ID   G1N9K2_MELGA            Unreviewed;      1403 AA.
AC   G1N9K2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   12-AUG-2020, entry version 72.
DE   RecName: Full=Cystic fibrosis transmembrane conductance regulator {ECO:0000256|RuleBase:RU362037};
DE            EC=5.6.1.6 {ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=ATP-binding cassette sub-family C member 7 {ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=Channel conductance-controlling ATPase {ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=cAMP-dependent chloride channel {ECO:0000256|RuleBase:RU362037};
GN   Name=CFTR {ECO:0000313|Ensembl:ENSMGAP00000009096};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000009096, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000009096, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000009096}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
CC   -!- FUNCTION: Epithelial ion channel that plays an important role in the
CC       regulation of epithelial ion and water transport and fluid homeostasis.
CC       Mediates the transport of chloride ions across the cell membrane.
CC       Channel activity is coupled to ATP hydrolysis. The ion channel is also
CC       permeable to HCO(3-); selectivity depends on the extracellular chloride
CC       concentration. Exerts its function also by modulating the activity of
CC       other ion channels and transporters. Contributes to the regulation of
CC       the pH and the ion content of the epithelial fluid layer.
CC       {ECO:0000256|RuleBase:RU362037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + closed Cl(-) channel = ADP + phosphate + open
CC         Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000256|ARBA:ARBA00001728,
CC         ECO:0000256|RuleBase:RU362037};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362037}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|RuleBase:RU362037}. Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004520}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Recycling endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004195}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       CFTR transporter (TC 3.A.1.202) subfamily.
CC       {ECO:0000256|ARBA:ARBA00009118, ECO:0000256|RuleBase:RU362037}.
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DR   Ensembl; ENSMGAT00000009910; ENSMGAP00000009096; ENSMGAG00000008826.
DR   GeneTree; ENSGT00940000158567; -.
DR   HOGENOM; CLU_000604_27_1_1; -.
DR   InParanoid; G1N9K2; -.
DR   OMA; YWPNRGQ; -.
DR   TreeFam; TF105200; -.
DR   Proteomes; UP000001645; Chromosome 1.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:Ensembl.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0019869; F:chloride channel inhibitor activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0005260; F:intracellularly ATP-gated chloride channel activity; IEA:UniProtKB-EC.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR   GO; GO:0106138; F:Sec61 translocon complex binding; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:1904322; P:cellular response to forskolin; IEA:Ensembl.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR   GO; GO:0051454; P:intracellular pH elevation; IEA:Ensembl.
DR   GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR   GO; GO:0050891; P:multicellular organismal water homeostasis; IEA:Ensembl.
DR   GO; GO:1902161; P:positive regulation of cyclic nucleotide-gated ion channel activity; IEA:Ensembl.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:1902943; P:positive regulation of voltage-gated chloride channel activity; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
DR   GO; GO:0035377; P:transepithelial water transport; IEA:Ensembl.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:Ensembl.
DR   Gene3D; 1.20.1560.10; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR009147; CFTR/ABCC7.
DR   InterPro; IPR025837; CFTR_reg_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24223:SF19; PTHR24223:SF19; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF14396; CFTR_R; 1.
DR   PRINTS; PR01851; CYSFIBREGLTR.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF90123; SSF90123; 2.
DR   TIGRFAMs; TIGR01271; CFTR_protein; 1.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|RuleBase:RU362037};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU362037};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173,
KW   ECO:0000256|RuleBase:RU362037};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU362037};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362037}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362037};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|RuleBase:RU362037};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW   ECO:0000256|RuleBase:RU362037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362037};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362037}; Transport {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        106..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        209..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        849..874
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        906..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        945..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        976..998
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        1004..1023
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        1095..1113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   DOMAIN          73..310
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          410..633
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          850..1145
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1198..1403
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   NP_BIND         445..452
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
FT   NP_BIND         1232..1239
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   1403 AA;  158740 MW;  29C3D4D883E3FD0D CRC64;
     FFFRWTKPIL KKGYRQRLEL SDIYQIPSAD SADNLSEKLE REWDRELATS KKKPKLINAL
     RRCFFWKFMF YGILLYLGEV TKSVQPLLLG RIIASYDPDN FSERSIAYYL GIGLCLLFLV
     RTLLIHPSIF GLHHIGMQIR IALFSLIYKK TLKLSSKVLD KISTGQLVSL LSNNLNKFDE
     GLALAHFVWI APLQVALLMG LLWDMLQASA FAGLAFLIVM AFFQAWLGQM MMKYRDRRAG
     KINERLVITS EIIENIQSVK AYCWEDAMEK MIESLRETEL KLTRKAAYVR YFNSSAFFFS
     GFFVVFLAVV PYAVTKGIIL RKIFTTISFC IVLRMTVTRQ FPGSVQTWYD SIGAINKIQD
     FLLKEEYKAL EYNLTTTGVE VDKVTAFWDE GIGELFVKAK QENNNSKAPS NDNNLFFSNF
     PLHASPVLQD INFKIEKGEL LAVSGSTGSG KTSLLMLIMG ELEPSQGKIK HSGRISFSPQ
     VSWIMPGTIK ENIIFGVSYD EYRYKSVIQA CQLEEDILKF PDKDYTVLGE GGIILSGGQR
     ARISLARAVY KDADLYLMDS PFGYLDIFTE KEIFESCVCK LMANKTRILV TSKLEHLKIA
     DKILILHEGS CYFYGTFSEL QGQRPDFSSE LMGFDSFDQF SAERRNSIIT ETLRRFSFEG
     ESMGSRNEIK KQSFKQTSDF NDKRKNSIII NPLNAGRKLS IMQKNGTQVN GLEDGHVDPS
     ERRISLVPDL EQGDVGLPRS NMLNSDHMLQ SRRRQSVLSL MTGTSVNQGP HVSKKGSTTF
     RKMSMVPQTN LSSEIDIYTR RLSRDSILDI TDEINEDDLK ECFTDDAESM GTVTTWNTYF
     RYITIHKSLI FVLILCVIIF LLEVAASLVL LLFLQKAAKI NETQPENATS DSPPVIITDT
     SSYYMIYIYV GIADTLLAMG IFRGLPLVHT LITVSKTLHQ KMVHAVLYAP MSAFNSLKAG
     GILNRFSKDT AILDDLLPLT VFDLIQLILI VIGAITVVSI LQPYIFLASV PVIAAFIVLR
     AYFLHTSQQL KQLESEARSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK ALNLHTANWF
     LYLSTLRWFQ MRIEMIFVVF FSAVAFISII TTGDGPGRVG IILTLAMNIM GTLQWAVNSS
     IDVDSLMRSV SRIFKFIDMP TEEMKTIKPQ KNNQFSDALV IENRHVKDEK NWPSGGQMTV
     TDLTARYTEG GTAVLENISF SISSGQTVGL LGRTGSGKST LLFAFLRLLN TEGDIRIDGI
     SWNTVSLQQW RKAFGVIPQK VFIFSGTFRK NLDPYGQWND EEIWKVAEEV GLKSVIEQFP
     GQLDFVLVDG GCVLSHGHKQ LMCLARSVLS KAKILLLDEP SAHLDPITSQ VIRKTLKHAF
     ADCTVILSEH RLEAILECQR FLV
//