:0000269|PubMed:7683628}.
/FTId=VAR_011565.
VARIANT 1137 1137 M -> V (in CF; decreases channel
activity; no visible effect on protein
maturation; dbSNP:rs397508553).
{ECO:0000269|PubMed:9804160}.
/FTId=VAR_000249.
VARIANT 1140 1140 Missing (in CF; abolishes channel
activity; no visible effect on protein
maturation). {ECO:0000269|PubMed:9101301,
ECO:0000269|PubMed:9804160}.
/FTId=VAR_000250.
VARIANT 1152 1152 D -> H (in CF; decreases channel
activity; no visible effect on protein
maturation; dbSNP:rs75541969).
{ECO:0000269|PubMed:9804160}.
/FTId=VAR_000251.
VARIANT 1162 1162 R -> L (in dbSNP:rs1800120).
/FTId=VAR_000252.
VARIANT 1220 1220 T -> I (in dbSNP:rs1800123).
{ECO:0000269|PubMed:7522211}.
/FTId=VAR_000253.
VARIANT 1234 1234 I -> V (in CF; dbSNP:rs75389940).
/FTId=VAR_000254.
VARIANT 1235 1235 S -> R (in CF; dbSNP:rs34911792).
/FTId=VAR_000255.
VARIANT 1244 1244 G -> E (in CF; dbSNP:rs267606723).
/FTId=VAR_000256.
VARIANT 1249 1249 G -> E (in CF; dbSNP:rs121909040).
{ECO:0000269|PubMed:7520022}.
/FTId=VAR_000257.
VARIANT 1251 1251 S -> N (in CF; dbSNP:rs74503330).
/FTId=VAR_000258.
VARIANT 1255 1255 S -> P (in CF; dbSNP:rs121909041).
{ECO:0000269|PubMed:1284530}.
/FTId=VAR_000259.
VARIANT 1270 1270 D -> N (in CF; dbSNP:rs11971167).
/FTId=VAR_000260.
VARIANT 1282 1282 W -> R (in CF; dbSNP:rs397508616).
/FTId=VAR_000261.
VARIANT 1283 1283 R -> M (in CF; dbSNP:rs77902683).
{ECO:0000269|PubMed:1284468}.
/FTId=VAR_000262.
VARIANT 1286 1286 F -> S (in CF; dbSNP:rs121909028).
/FTId=VAR_000263.
VARIANT 1291 1291 Q -> H (in CF; dbSNP:rs121909015).
{ECO:0000269|PubMed:1284466}.
/FTId=VAR_000264.
VARIANT 1291 1291 Q -> R (in CF; dbSNP:rs397508621).
{ECO:0000269|PubMed:7525450}.
/FTId=VAR_000265.
VARIANT 1303 1303 N -> H (in CF; dbSNP:rs121909042).
/FTId=VAR_000266.
VARIANT 1303 1303 N -> K (in CF; impaired maturation of
glycan chains; has low in vitro channel
activity at low temperature;
dbSNP:rs80034486).
{ECO:0000269|PubMed:1712898,
ECO:0000269|PubMed:17182731,
ECO:0000269|PubMed:9401006}.
/FTId=VAR_000267.
VARIANT 1349 1349 G -> D (in CF; no effect on maturation of
glycan chains; dbSNP:rs193922525).
{ECO:0000269|PubMed:1712898}.
/FTId=VAR_000268.
VARIANT 1364 1364 A -> V (in CBAVD; dbSNP:rs397508670).
{ECO:0000269|Ref.112}.
/FTId=VAR_000269.
VARIANT 1397 1397 V -> E (in CF; dbSNP:rs397508691).
{ECO:0000269|PubMed:7524913}.
/FTId=VAR_000270.
VARIANT 1453 1453 R -> W (in dbSNP:rs4148725).
{ECO:0000269|Ref.3}.
/FTId=VAR_048152.
MUTAGEN 464 464 K->M: Impaired maturation of glycan
chains indicating impaired trafficking
from the endoplasmic reticulum to the
cell membrane.
{ECO:0000269|PubMed:1699669}.
MUTAGEN 508 508 F->R: Impaired maturation of glycan
chains indicating impaired trafficking
from the endoplasmic reticulum to the
cell membrane.
{ECO:0000269|PubMed:1699669,
ECO:0000269|PubMed:1712898}.
MUTAGEN 539 539 I->T: Enhances trafficking from the
endoplasmic reticulum to the cell
membrane. {ECO:0000269|PubMed:28001373}.
MUTAGEN 894 894 N->D: Abolishes N-glycosylation, enhances
endocytosis and impairs subsequent
recycling to the cell surface; when
associated with D-900.
{ECO:0000269|PubMed:20008117}.
MUTAGEN 900 900 N->D: Abolishes N-glycosylation, enhances
endocytosis and impairs subsequent
recycling to the cell surface; when
associated with D-894.
{ECO:0000269|PubMed:20008117}.
MUTAGEN 1137 1137 M->R: Abolishes channel activity. Impairs
protein maturation, suggesting the
protein is retained in the endoplasmic
reticulum. {ECO:0000269|PubMed:9804160}.
MUTAGEN 1139 1139 I->V: Decreases channel activity, no
visible effect on protein maturation.
{ECO:0000269|PubMed:9804160}.
MUTAGEN 1154 1154 D->G: Decreases channel activity, no
visible effect on protein maturation.
{ECO:0000269|PubMed:9804160}.
MUTAGEN 1250 1250 K->M: No effect on maturation of glycans,
suggesting that trafficking to the plasma
membrane is not altered.
{ECO:0000269|PubMed:1699669}.
CONFLICT 620 620 H -> N (in Ref. 1; AAA35680).
{ECO:0000305}.
CONFLICT 833 833 F -> L (in Ref. 1; AAA35680).
{ECO:0000305}.
STRAND 11 19 {ECO:0000244|PDB:3ISW}.
STRAND 390 399 {ECO:0000244|PDB:2PZE}.
HELIX 403 411 {ECO:0000244|PDB:2BBS}.
HELIX 414 417 {ECO:0000244|PDB:2BBT}.
HELIX 433 436 {ECO:0000244|PDB:1XMI}.
STRAND 440 449 {ECO:0000244|PDB:2PZE}.
STRAND 453 457 {ECO:0000244|PDB:2PZE}.
HELIX 464 471 {ECO:0000244|PDB:2PZE}.
STRAND 478 484 {ECO:0000244|PDB:2PZE}.
STRAND 488 491 {ECO:0000244|PDB:2PZE}.
STRAND 499 501 {ECO:0000244|PDB:2PZG}.
HELIX 502 507 {ECO:0000244|PDB:2PZE}.
HELIX 514 523 {ECO:0000244|PDB:2PZE}.
HELIX 527 530 {ECO:0000244|PDB:2PZE}.
STRAND 533 535 {ECO:0000244|PDB:2PZF}.
HELIX 536 538 {ECO:0000244|PDB:2PZE}.
STRAND 540 542 {ECO:0000244|PDB:1XMJ}.
HELIX 550 563 {ECO:0000244|PDB:2PZE}.
STRAND 567 573 {ECO:0000244|PDB:2PZE}.
TURN 574 577 {ECO:0000244|PDB:2PZE}.
HELIX 580 589 {ECO:0000244|PDB:2PZE}.
HELIX 590 594 {ECO:0000244|PDB:2PZE}.
TURN 595 597 {ECO:0000244|PDB:2PZE}.
STRAND 598 603 {ECO:0000244|PDB:2PZE}.
HELIX 607 612 {ECO:0000244|PDB:2PZE}.
STRAND 614 620 {ECO:0000244|PDB:2PZE}.
STRAND 623 628 {ECO:0000244|PDB:2PZE}.
HELIX 630 634 {ECO:0000244|PDB:2PZE}.
HELIX 640 644 {ECO:0000244|PDB:2PZE}.
HELIX 650 652 {ECO:0000244|PDB:2BBS}.
HELIX 655 669 {ECO:0000244|PDB:2BBS}.
STRAND 1204 1207 {ECO:0000244|PDB:3GD7}.
STRAND 1210 1223 {ECO:0000244|PDB:3GD7}.
STRAND 1226 1234 {ECO:0000244|PDB:3GD7}.
STRAND 1239 1245 {ECO:0000244|PDB:3GD7}.
HELIX 1250 1258 {ECO:0000244|PDB:3GD7}.
STRAND 1261 1271 {ECO:0000244|PDB:3GD7}.
HELIX 1279 1284 {ECO:0000244|PDB:3GD7}.
STRAND 1286 1290 {ECO:0000244|PDB:3GD7}.
STRAND 1297 1299 {ECO:0000244|PDB:3GD7}.
HELIX 1300 1304 {ECO:0000244|PDB:3GD7}.
HELIX 1312 1321 {ECO:0000244|PDB:3GD7}.
HELIX 1325 1328 {ECO:0000244|PDB:3GD7}.
HELIX 1334 1336 {ECO:0000244|PDB:3GD7}.
TURN 1341 1345 {ECO:0000244|PDB:3GD7}.
HELIX 1348 1361 {ECO:0000244|PDB:3GD7}.
STRAND 1366 1371 {ECO:0000244|PDB:3GD7}.
HELIX 1372 1375 {ECO:0000244|PDB:3GD7}.
HELIX 1378 1389 {ECO:0000244|PDB:3GD7}.
TURN 1390 1394 {ECO:0000244|PDB:3GD7}.
STRAND 1397 1400 {ECO:0000244|PDB:3GD7}.
STRAND 1402 1404 {ECO:0000244|PDB:3GD7}.
HELIX 1405 1407 {ECO:0000244|PDB:3GD7}.
STRAND 1411 1417 {ECO:0000244|PDB:3GD7}.
STRAND 1420 1426 {ECO:0000244|PDB:3GD7}.
HELIX 1427 1432 {ECO:0000244|PDB:3GD7}.
HELIX 1436 1441 {ECO:0000244|PDB:3GD7}.
STRAND 1442 1445 {ECO:0000244|PDB:3GD7}.
STRAND 1448 1457 {ECO:0000244|PDB:3GD7}.
STRAND 1462 1465 {ECO:0000244|PDB:3GD7}.
STRAND 1478 1480 {ECO:0000244|PDB:2LOB}.
SEQUENCE 1480 AA; 168142 MW; 8D082AA2E768C065 CRC64;
MQRSPLEKAS VVSKLFFSWT RPILRKGYRQ RLELSDIYQI PSVDSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGIFLYL GEVTKAVQPL LLGRIIASYD PDNKEERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL
GRMMMKYRDQ RAGKISERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNNNNRK
TSNGDDSLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMV IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLQPDF SSKLMGCDSF DQFSAERRNS
ILTETLHRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNPINSIRK FSIVQKTPLQ
MNGIEEDSDE PLERRLSLVP DSEQGEAILP RISVISTGPT LQARRRQSVL NLMTHSVNQG
QNIHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI
PAVTTWNTYL RYITVHKSLI FVLIWCLVIF LAEVAASLVV LWLLGNTPLQ DKGNSTHSRN
NSYAVIITST SSYYVFYIYV GVADTLLAMG FFRGLPLVHT LITVSKILHH KMLHSVLQAP
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVAV LQPYIFVATV
PVIVAFIMLR AYFLQTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK PYKNGQLSKV MIIENSHVKK
DDIWPSGGQM TVKDLTAKYT EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL
LNTEGEIQID GVSWDSITLQ QWRKAFGVIP QKVFIFSGTF RKNLDPYEQW SDQEIWKVAD
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT
YQIIRRTLKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNERSLFRQA
ISPSDRVKLF PHRNSSKCKS KPQIAALKEE TEEEVQDTRL


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