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

 CFTR_DANRE              Reviewed;        1485 AA.
Q1LX78; B7ZVN9;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 1.
30-AUG-2017, entry version 102.
RecName: Full=Cystic fibrosis transmembrane conductance regulator {ECO:0000255|RuleBase:RU362037};
EC=3.6.3.49 {ECO:0000255|RuleBase:RU362037, ECO:0000269|PubMed:27912062};
AltName: Full=ATP-binding cassette sub-family C member 7 {ECO:0000255|RuleBase:RU362037};
AltName: Full=Channel conductance-controlling ATPase {ECO:0000255|RuleBase:RU362037};
AltName: Full=cAMP-dependent chloride channel {ECO:0000255|RuleBase:RU362037};
Name=cftr {ECO:0000312|ZFIN:ZDB-GENE-050517-20};
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955 {ECO:0000312|Ensembl:ENSDARP00000060242};
[1] {ECO:0000312|Ensembl:ENSDARP00000060242, ECO:0000312|Proteomes:UP000000437}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen {ECO:0000312|Ensembl:ENSDARP00000060242,
ECO:0000312|Proteomes:UP000000437};
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2] {ECO:0000312|EMBL:AAI71654.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[4]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=20732993; DOI=10.1128/IAI.00302-10;
Phennicie R.T., Sullivan M.J., Singer J.T., Yoder J.A., Kim C.H.;
"Specific resistance to Pseudomonas aeruginosa infection in zebrafish
is mediated by the cystic fibrosis transmembrane conductance
regulator.";
Infect. Immun. 78:4542-4550(2010).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 205-SER-PRO-206.
PubMed=23487313; DOI=10.1242/dev.091819;
Navis A., Marjoram L., Bagnat M.;
"Cftr controls lumen expansion and function of Kupffer's vesicle in
zebrafish.";
Development 140:1703-1712(2013).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=26432887; DOI=10.1242/bio.014076;
Roxo-Rosa M., Jacinto R., Sampaio P., Lopes S.S.;
"The zebrafish Kupffer's vesicle as a model system for the molecular
mechanisms by which the lack of Polycystin-2 leads to stimulation of
CFTR.";
Biol. Open 4:1356-1366(2015).
[7]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
STAGE, AND TISSUE SPECIFICITY.
PubMed=25592226; DOI=10.1016/j.ydbio.2014.12.034;
Navis A., Bagnat M.;
"Loss of cftr function leads to pancreatic destruction in larval
zebrafish.";
Dev. Biol. 399:237-248(2015).
[8]
STRUCTURE BY ELECTRON MICROSCOPY (3.73 ANGSTROMS), CATALYTIC ACTIVITY,
TOPOLOGY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=27912062; DOI=10.1016/j.cell.2016.11.014;
Zhang Z., Chen J.;
"Atomic structure of the cystic fibrosis transmembrane conductance
regulator.";
Cell 167:1586-1597(2016).
-!- FUNCTION: Epithelial ion channel that plays an important role in
the regulation of epithelial ion and water transport and fluid
homeostasis (PubMed:20933420, PubMed:23487313, PubMed:25592226).
Mediates the transport of chloride ions across the cell membrane
(By similarity). 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 (By similarity). Required
for normal fluid homeostasis in the gut (PubMed:20933420).
Required for normal volume expansion of Kupffer's vesicle during
embryonic development and for normal establishment of left-right
body patterning (PubMed:23487313, PubMed:26432887). Required for
normal resistance to infection by P.aeruginosa strain PA14 and
strain SMC573 (PubMed:20732993). {ECO:0000250|UniProtKB:P13569,
ECO:0000269|PubMed:20732993, ECO:0000269|PubMed:20933420,
ECO:0000269|PubMed:23487313, ECO:0000269|PubMed:26432887,
ECO:0000305|PubMed:25592226}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000255|RuleBase:RU362037, ECO:0000269|PubMed:27912062}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.22 mM for ATP {ECO:0000269|PubMed:27912062};
-!- SUBUNIT: Monomer; does not require oligomerization for channel
activity (By similarity). Interacts with cse1l; this interaction
may downregulate cftr activity (PubMed:20933420).
{ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:20933420}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:20933420, ECO:0000269|PubMed:23487313,
ECO:0000269|PubMed:25592226}; Multi-pass membrane protein
{ECO:0000269|PubMed:27912062}. Early endosome membrane
{ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein
{ECO:0000269|PubMed:27912062}. Cell membrane
{ECO:0000269|PubMed:23487313, ECO:0000305|PubMed:27912062}; Multi-
pass membrane protein {ECO:0000269|PubMed:27912062}. Recycling
endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass
membrane protein {ECO:0000269|PubMed:27912062}. Endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass
membrane protein {ECO:0000269|PubMed:27912062}. Note=The channel
is internalized from the cell surface into an endosomal recycling
compartment, from where it is recycled to the cell membrane.
{ECO:0000250|UniProtKB:P13569}.
-!- TISSUE SPECIFICITY: Detected in gut epithelium (at protein level)
(PubMed:20933420). Detected in kidney, spleen, intestine and liver
(PubMed:20732993). Detected in pancreatic duct epithelium at 5 dpf
and throughout adult life (PubMed:25592226).
{ECO:0000269|PubMed:20732993, ECO:0000269|PubMed:25592226}.
-!- DEVELOPMENTAL STAGE: First detected in developing pancreatic duct
at 3 dpf (PubMed:25592226). Detected on Kupffer's vesicle during
embryonic development (PubMed:23487313, PubMed:26432887). Detected
on neural floorplate, brain and pronephric duct primordia in
embryos at the 10 somite stage (PubMed:26432887).
{ECO:0000269|PubMed:23487313, ECO:0000269|PubMed:25592226,
ECO:0000269|PubMed:26432887}.
-!- 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. The first ABC transporter nucleotide-binding domain has
no ATPase activity by itself. {ECO:0000250|UniProtKB:P13569,
ECO:0000250|UniProtKB:P26361}.
-!- 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: Phosphorylated; this activates the channel (PubMed:27912062).
Dephosphorylation strongly decreases ATPase activity
(PubMed:27912062). Phosphorylation at PKA sites activates the
channel. Phosphorylation at PKC sites enhances the response to
phosphorylation by PKA (By similarity).
{ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:27912062}.
-!- DISRUPTION PHENOTYPE: Considerable lethality around 10 dpf
(PubMed:25592226). No effect on initial pancreas development, but
at 16 dpf mutants display loss of pancreatic acinar tissue
(PubMed:25592226). At 22 dpf, most pancreatic acinar tissue has
disappeared and has been replaced by fibrotic tissue that
surrounds dilated, mucus-filled ducts (PubMed:25592226).
Morpholino knockdown of the protein in 48 hpf embryos leads to
impaired resistance to P.aeruginosa strain PA14 and strain SMC573,
as shown by the increased bacterial burden, but there is no effect
on resistance to E.tarda, B.cenocepacia, S.aureus MZ100, E.coli
XL-10 and H.influenzae Hib EAGAN (PubMed:20732993). Morpholino
knockdown of the protein causes an importanr reduction of the
volume of Kupffer's vesicle during embryonic development
(PubMed:26432887). {ECO:0000269|PubMed:20732993,
ECO:0000269|PubMed:25592226, ECO:0000269|PubMed:26432887}.
-!- MISCELLANEOUS: Mutations that lead to the production of a severely
truncated protein that ends before the start of the fourth
transmembrane domain disrupt normal left-right body patterning
during embryogenesis and abolish lumen expansion of Kupffer's
vesicle. {ECO:0000269|PubMed:23487313}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. CFTR transporter (TC 3.A.1.202) subfamily.
{ECO:0000255|RuleBase:RU362037}.
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EMBL; BX470130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC171654; AAI71654.1; -; mRNA.
RefSeq; NP_001038348.1; NM_001044883.1.
UniGene; Dr.74099; -.
PDB; 5UAR; EM; 3.73 A; A=1-1485.
PDBsum; 5UAR; -.
ProteinModelPortal; Q1LX78; -.
SMR; Q1LX78; -.
STRING; 7955.ENSDARP00000060242; -.
PaxDb; Q1LX78; -.
Ensembl; ENSDART00000060243; ENSDARP00000060242; ENSDARG00000041107.
GeneID; 559080; -.
KEGG; dre:559080; -.
CTD; 1080; -.
ZFIN; ZDB-GENE-050517-20; cftr.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00890000139450; -.
HOVERGEN; HBG004169; -.
InParanoid; Q1LX78; -.
KO; K05031; -.
PhylomeDB; Q1LX78; -.
TreeFam; TF105200; -.
Reactome; R-DRE-382556; ABC-family proteins mediated transport.
Reactome; R-DRE-5627083; RHO GTPases regulate CFTR trafficking.
Reactome; R-DRE-5689880; Ub-specific processing proteases.
Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
Proteomes; UP000000437; Chromosome 18.
Bgee; ENSDARG00000041107; -.
ExpressionAtlas; Q1LX78; baseline.
GO; GO:0016324; C:apical plasma membrane; IDA:ZFIN.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
GO; GO:0005260; F:intracellular ATPase-gated chloride channel activity; ISS:UniProtKB.
GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:ZFIN.
GO; GO:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
GO; GO:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
GO; GO:0031016; P:pancreas development; IMP:ZFIN.
GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP:ZFIN.
GO; GO:0002679; P:respiratory burst involved in defense response; IMP:ZFIN.
GO; GO:0035377; P:transepithelial water transport; ISS: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; ATP-binding; Cell membrane; Chloride; Chloride channel;
Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein;
Hydrolase; Ion channel; Ion transport; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1485 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000439670.
TOPO_DOM 1 78 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 79 99 Helical; Name=1.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 100 123 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 124 149 Helical; Name=2.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 150 195 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 196 216 Helical; Name=3.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 217 224 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 225 245 Helical; Name=4.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 246 299 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 300 320 Helical; Name=5.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 321 340 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 341 363 Helical; Name=6.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 364 856 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 857 877 Helical; Name=7.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 878 924 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 925 946 Discontinuously helical; Name=8.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 947 996 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 997 1019 Helical; Name=9.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 1020 1021 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 1022 1042 Helical; Name=10.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 1043 1103 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 1104 1124 Helical; Name=11.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 1125 1138 Extracellular.
{ECO:0000269|PubMed:27912062}.
TRANSMEM 1139 1159 Helical; Name=12.
{ECO:0000269|PubMed:27912062}.
TOPO_DOM 1160 1485 Cytoplasmic.
{ECO:0000269|PubMed:27912062}.
DOMAIN 83 353 ABC transmembrane type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 424 645 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 860 1163 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1211 1444 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 457 464 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1245 1252 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 653 826 Intrinsically disordered R region.
{ECO:0000250|UniProtKB:P13569}.
MOTIF 1483 1485 PDZ-binding.
{ECO:0000250|UniProtKB:P13569}.
BINDING 402 402 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 492 492 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 1220 1220 ATP 2. {ECO:0000250|UniProtKB:P13569}.
CARBOHYD 897 897 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 903 903 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 205 206 Missing: In pd1048; abolishes trafficking
to the cell membrane and leads to severe
reduction of the size of the Kupffer's
vesicle. {ECO:0000269|PubMed:23487313}.
CONFLICT 658 658 C -> S (in Ref. 2; AAI71654).
{ECO:0000305}.
SEQUENCE 1485 AA; 168400 MW; 62601EBC307A3B8A CRC64;
MQRSPVEDAN CLSRYFFWWT NPIMRKGFKE KLRPSDVYQA PSQDAADILA ERLEKEWDRE
VASGKKKPSL LRAMARCYIK PFLLFGFLLY IGEATKTVQP QLLGRIIASF DPAHEPERAN
GYFLAFGLGL LFTARFLLLQ PAMFGLHHLG MQIRIALFSI IYKKTLKLSS RVLDKISTGQ
LVSLMSANLG KFDQSLGMAH FIWISPLQCI LCTGLIWELI DVNSFCALAA ISLLGVLQAF
LSHKMGPYKA QKVLLTNKRL ALTSEIMENL HSVKAYGWEE IMETLIKNIR QDEVKLTRKI
GSLRYFYSSA YFFSAIFVIV AAVVPHALSR GINLRRIFTT LSYCMVLRMT VTRQLPGSIQ
MWYDTMRLIW KIEEFLSKEE YKLMEYDLSI TELELQDVTA SWDEGPGELL ERIKQENKAN
GHHNGDAGLF FTNLYVAPVL KDISLKLKKG EMLAVTGSMG SGKSSLLMTI LGELVPSSGK
IRHSGRISYS SQTAWIMPGT IRDNILFGLT YDEYRYKSVV KACQLEEDLA ALPEKDKTPM
AEGGLNLSGG QKARVALARA VYRDADLYLL DAPFTHLDIA TEKEIFDKCL CKLMASKTRI
LVTNKIEHLK RADKILLLHN GESFFYGTFP ELQSERPDFS SLLLGLEAYD NISAERRCSI
LTETLHRVSV DESAGMQPER SAFRQVPPTK PMYIDERKAS VIVNPLGVAR KASFIQVPEE
EVRRTLPDRK FSLVPENELV DESFMGSDVY HNHGVHMAGQ RRQSVLAFMT NAQGQGRREH
LQSSFRRRLS VVPQSELASE LDIYTRRLSD STYDMTGILE EENIEACLTD EIDEIEETFE
TTKWNTYVRY VSNNKSLLYV LIFILFIAAI EIAGSVAGIF LITDELWREE HQRSEPNMTK
HSNASSSGQT YAITVTPTSS YYILYIYVAT SESLLAMGFF RGLPFVHTTI TISKKLHQKM
LHAVLSAPMS VLNTMKTGRI MNRFTKDMAT IDDMLPLLMF DFVQLTVVVV GCILVVSIVR
PYIFLAATPL AIIFIVMRKY FLRTGQQLKQ LETEARSPIF SHLIMSLKGL WTIRAFERQA
YFEALFHKTL NTHTATWFLY LSTLRWFLFR ADILFVFFFT LAAWIAVGTN QDKPGEIGII
ICLAMLILGT FQWCVATSIA VDGMMRSVDR VFKFIDLPSE TPKPDKGKDS DLIIENVDAQ
ADSSWPHRGQ IEVRNLTVKY TEAGHAVLKN LSFSAEGRQR VGILGRTGSG KSSLFNALLK
LVYTDGEISI DGVNWNKMPL QKWRKAFGVV PQKVFIFTGP LRMNLDPYGC HSDEELWRVA
EEVGLKTVIE QFPDKLDFQL EYGGYVLSNG HKQLICLARS ILSGARILLL DEPSAHLDPV
TIKVLKKTLR QSFSTCTILL SEHKVEPLLE CQSFLMMDKG QVKTYDSIQK LLNETSHLKQ
AISPAERLKL FPRRNSSMRT PQSKLSSVTQ TLQEEAEDNI QDTRL


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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
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
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-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-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-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-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-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-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-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-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
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-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-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
EH2805 Cystic Fibrosis Transmembrane Conductance Regulator Elisa Kit 96T
Y108236 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 100ug
Y102989 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
Y102988 Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) 200ug
Y050516 Anti_CFTR(Cystic fibrosis transmembrane conductance regulator) 100ug


 

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