ID G1N9K2_MELGA Unreviewed; 1403 AA.
AC G1N9K2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 07-OCT-2020, entry version 73.
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: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: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: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: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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, 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
//