ID G1N9K2_MELGA Unreviewed; 1518 AA.
AC G1N9K2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 28-JUN-2023, entry version 84.
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:ENSMGAP00000009096.3};
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:ENSMGAP00000009096.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000009096.3, 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:ENSMGAP00000009096.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) 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 + H2O + closed Cl(-) channel = ADP + phosphate + open
CC Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000256|ARBA:ARBA00034073,
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. 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 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: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-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; 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:0051087; F:protein-folding chaperone 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:0051649; P:establishment of localization in cell; 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-level 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 CDD; cd18594; ABC_6TM_CFTR_D1; 1.
DR CDD; cd18600; ABC_6TM_CFTR_D2; 1.
DR CDD; cd03291; ABCC_CFTR1; 1.
DR CDD; cd03289; ABCC_CFTR2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047082; CFTR1_ATP-bd_dom1.
DR InterPro; IPR025837; CFTR_reg_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF19; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; 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; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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,
KW 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 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 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
//