ID   G1N9K2_MELGA            Unreviewed;      1518 AA.
AC   G1N9K2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Cystic fibrosis transmembrane conductance regulator {ECO:0000256|ARBA:ARBA00016668, ECO:0000256|RuleBase:RU362037};
DE            EC=5.6.1.6 {ECO:0000256|ARBA:ARBA00012195, ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=ATP-binding cassette sub-family C member 7 {ECO:0000256|ARBA:ARBA00029720, ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=Channel conductance-controlling ATPase {ECO:0000256|ARBA:ARBA00031358, ECO:0000256|RuleBase:RU362037};
DE   AltName: Full=cAMP-dependent chloride channel {ECO:0000256|ARBA:ARBA00033163, 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; ENSMGAT00000009910.3; ENSMGAP00000009096.3; ENSMGAG00000008826.3.
DR   GeneTree; ENSGT00940000158567; -.
DR   HOGENOM; CLU_000604_27_1_1; -.
DR   InParanoid; G1N9K2; -.
DR   OMA; NIRQEEM; -.
DR   TreeFam; TF105200; -.
DR   Proteomes; UP000001645; Chromosome 1.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
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:0015108; F:chloride transmembrane transporter 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:0070175; P:positive regulation of enamel mineralization; 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   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_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};
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};
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        153..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        229..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        256..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        896..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        954..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        993..1012
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        1024..1046
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        1052..1071
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   TRANSMEM        1143..1161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362037"
FT   DOMAIN          120..357
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          457..680
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          897..1193
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          1246..1479
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   NP_BIND         492..499
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
FT   NP_BIND         1280..1287
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00434"
FT   REGION          1488..1518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1501..1518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1518 AA;  172026 MW;  7A859A9A53B2D047 CRC64;
     MFGIYVCLLF ETTGKTFMCA LATSSLLVLF KENRLLYRSK QMVICLSSYS LWTKPILKKG
     YRQRLELSDI YQIPSADSAD NLSEKLEREW DRELATSKKK PKLINALRRC FFWKFMFYGI
     LLYLGEVTKS VQPLLLGRII ASYDPDNFSE RSIAYYLGIG LCLLFLVRTL LIHPSIFGLH
     HIGMQIRIAL FSLIYKKTLK LSSKVLDKIS TGQLVSLLSN NLNKFDEGLA LAHFVWIAPL
     QVALLMGLLW DMLQASAFAG LAFLIVMAFF QAWLGQMMMK YRDRRAGKIN ERLVITSEII
     ENIQSVKAYC WEDAMEKMIE SLRETELKLT RKAAYVRYFN SSAFFFSGFF VVFLAVVPYA
     VTKGIILRKI FTTISFCIVL RMTVTRQFPG SVQTWYDSIG AINKIQDFLL KEEYKALEYN
     LTTTGVEVDK VTAFWDEGIG ELFVKAKQEN NNSKAPSNDN NLFFSNFPLH ASPVLQDINF
     KIEKGELLAV SGSTGSGKTS LLMLIMGELE PSQGKIKHSG RISFSPQVSW IMPGTIKENI
     IFGVSYDEYR YKSVIQACQL EEDILKFPDK DYTVLGEGGI ILSGGQRARI SLARAVYKDA
     DLYLMDSPFG YLDIFTEKEI FESCVCKLMA NKTRILVTSK LEHLKIADKI LILHEGSCYF
     YGTFSELQGQ RPDFSSELMG FDSFDQFSAE RRNSIITETL RRFSFEGESM GSRNEIKKQS
     FKQTSDFNDK RKNSIIINPL NAGRKLSIMQ KNGTQVNGLE DGHVDPSERR ISLVPDLEQG
     DVGLPRSNML NSDHMLQSRR RQSVLSLMTG TSVNQGPHVS KKGSTTFRKM SMVPQTNLSS
     EIDIYTRRLS RDSILDITDE INEDDLKECF TDDAESMGTV TTWNTYFRYI TIHKSLIFVL
     ILCVIIFLLE VAASLVLLLF LQNRAAKINE TQPENATSDS PPVIITDTSS YYMIYIYVGI
     ADTLLAMGIF RGLPLVHTLI TVSKTLHQKM VHAVLYAPMS AFNSLKAGGI LNRFSKDTAI
     LDDLLPLTVF DLIQLILIVI GAITVVSILQ PYIFLASVPV IAAFIVLRAY FLHTSQQLKQ
     LESEARSPIF THLVTSLKGL WTLRAFGRQP YFETLFHKAL NLHTANWFLY LSTLRWFQMR
     IEMIFVVFFS AVAFISIITT GDGPGRVGII LTLAMNIMGT LQWAVNSSID VDSLMRSVSR
     IFKFIDMPTE EMKTIKPQKN NQFSDALVIE NRHVKDEKNW PSGGQMTVTD LTARYTEGGT
     AVLENISFSI SSGQTVGLLG RTGSGKSTLL FAFLRLLNTE GDIRIDGISW NTVSLQQWRK
     AFGVIPQKVF IFSGTFRKNL DPYGQWNDEE IWKVAEEVGL KSVIEQFPGQ LDFVLVDGGC
     VLSHGHKQLM CLARSVLSKA KILLLDEPSA HLDPITSQVI RKTLKHAFAD CTVILSEHRL
     EAILECQRFL VIEDNKMRQY ESIQKLLSEK SSLRQAISHA DRLKLLPAHR RNSSKRKPRP
     QICALQEETE EEVQETRL
//