Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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_MOUSE              Reviewed;        1476 AA.
P26361; Q63893; Q63894; Q9JKQ6;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 2.
30-AUG-2017, entry version 177.
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:0000250|UniProtKB:P13569};
AltName: Full=cAMP-dependent chloride channel;
Name=Cftr; Synonyms=Abcc7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1712752; DOI=10.1016/0888-7543(91)90312-3;
Tata F., Stanier P., Wicking C., Halford S., Kruyer H., Lench N.J.,
Scambler P.J., Hansen C., Braman J.C., Williamson R., Wainwright B.J.;
"Cloning the mouse homolog of the human cystic fibrosis transmembrane
conductance regulator gene.";
Genomics 10:301-307(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1716243; DOI=10.1016/0888-7543(91)90434-G;
Yorifuji T., Lemna W.K., Ballard C.F., Rosenbloom C.L., Rozmahel R.,
Plavsic N., Tsui L.-C., Beaudet A.L.;
"Molecular cloning and sequence analysis of the murine cDNA for the
cystic fibrosis transmembrane conductance regulator.";
Genomics 10:547-550(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10655503; DOI=10.1073/pnas.97.3.1172;
Ellsworth R.E., Jamison D.C., Touchman J.W., Chissoe S.L.,
Braden Maduro V.V., Bouffard G.G., Dietrich N.L.,
Beckstrom-Sternberg S.M., Iyer L.M., Weintraub L.A., Cotton M.,
Courtney L., Edwards J., Maupin R., Ozersky P., Rohlfing T.,
Wohldmann P., Miner T., Kemp K., Kramer J., Korf I., Pepin K.,
Antonacci-Fulton L., Fulton R.S., Minx P., Hillier L.W., Wilson R.K.,
Waterston R.H., Miller W., Green E.D.;
"Comparative genomic sequence analysis of the human and mouse cystic
fibrosis transmembrane conductance regulator genes.";
Proc. Natl. Acad. Sci. U.S.A. 97:1172-1177(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
PubMed=7526924; DOI=10.1093/hmg/3.7.1089;
Denamur E., Chehab F.F.;
"Analysis of the mouse and rat CFTR promoter regions.";
Hum. Mol. Genet. 3:1089-1094(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-600, AND ALTERNATIVE
SPLICING.
TISSUE=Testis;
PubMed=7691356; DOI=10.1038/ng0893-426;
Delaney S.J., Rich D.P., Thomson S.A., Hargrave M.R., Lovelock P.K.,
Welsh M.J., Wainwright B.J.;
"Cystic fibrosis transmembrane conductance regulator splice variants
are not conserved and fail to produce chloride channels.";
Nat. Genet. 4:426-431(1993).
[6]
DISRUPTION PHENOTYPE.
PubMed=7685652; DOI=10.1038/ng0593-35;
Ratcliff R., Evans M.J., Cuthbert A.W., MacVinish L.J., Foster D.,
Anderson J.R., Colledge W.H.;
"Production of a severe cystic fibrosis mutation in mice by gene
targeting.";
Nat. Genet. 4:35-41(1993).
[7]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH AHCYL1.
PubMed=19033647; DOI=10.1172/JCI37914;
Yang D., Shcheynikov N., Zeng W., Ohana E., So I., Ando H.,
Mizutani A., Mikoshiba K., Muallem S.;
"IRBIT coordinates epithelial fluid and HCO3- secretion by stimulating
the transporters pNBC1 and CFTR in the murine pancreatic duct.";
J. Clin. Invest. 119:193-202(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-698 AND SER-790, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=20231442; DOI=10.1073/pnas.0902661107;
Lu M., Dong K., Egan M.E., Giebisch G.H., Boulpaep E.L., Hebert S.C.;
"Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-
PKA-regulated apical chloride channels in cortical collecting duct.";
Proc. Natl. Acad. Sci. U.S.A. 107:6082-6087(2010).
[10]
FUNCTION, AND INTERACTION WITH SLC26A3; SLC26A6 AND SLC9A3R1.
PubMed=21976599; DOI=10.1095/biolreprod.111.094037;
Chavez J.C., Hernandez-Gonzalez E.O., Wertheimer E., Visconti P.E.,
Darszon A., Trevino C.L.;
"Participation of the Cl-/HCO(3)- exchangers SLC26A3 and SLC26A6, the
Cl- channel CFTR, and the regulatory factor SLC9A3R1 in mouse sperm
capacitation.";
Biol. Reprod. 86:1-14(2012).
[11]
INTERACTION WITH AHCYL1.
PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K.,
Ando H., Mizutani A., Abe T., Kiyonari H., Seki G., Yule D.,
Mikoshiba K., Muallem S.;
"Irbit mediates synergy between ca(2+) and cAMP signaling pathways
during epithelial transport in mice.";
Gastroenterology 145:232-241(2013).
[12]
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).
[13]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 389-673 IN COMPLEXES WITH
ATP AND ATP ANALOGS, AND DOMAIN.
PubMed=14685259; DOI=10.1038/sj.emboj.7600040;
Lewis H.A., Buchanan S.G., Burley S.K., Conners K., Dickey M.,
Dorwart M., Fowler R., Gao X., Guggino W.B., Hendrickson W.A.,
Hunt J.F., Kearins M.C., Lorimer D., Maloney P.C., Post K.W.,
Rajashankar K.R., Rutter M.E., Sauder J.M., Shriver S.,
Thibodeau P.H., Thomas P.J., Zhang M., Zhao X., Emtage S.;
"Structure of nucleotide-binding domain 1 of the cystic fibrosis
transmembrane conductance regulator.";
EMBO J. 23:282-293(2004).
[14] {ECO:0000244|PDB:1XF9, ECO:0000244|PDB:1XFA}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 389-670 IN COMPLEX WITH ATP,
DOMAIN, AND MUTAGENESIS OF PHE-508.
PubMed=15619636; DOI=10.1038/nsmb881;
Thibodeau P.H., Brautigam C.A., Machius M., Thomas P.J.;
"Side chain and backbone contributions of Phe508 to CFTR folding.";
Nat. Struct. Mol. Biol. 12:10-16(2005).
[15] {ECO:0000244|PDB:3SI7}
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 389-673 IN COMPLEX WITH ATP
AND MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PHE-508.
PubMed=22265409; DOI=10.1016/j.cell.2011.11.023;
Mendoza J.L., Schmidt A., Li Q., Nuvaga E., Barrett T., Bridges R.J.,
Feranchak A.P., Brautigam C.A., Thomas P.J.;
"Requirements for efficient correction of F508 CFTR revealed by
analyses of evolved sequences.";
Cell 148:164-174(2012).
-!- 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:20231442, PubMed:22265409).
Channel activity is coupled to ATP hydrolysis. The ion channel is
also permeable to HCO(3-); selectivity depends on the
extracellular chloride concentration. Exerts its function also by
modulating the activity of other ion channels and transporters.
Contributes to the regulation of the pH and the ion content of the
epithelial fluid layer. Modulates the activity of the epithelial
sodium channel (ENaC) complex, in part by regulating the cell
surface expression of the ENaC complex. May regulate bicarbonate
secretion and salvage in epithelial cells by regulating the
transporter SLC4A7. Can inhibit the chloride channel activity of
ANO1 (By similarity). Plays a role in the chloride and bicarbonate
homeostasis during sperm epididymal maturation and capacitation
(PubMed:21976599). {ECO:0000250|UniProtKB:P13569,
ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:20231442,
ECO:0000269|PubMed:21976599, ECO:0000269|PubMed:22265409,
ECO:0000269|PubMed:26823428}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P13569}.
-!- SUBUNIT: Monomer; does not require oligomerization for channel
activity. May form oligomers in the membrane (By similarity).
Interacts with SLC26A3, SLC26A6 and SLC9A3R1 (PubMed:21976599).
Interacts with SHANK2 (By similarity). Interacts with MYO6 (By
similarity). Interacts (via C-terminus) with GOPC (via PDZ
domain); this promotes CFTR internalization and thereby decreases
channel activity. Interacts with SLC4A7 through SLC9A3R1. Found in
a complex with MYO5B and RAB11A. Interacts with ANO1. Interacts
with SLC26A8 (By similarity). Interacts with AHCYL1; the
interaction increases CFTR activity (PubMed:19033647,
PubMed:23542070). Interacts with CSE1L (By similarity).
{ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P34158,
ECO:0000269|PubMed:19033647, ECO:0000269|PubMed:21976599,
ECO:0000269|PubMed:23542070}.
-!- INTERACTION:
P19120:HSPA8 (xeno); NbExp=5; IntAct=EBI-6115317, EBI-907802;
Q9WVC8:Slc26a3; NbExp=3; IntAct=EBI-6115317, EBI-6895537;
Q8CIW6:Slc26a6; NbExp=3; IntAct=EBI-6115317, EBI-6895517;
P70441:Slc9a3r1; NbExp=3; IntAct=EBI-6115317, EBI-1184085;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:20231442}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Early endosome membrane
{ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P13569}. Cell membrane
{ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:22265409}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P13569}. Recycling
endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P13569}. Endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P13569}. Note=The channel
is internalized from the cell surface into an endosomal recycling
compartment, from where it is recycled to the cell membrane. In
the oviduct and bronchus, detected on the apical side of
epithelial cells, but not associated with cilia.
{ECO:0000250|UniProtKB:P13569}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P26361-1; Sequence=Displayed;
Name=2;
IsoId=P26361-2; Sequence=VSP_000062, VSP_000063;
Name=3;
IsoId=P26361-3; Sequence=VSP_000064, VSP_000065;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in a variety of
epithelial tissues including colon, kidney, lung, small intestine,
pancreatic duct and testis. Isoforms 2 and 3 are expressed only in
testis. {ECO:0000269|PubMed:19033647}.
-!- DOMAIN: Binds and hydrolyzes ATP via the two cytoplasmic ABC
transporter nucleotide-binding domains. The two ATP-binding
domains interact with each other, forming a head-to-tail dimer.
Normal ATPase activity requires interaction between the two
domains (By similarity). The first ABC transporter nucleotide-
binding domain has no ATPase activity by itself (PubMed:14685259,
PubMed:15619636). {ECO:0000250|UniProtKB:P13569,
ECO:0000269|PubMed:14685259, ECO:0000269|PubMed:15619636}.
-!- DOMAIN: The PDZ-binding motif mediates interactions with GOPC and
with the SLC4A7, SLC9A3R1/EBP50 complex.
{ECO:0000250|UniProtKB:P13569}.
-!- DOMAIN: The R region is intrinsically disordered. It mediates
channel activation when it is phosphorylated, but not in the
absence of phosphorylation. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: Phosphorylated; cAMP treatment promotes phosphorylation and
activates the channel. Dephosphorylation decreases the ATPase
activity (in vitro). Phosphorylation at PKA sites activates the
channel. Phosphorylation at PKC sites enhances the response to
phosphorylation by PKA. Phosphorylated by AMPK; this inhibits
channel activity. {ECO:0000250|UniProtKB:P13569}.
-!- PTM: Ubiquitinated, leading to its degradation in the lysosome.
Deubiquitination by USP10 in early endosomes enhances its
endocytic recycling to the cell membrane. Ubiquitinated by RNF185
during ER stress. {ECO:0000250|UniProtKB:P13569}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate, but about 80% die within two to five days after birth due to
peritonitis (PubMed:7685652). Those that survive fail to thrive,
appear runted and weigh about half as much as wild-type
littermates (PubMed:7685652). Many of the surviving pups die when
they start ingesting solid food, due to intestinal blockage caused
by excessive mucus accumulation (PubMed:7685652). None survive for
more than about 45 days after birth (PubMed:7685652). Intestinal
crypts in the jejunum and ileum are filled with excessive mucus
(PubMed:7685652). Excessive accumulation of mucus is also seen in
colon (PubMed:7685652). In contrast, their lungs do not present
pathological mucus accumulation (PubMed:7685652). Likewise, only
five out of ten animals show dilatation and blockage of several
small pancreatic ducts (PubMed:7685652). Besides, mutant mice
present defects in their lacrimal glands that make them more
susceptible to develop eye infections (PubMed:7685652). In caecum
epithelium, forskolin-sensitive ion transport is nearly abolished
(PubMed:7685652). {ECO:0000269|PubMed:7685652}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M69298; AAA37417.1; -; mRNA.
EMBL; M60493; AAA18903.1; -; mRNA.
EMBL; AF162137; AAF30300.1; -; Genomic_DNA.
EMBL; L04873; AAA73562.1; -; Genomic_DNA.
EMBL; S65942; AAB28393.1; -; Genomic_DNA.
EMBL; S65940; AAB28393.1; JOINED; Genomic_DNA.
EMBL; S65941; AAB28393.1; JOINED; Genomic_DNA.
EMBL; S65942; AAB28391.1; -; Genomic_DNA.
EMBL; S65941; AAB28392.1; -; Genomic_DNA.
EMBL; S65940; AAB28392.1; JOINED; Genomic_DNA.
CCDS; CCDS19930.1; -. [P26361-1]
PIR; A39901; A39901.
PIR; A40303; A40303.
PIR; I49593; I49593.
PIR; I58115; I58115.
PIR; I78527; I78527.
RefSeq; NP_066388.1; NM_021050.2. [P26361-1]
RefSeq; XP_006505040.1; XM_006504977.1. [P26361-1]
RefSeq; XP_006505041.1; XM_006504978.1. [P26361-1]
UniGene; Mm.15621; -.
PDB; 1Q3H; X-ray; 2.50 A; A/B/C/D=389-673.
PDB; 1R0W; X-ray; 2.20 A; A/B/C/D=389-673.
PDB; 1R0X; X-ray; 2.20 A; A/B/C/D=389-673.
PDB; 1R0Y; X-ray; 2.55 A; A/B/C/D=389-673.
PDB; 1R0Z; X-ray; 2.35 A; A/B/C/D=389-673.
PDB; 1R10; X-ray; 3.00 A; A/B=389-673.
PDB; 1XF9; X-ray; 2.70 A; A/B/C/D=389-670.
PDB; 1XFA; X-ray; 3.10 A; A/B=389-670.
PDB; 3SI7; X-ray; 2.25 A; A/B/C/D=389-673.
PDBsum; 1Q3H; -.
PDBsum; 1R0W; -.
PDBsum; 1R0X; -.
PDBsum; 1R0Y; -.
PDBsum; 1R0Z; -.
PDBsum; 1R10; -.
PDBsum; 1XF9; -.
PDBsum; 1XFA; -.
PDBsum; 3SI7; -.
ProteinModelPortal; P26361; -.
SMR; P26361; -.
BioGrid; 198687; 2.
DIP; DIP-29618N; -.
IntAct; P26361; 9.
MINT; MINT-2841263; -.
STRING; 10090.ENSMUSP00000049228; -.
iPTMnet; P26361; -.
PhosphoSitePlus; P26361; -.
MaxQB; P26361; -.
PaxDb; P26361; -.
PeptideAtlas; P26361; -.
PRIDE; P26361; -.
DNASU; 12638; -.
Ensembl; ENSMUST00000045706; ENSMUSP00000049228; ENSMUSG00000041301. [P26361-1]
Ensembl; ENSMUST00000115405; ENSMUSP00000111064; ENSMUSG00000041301. [P26361-3]
Ensembl; ENSMUST00000140407; ENSMUSP00000116957; ENSMUSG00000041301. [P26361-2]
GeneID; 12638; -.
KEGG; mmu:12638; -.
UCSC; uc009bai.1; mouse. [P26361-1]
CTD; 1080; -.
MGI; MGI:88388; Cftr.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00890000139450; -.
HOGENOM; HOG000185880; -.
HOVERGEN; HBG004169; -.
InParanoid; P26361; -.
KO; K05031; -.
OMA; LAHFVWI; -.
OrthoDB; EOG091G00K4; -.
PhylomeDB; P26361; -.
TreeFam; TF105200; -.
BRENDA; 3.6.3.49; 3474.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
Reactome; R-MMU-5627083; RHO GTPases regulate CFTR trafficking.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
ChiTaRS; Cftr; mouse.
EvolutionaryTrace; P26361; -.
PRO; PR:P26361; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000041301; -.
ExpressionAtlas; P26361; baseline and differential.
Genevisible; P26361; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0031205; C:endoplasmic reticulum Sec complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0055037; C:recycling endosome; ISO:MGI.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0005254; F:chloride channel activity; IDA:UniProtKB.
GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0005260; F:intracellular ATPase-gated chloride channel activity; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; IDA:UniProtKB.
GO; GO:0006821; P:chloride transport; IGI:MGI.
GO; GO:0006695; P:cholesterol biosynthetic process; IMP:MGI.
GO; GO:0030301; P:cholesterol transport; IMP:MGI.
GO; GO:0051454; P:intracellular pH elevation; IMP:UniProtKB.
GO; GO:0060081; P:membrane hyperpolarization; IMP:UniProtKB.
GO; GO:0050891; P:multicellular organismal water homeostasis; ISS: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; ISO:MGI.
GO; GO:0048240; P:sperm capacitation; IMP:UniProtKB.
GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:UniProtKB.
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; 3.
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; Endoplasmic reticulum;
Endosome; Glycoprotein; Hydrolase; Ion channel; Ion transport;
Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 1476 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000093424.
TOPO_DOM 1 77 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 78 98 Helical; Name=1.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 99 122 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 123 146 Helical; Name=2.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 147 195 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 196 216 Helical; Name=3.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 217 222 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 223 243 Helical; Name=4.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 244 298 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 299 319 Helical; Name=5.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 320 339 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 340 358 Helical; Name=6.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 359 853 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 854 874 Helical; Name=7.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 875 913 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 914 934 Discontinuously helical; Name=8.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 935 985 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 986 1006 Helical; Name=9.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1007 1008 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1009 1029 Helical; Name=10.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1030 1090 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1091 1111 Helical; Name=11.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1112 1125 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1126 1146 Helical; Name=12.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1147 1476 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
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 854 1153 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1208 1439 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 458 465 ATP 1. {ECO:0000244|PDB:1Q3H,
ECO:0000244|PDB:1R0X,
ECO:0000244|PDB:1R0Z,
ECO:0000244|PDB:1R10,
ECO:0000244|PDB:1XF9,
ECO:0000244|PDB:1XFA,
ECO:0000244|PDB:3SI7,
ECO:0000255|PROSITE-ProRule:PRU00434}.
NP_BIND 1240 1247 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 654 826 Intrinsically disordered R region.
{ECO:0000250|UniProtKB:P13569}.
MOTIF 1474 1476 PDZ-binding.
{ECO:0000250|UniProtKB:P13569}.
BINDING 401 401 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 493 493 ATP 1. {ECO:0000244|PDB:1Q3H,
ECO:0000244|PDB:1R0X,
ECO:0000244|PDB:1R0Z,
ECO:0000244|PDB:1XFA}.
BINDING 1215 1215 ATP 2. {ECO:0000250|UniProtKB:P13569}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 670 670 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 715 715 Phosphothreonine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 763 763 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 808 808 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1440 1440 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 524 524 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 1391 1391 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
CARBOHYD 889 889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 895 895 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 561 600 AVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTR
-> QRTRSPYLEIRIFLCLFLYTRMKVCATTPEQYIKMLIC
TY (in isoform 3). {ECO:0000305}.
/FTId=VSP_000064.
VAR_SEQ 561 576 AVYKDADLYLLDSPFG -> FLICLQTKDKVSLFRN (in
isoform 2). {ECO:0000305}.
/FTId=VSP_000062.
VAR_SEQ 577 1476 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_000063.
VAR_SEQ 601 1476 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_000065.
MUTAGEN 508 508 F->A,L,Q: Mildly impairs protein
maturation.
{ECO:0000269|PubMed:15619636}.
MUTAGEN 508 508 F->C,M: No effect on protein maturation.
{ECO:0000269|PubMed:15619636}.
MUTAGEN 508 508 F->E,D,G,H,I,K,P,R,Y: Abolishes normal
maturation.
{ECO:0000269|PubMed:15619636}.
MUTAGEN 508 508 F->N,S,V: Nearly abolishes normal
maturation.
{ECO:0000269|PubMed:15619636}.
MUTAGEN 508 508 Missing: Impairs protein folding, due to
small local changes that probably disrupt
crucial interactions with the
transmembrane domain. Abolishes normal
maturation. {ECO:0000269|PubMed:15619636,
ECO:0000269|PubMed:22265409}.
CONFLICT 20 22 TTP -> STA (in Ref. 3; AAF30300).
{ECO:0000305}.
CONFLICT 30 30 H -> Q (in Ref. 3; AAF30300).
{ECO:0000305}.
CONFLICT 410 412 EKV -> QKA (in Ref. 1; AAA37417).
{ECO:0000305}.
CONFLICT 462 462 S -> L (in Ref. 1; AAA37417).
{ECO:0000305}.
CONFLICT 623 623 S -> T (in Ref. 1; AAA37417).
{ECO:0000305}.
CONFLICT 639 639 D -> S (in Ref. 1; AAA37417).
{ECO:0000305}.
STRAND 392 400 {ECO:0000244|PDB:1R0W}.
HELIX 405 412 {ECO:0000244|PDB:1R0W}.
HELIX 423 425 {ECO:0000244|PDB:1R0Z}.
HELIX 430 435 {ECO:0000244|PDB:1R0W}.
STRAND 439 448 {ECO:0000244|PDB:1R0W}.
STRAND 453 459 {ECO:0000244|PDB:1R0W}.
HELIX 464 471 {ECO:0000244|PDB:1R0W}.
STRAND 478 483 {ECO:0000244|PDB:1R0W}.
STRAND 488 491 {ECO:0000244|PDB:1R0W}.
STRAND 499 501 {ECO:0000244|PDB:1R0W}.
HELIX 502 506 {ECO:0000244|PDB:1R0W}.
TURN 507 509 {ECO:0000244|PDB:1R0W}.
HELIX 514 523 {ECO:0000244|PDB:1R0W}.
HELIX 527 530 {ECO:0000244|PDB:1R0W}.
HELIX 536 538 {ECO:0000244|PDB:1R0W}.
HELIX 543 545 {ECO:0000244|PDB:1R0X}.
HELIX 550 563 {ECO:0000244|PDB:1R0W}.
STRAND 567 573 {ECO:0000244|PDB:1R0W}.
HELIX 580 589 {ECO:0000244|PDB:1R0W}.
HELIX 590 594 {ECO:0000244|PDB:1R0W}.
TURN 595 597 {ECO:0000244|PDB:1R0W}.
STRAND 598 603 {ECO:0000244|PDB:1R0W}.
HELIX 607 611 {ECO:0000244|PDB:1R0W}.
STRAND 614 620 {ECO:0000244|PDB:1R0W}.
STRAND 623 628 {ECO:0000244|PDB:1R0W}.
HELIX 630 636 {ECO:0000244|PDB:1R0W}.
HELIX 638 645 {ECO:0000244|PDB:1R0W}.
STRAND 647 649 {ECO:0000244|PDB:1R0W}.
HELIX 650 652 {ECO:0000244|PDB:1R0W}.
HELIX 655 668 {ECO:0000244|PDB:1R0W}.
SEQUENCE 1476 AA; 167870 MW; 3D1B0BBDD80C1DA8 CRC64;
MQKSPLEKAS FISKLFFSWT TPILRKGYRH HLELSDIYQA PSADSADHLS EKLEREWDRE
QASKKNPQLI HALRRCFFWR FLFYGILLYL GEVTKAVQPV LLGRIIASYD PENKVERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHRIGM QMRTAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF IWIAPLQVTL LMGLLWDLLQ FSAFCGLGLL IILVIFQAIL
GKMMVKYRDQ RAAKINERLV ITSEIIDNIY SVKAYCWESA MEKMIENLRE VELKMTRKAA
YMRFFTSSAF FFSGFFVVFL SVLPYTVING IVLRKIFTTI SFCIVLRMSV TRQFPTAVQI
WYDSFGMIRK IQDFLQKQEY KVLEYNLMTT GIIMENVTAF WEEGFGELLE KVQQSNGDRK
HSSDENNVSF SHLCLVGNPV LKNINLNIEK GEMLAITGST GSGKTSLLML ILGELEASEG
IIKHSGRVSF CSQFSWIMPG TIKENIIFGV SYDEYRYKSV VKACQLQQDI TKFAEQDNTV
LGEGGVTLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV FTEEQVFESC VCKLMANKTR
ILVTSKMEHL RKADKILILH QGSSYFYGTF SELQSLRPDF SSKLMGYDTF DQFTEERRSS
ILTETLRRFS VDDSSAPWSK PKQSFRQTGE VGEKRKNSIL NSFSSVRKIS IVQKTPLCID
GESDDLQEKR LSLVPDSEQG EAALPRSNMI ATGPTFPGRR RQSVLDLMTF TPNSGSSNLQ
RTRTSIRKIS LVPQISLNEV DVYSRRLSQD STLNITEEIN EEDLKECFLD DVIKIPPVTT
WNTYLRYFTL HKGLLLVLIW CVLVFLVEVA ASLFVLWLLK NNPVNSGNNG TKISNSSYVV
IITSTSFYYI FYIYVGVADT LLALSLFRGL PLVHTLITAS KILHRKMLHS ILHAPMSTIS
KLKAGGILNR FSKDIAILDD FLPLTIFDFI QLVFIVIGAI IVVSALQPYI FLATVPGLVV
FILLRAYFLH TAQQLKQLES EGRSPIFTHL VTSLKGLWTL RAFRRQTYFE TLFHKALNLH
TANWFMYLAT LRWFQMRIDM IFVLFFIVVT FISILTTGEG EGTAGIILTL AMNIMSTLQW
AVNSSIDTDS LMRSVSRVFK FIDIQTEESM YTQIIKELPR EGSSDVLVIK NEHVKKSDIW
PSGGEMVVKD LTVKYMDDGN AVLENISFSI SPGQRVGLLG RTGSGKSTLL SAFLRMLNIK
GDIEIDGVSW NSVTLQEWRK AFGVITQKVF IFSGTFRQNL DPNGKWKDEE IWKVADEVGL
KSVIEQFPGQ LNFTLVDGGY VLSHGHKQLM CLARSVLSKA KIILLDEPSA HLDPITYQVI
RRVLKQAFAG CTVILCEHRI EAMLDCQRFL VIEESNVWQY DSLQALLSEK SIFQQAISSS
EKMRFFQGRH SSKHKPRTQI TALKEETEEE VQETRL


Related products :

Catalog number Product name Quantity
EIAAB06989 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Pig,Sus scrofa
EIAAB06993 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Oryctolagus cunicu
EIAAB06991 ABCC7,ATP-binding cassette sub-family C member 7,Bos taurus,Bovine,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator
EIAAB06992 Abcc7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,Cftr,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Rat,Rattus norvegi
EIAAB06988 Abcc7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,Cftr,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Mouse,Mus musculus
EIAAB06994 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane conductance regulator,Homo sapiens,Human
EIAAB06990 ABCC7,ATP-binding cassette sub-family C member 7,cAMP-dependent chloride channel,Canis familiaris,Canis lupus familiaris,CFTR,CFTR,Channel conductance-controlling ATPase,Cystic fibrosis transmembrane
20-783-73186 MOUSE ANTI HUMAN CFTR - CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR PROTEIN; CFTR; cAMP-dependent chloride channel; ATP-binding cassette transporter sub-family C member 7 Monoclonal 0.2 mg
CGA CFTR Gene cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7)
CSB-EL005292RA Rat cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL005292DO Dog cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL005292PI Pig cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL005292SH Sheep cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Sheep, Sample Type serum, plasma 96T
CSB-EL005292RH Monkey cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Monkey, Sample Type serum, plasma 96T
CSB-EL005292MO Mouse cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL005292HU Human cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL005292BO Bovine cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL005292GU Guinea pig cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
CSB-EL005292HO Horse cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Horse, Sample Type serum, plasma 96T
CSB-EL005292RB Rabbit cystic fibrosis transmembrane conductance regulator (ATP-binding cassette sub-family C, member 7) (CFTR) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
DL-CFTR-Hu Human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) ELISA Kit 96T
Y102989 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
Y108236 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 100ug
Y102988 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
GWB-E45859 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), Antibody


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur