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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_MUSPF              Reviewed;        1484 AA.
Q07E16;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 1.
25-OCT-2017, entry version 78.
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;
Mustela putorius furo (European domestic ferret) (Mustela furo).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae;
Mustelinae; Mustela.
NCBI_TaxID=9669;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J.,
Hansen N., Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P.,
Laric P., Larson S., Lee-Lin S.-Q., Legaspi R., Madden M.,
Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C., Maskeri B.,
McDowell J., Mojidi H.A., Mullikin J.C., Oestreicher J.S., Park M.,
Portnoy M.E., Prasad A., Puri O., Reddix-Dugue N., Schandler K.,
Schueler M.G., Sison C., Stantripop S., Stephen E., Taye A.,
Thomas J.W., Thomas P.J., Tsipouri V., Ung L., Vogt J.L.,
Wetherby K.D., Young A., Green E.D.;
"NISC comparative sequencing initiative.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Epithelial ion channel that plays an important role in
the regulation of epithelial ion and water transport and fluid
homeostasis. 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. 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 (By similarity).
{ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
-!- 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 (By similarity).
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 (By similarity). Interacts
with CSE1L (By similarity). {ECO:0000250|UniProtKB:P13569,
ECO:0000250|UniProtKB:P26361, ECO:0000250|UniProtKB:P34158}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:P26361}; 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:0000250|UniProtKB:P26361}; 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}.
-!- 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 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}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
family. CFTR transporter (TC 3.A.1.202) subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DP000183; ABI93660.1; -; Genomic_DNA.
RefSeq; XP_004741961.1; XM_004741904.2.
ProteinModelPortal; Q07E16; -.
STRING; 9669.ENSMPUP00000007081; -.
Ensembl; ENSMPUT00000007199; ENSMPUP00000007081; ENSMPUG00000007138.
GeneID; 101672484; -.
CTD; 1080; -.
eggNOG; KOG0054; Eukaryota.
eggNOG; COG1132; LUCA.
GeneTree; ENSGT00900000140905; -.
HOVERGEN; HBG004169; -.
InParanoid; Q07E16; -.
OMA; LAHFVWI; -.
OrthoDB; EOG091G00K4; -.
Proteomes; UP000000715; Unassembled WGS sequence.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C: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; ISS:UniProtKB.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
GO; GO:0015106; F:bicarbonate transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
GO; GO:0019869; F:chloride channel inhibitor activity; ISS:UniProtKB.
GO; GO:0015108; F:chloride transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0005260; F:intracellular ATPase-gated chloride channel activity; ISS:UniProtKB.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0015701; P:bicarbonate transport; ISS:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; ISS: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:0050891; P:multicellular organismal water homeostasis; ISS:UniProtKB.
GO; GO:1902161; P:positive regulation of cyclic nucleotide-gated ion channel activity; IEA:Ensembl.
GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IEA:Ensembl.
GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:Ensembl.
Gene3D; 1.20.1560.10; -; 2.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR011527; ABC1_TM_dom.
InterPro; IPR036640; ABC1_TM_sf.
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:SF19; PTHR24223:SF19; 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.
3: Inferred from homology;
ATP-binding; Cell membrane; Chloride; Chloride channel;
Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein;
Hydrolase; Ion channel; Ion transport; Isopeptide bond; Lipoprotein;
Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 1484 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000260778.
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 359 860 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 861 881 Helical; Name=7.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 882 920 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 921 941 Discontinuously helical; Name=8.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 942 992 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 993 1013 Helical; Name=9.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1014 1015 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1016 1036 Helical; Name=10.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1037 1097 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1098 1118 Helical; Name=11.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1119 1132 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1133 1153 Helical; Name=12.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1154 1484 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 861 1157 ABC transmembrane type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00441}.
DOMAIN 1214 1447 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 458 465 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1248 1255 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 654 833 Intrinsically disordered R region.
{ECO:0000250|UniProtKB:P13569}.
MOTIF 1482 1484 PDZ-binding.
{ECO:0000250|UniProtKB:P13569}.
BINDING 401 401 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 434 434 ATP 1. {ECO:0000250|UniProtKB:P13569}.
BINDING 493 493 ATP 1. {ECO:0000250|UniProtKB:P26361}.
BINDING 1223 1223 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 686 686 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 700 700 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 712 712 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 717 717 Phosphothreonine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 792 792 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 797 797 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1448 1448 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 524 524 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 1399 1399 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
CARBOHYD 896 896 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 902 902 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 688 688 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P13569}.
SEQUENCE 1484 AA; 168516 MW; 809E7AA514D45224 CRC64;
MQRSPLEKAS VLSKLFFSWT RPILTKGYRQ RLELSDIYQI PSADSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGIILYL GEVTKSVQPL LLGRIIASYD PDNKEERSIA
IYLGIGLCLL FVMRTLLLHP AIFGLHRIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVTL LMGLLWDLLQ ASAFCGLAFL IVLALFQAGL
GRMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKMIESIRQ TELKLTRKAA
YVRYFNSSAF FFSGFFVVFL SVLPYALIKT IVLRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELLE KAKQNSNDRK
ISNADNSLFF SNFSLLGAPV LKDISFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSCYFYGTF SELQNLRPDF SSKLMGYDSF DQFSAERRNS
IITETLRRFS LEGDAPVSWN ETKKQSFKQT GEFGEKRKNS ILNPVNSIRK FSVVQKTPLQ
MNGIEEDSDE PLERRLSLVP DGAEQGEAIL PRSNMINTGP TLQRQRRQSV LNLMTCSPGN
QGQSFHGRTA SSTRKMSLAP QANLTEMDIY SRRLSQDSGL EISEEINEED LKECFIDDVE
SIPPVTTWNT YLRYVTIHKS LVFVLIWCLV IFLAEVAISL VVLWLLKKTA SQDKGNSTQS
INSSYTVIFT STSTYYVFYI YVGVADTLLA LGFFRGLPLV HTLITVSKIL HHKMLHAVLQ
APMSTLNALK AGGILNRFSK DIAILDDLLP LTIFDFVQLL LIVIGAVTVV SALQPYIFLA
TVPVIAAFIM LRAYFLHTSQ QLKQLESEGR SPIFTHLVTS LKGLWTLRAF GRQPYFETLF
HKALNLHTAN WFLYLSTLRW FQMRMEIIFV IFFIAITFIS ILTTGEGVGA VGIILTLAMN
IMGTLQWAVN SSIDVDSLMR SVSRVFKFID MPAEESKPPT KSFKPSKDVQ LSKVLITENH
HVREDDIWPS GGQMTVKDLT AKYIDGGNAI LENISFSISP GQRVGLLGRT GSGKSTLLSA
FLRLLNTEGE IQIDGVSWDS ITLQEWRKAF GVIPQKVFIF SGTFRKNLDP YGQWNDQEIW
KVADEVGLRS VIEQFPGKLD FVLVDGGCVL SHGHKQLMCL ARSVLSKAKI LLLDEPSAHL
DPITYQIIRR TLKQAFADCT VILSEHRIEA MLECQRFLVI EENKVRQYDS LQRLLSEKSL
FRQAISPSDR LRFFPHRNSS KHKSRSQIAA LKEETEEEVQ ETRL


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