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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_ATEGE              Reviewed;        1480 AA.
Q09YK5;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
25-OCT-2017, entry version 65.
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;
Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider
monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Atelidae; Atelinae; Ateles.
NCBI_TaxID=9509;
[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; DP000177; ABI75275.1; -; Genomic_DNA.
ProteinModelPortal; Q09YK5; -.
HOVERGEN; HBG004169; -.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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: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:0005260; F:intracellular ATPase-gated chloride channel activity; ISS:UniProtKB.
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: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:0048240; P:sperm capacitation; ISS:UniProtKB.
GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB.
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;
Endoplasmic reticulum; Endosome; Glycoprotein; Hydrolase; Ion channel;
Ion transport; Isopeptide bond; Lipoprotein; Membrane;
Nucleotide-binding; Palmitate; Phosphoprotein; Repeat; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 1480 Cystic fibrosis transmembrane conductance
regulator.
/FTId=PRO_0000260770.
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 359 858 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 859 879 Helical; Name=7.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 880 918 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 919 939 Discontinuously helical; Name=8.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 940 990 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 991 1011 Helical; Name=9.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1012 1013 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1014 1034 Helical; Name=10.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1035 1095 Cytoplasmic.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1096 1116 Helical; Name=11.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1117 1130 Extracellular.
{ECO:0000250|UniProtKB:P13569}.
TRANSMEM 1131 1151 Helical; Name=12.
{ECO:0000250|UniProtKB:P13569}.
TOPO_DOM 1152 1480 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 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:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1244 1251 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 654 831 Intrinsically disordered R region.
{ECO:0000250|UniProtKB:P13569}.
MOTIF 1478 1480 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 1219 1219 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 753 753 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 768 768 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 813 813 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1444 1444 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
MOD_RES 1456 1456 Phosphoserine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 524 524 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
LIPID 1395 1395 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P13569}.
CARBOHYD 894 894 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 900 900 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 909 909 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 1480 AA; 168035 MW; 1ECE0F4FEE7249C7 CRC64;
MQRSPLEKAS VVSKLFFSWT RPILKKGYRQ RLELSDIYQI PSANSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGILLYL GEVTKAVQPL LLGRIIASYD PDNKTERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL
GRMMMKYRDQ RAGKINERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IVLRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNSNNRK
TSNGDDNLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAAKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLRPDF SSKLMGYDSF DQFSSERRNS
ILTETLRRFS LEGDAPVSWT ETKKQSFKQT GELGDKRKNS ILNSINSIRK FSIVQKTPLQ
MNGIEENSDE PLERRLSLVP DSEQGEAILP RISVINTGPA LQLRRRQSVL NMMTHSVNQG
QSVHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDNMESI
PAVTTWNTYL RYITLHKSLI FVLIWCLVIF LAEVAASLVV LWFLGNTPFQ DKGNSTYSRN
NSYAVIITNT SSYYVFYIYV GVADTLLALG FFRGLPLVHT LITVSKILHH KMLHSVLQAP
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVSV LQPYILLATV
PVIAAFILLR AYFLQTSQQL KQLESAGRSP IFTHLVTSLK GLWTIRAFGR QPYFETLFHK
ALNLHTANWF LYLATLRWFQ MRIEIIFVIF FIAVTFISIL TTGEGEGTVG IILTLAMNIM
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK AYKNGQLSKV MIIENSHVKK
NDIWPSGGQM TIKDLTAKYI EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL
LNTEGEIQID GVSWDSITLQ QWRKAFGVIP QKVFIFTGTF RKNLDPYEQW SDQEIWKVAD
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT
YQIIRRALKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNEKSLFQQA
ISHSDRVKLF PHRNSSKYKS PPQIASLKEE TEEEVQETRL


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