ID   G1N9K2_MELGA            Unreviewed;      1403 AA.
AC   G1N9K2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   08-MAY-2019, entry version 64.
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;
OC   Phasianidae; 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.,
RA   de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D.,
RA   Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P.,
RA   Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S.,
RA   Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M.,
RA   Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S.,
RA   Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F.,
RA   Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P.,
RA   Yorke J.A., Zhang L., Zhang H.B., Zhang X., 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
CC       the regulation of epithelial ion and water transport and fluid
CC       homeostasis. Mediates the transport of chloride ions across the
CC       cell membrane. Channel activity is coupled to ATP hydrolysis. The
CC       ion channel is also permeable to HCO(3-); selectivity depends on
CC       the extracellular chloride concentration. Exerts its function also
CC       by modulating the activity of other ion channels and transporters.
CC       Contributes to the regulation of the pH and the ion content of the
CC       epithelial fluid layer. {ECO:0000256|RuleBase:RU362037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(2)O + closed Cl(-) channel = ADP + phosphate +
CC         open Cl(-) channel.; EC=5.6.1.6;
CC         Evidence={ECO:0000256|RuleBase:RU362037};
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362037}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU362037}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
CC       family. CFTR transporter (TC 3.A.1.202) subfamily.
CC       {ECO:0000256|RuleBase:RU362037}.
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DR   Ensembl; ENSMGAT00000009910; ENSMGAP00000009096; ENSMGAG00000008826.
DR   eggNOG; KOG0054; Eukaryota.
DR   eggNOG; COG1132; LUCA.
DR   GeneTree; ENSGT00940000158567; -.
DR   InParanoid; G1N9K2; -.
DR   OMA; RCFFWKF; -.
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:0042626; F:ATPase activity, coupled to transmembrane movement of substances; 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|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|RuleBase:RU362037};
KW   Chloride {ECO:0000256|RuleBase:RU362037};
KW   Chloride channel {ECO:0000256|RuleBase:RU362037};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001645};
KW   Ion channel {ECO:0000256|RuleBase:RU362037};
KW   Ion transport {ECO:0000256|RuleBase:RU362037};
KW   Membrane {ECO:0000256|RuleBase:RU362037};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|RuleBase:RU362037};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU362037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Repeat {ECO:0000256|SAAS:SAAS01162082};
KW   Transmembrane {ECO:0000256|RuleBase:RU362037};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362037};
KW   Transport {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM     59     78       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    106    124       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    182    203       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    209    228       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    291    314       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    849    874       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    906    925       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    945    964       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM    976    998       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM   1004   1023       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   TRANSMEM   1095   1113       Helical. {ECO:0000256|RuleBase:RU362037}.
FT   DOMAIN       73    310       ABC transmembrane type-1.
FT                                {ECO:0000259|PROSITE:PS50929}.
FT   DOMAIN      410    633       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   DOMAIN      850   1145       ABC transmembrane type-1.
FT                                {ECO:0000259|PROSITE:PS50929}.
FT   DOMAIN     1198   1403       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND     445    452       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
FT   NP_BIND    1232   1239       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                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
//