ID A0A2D0QUE4_ICTPU Unreviewed; 1479 AA.
AC A0A2D0QUE4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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|RefSeq:XP_017321934.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017321934.1};
RN [1] {ECO:0000313|RefSeq:XP_017321934.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017321934.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_017321934.1; XM_017466445.3.
DR STRING; 7998.ENSIPUP00000034476; -.
DR Ensembl; ENSIPUT00000035827; ENSIPUP00000034476; ENSIPUG00000023141.
DR GeneID; 108264684; -.
DR KEGG; ipu:108264684; -.
DR CTD; 1080; -.
DR OMA; TEVMMEN; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000221080; Chromosome 4.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-UniRule.
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:0005260; F:intracellularly ATP-gated chloride channel activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
DR GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0070121; P:Kupffer's vesicle development; IEA:Ensembl.
DR GO; GO:0097535; P:lymphoid lineage cell migration into thymus; IEA:Ensembl.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IEA:Ensembl.
DR GO; GO:0060063; P:Spemann organizer formation at the embryonic shield; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
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; IPR025837; CFTR_reg_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01271; CFTR_protein; 1.
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 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}; 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 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 851..876
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 913..932
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 987..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 1014..1033
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 1099..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 1131..1153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
SQ SEQUENCE 1479 AA; 168295 MW; C3F594B0DBEE64B0 CRC64;
MQRSPVDDAG FLSRYFFWWT SPIMRKGFRK KLKTSDVYQT PSQDAADVLA ERLEKEWDRE
VISAKKKPSL LRALSRCFIR PFILFGILLY LGEATKTVQP QLLGRIIASF DPCHEPEREQ
GYFLALGLGL LFITRFLLLQ PAMFGLHHLG MQIRIALFSL IYKKTLKLSS RVLDKISTGQ
LVSLMSANLG KFDQSLGMAH FVWISPLQCI LCVGLIWELI EFNSFCALAA VSLLGVIQAC
LSHKMGPYQA KRLLLTNKRL ALTSEIMENL HSVKAYGWEE IMETIIKNIR QDEVKLTRKI
GSLRYFYSSA YFFSAIWVIM AAVLPQALTT NITVRRIFTT LSYCMVLRMT VTRQLPASIQ
MWYDTIRLIW KIEDFLSKEE YKLMEYDLSI TDMELENITA SWDEGIGELF EKIKQENKAN
GYPNGDGLFF TNLYVTPVLR NISLHLEKGE MLAVAGSTGS GKSSLLMTIL GELVPSSGKI
RHSGRVSYSS QTAWIMPGTI RDNILFGLIY EEYRYSRVVK ACQLEEDLAA LPENDRTPLA
EGGLNLSGGQ KARVALARAV YRDADTYLLD APFTHLDIAT EKEIFEKCLC RLMASKTRIV
VTNKIEHLKR ADKILLLHNG ECFFYGVFSE LQSRRPDFSS LLLGLEAYDN ITAERRCSIL
TETLRRVSVD ETSGIRPDRP SYRQVAPPTY IDERKASVVI NPLAADRKAS FIQVIEEEAK
RPLPDRKFSL VPDYELVDES FMGNDVYHNH GVHMAGQRRQ SVLAFMTNTQ GRRDQLQSSF
HSRLSIVPHS ELTSELDIYT RRLSKDSIYN ITGEMDEENI EACFADKQIE DAFETTTWNT
YLRYVSTNKS LTYVLIFILI IYAIEVAGSV VGIFLITDEI WKEENPGSNA TKQTNISLTG
TQYSVIARPS SSYYIIYIYV ATSESILALG FFRGLPLVHT MITISKKLHQ KMLSSVLRAP
MSVLNTMKTG RIMNRFTKDM ATIDDMLPLL MFDLIQLTLV VLGCILVVSI MRPYIFLAAT
PLAIVFIVMR KYFLRTGQQL KQMETEARSP IFSHLIISLK GLWTIRAFDR QAYFETLFHK
VLNTHTSIWF LYLSTLRWFL FRADIIYFFF FTLAAWIAVG TNQDKSGEIG IIIALAMLIL
GTFQWCVVTS IAVDGMMRSV ERVFKFIDLP SEEPKPRLGQ RKASTLVIEN PEACTDTCWP
SHGQMDIRNL TVKYTEAGHA VLKNLSFSVE GGQKVGILGR TGSGKSTLFN ALLRLAYTDG
DMSIDGVSCY NMSLQKWRKA FGVVPQKVFI FTGTFRLNLD PCGCHSDKEL WRVVEEVGLK
SVIEQFPDKL DFQLEYGGHV LSYGHKQLMC LARSILSRAR ILLLDEPSAH LDPITVKVLK
KTLRQSFSSC TILLCEHKVE PLLECQCFLM MEQGKVKTYE SIQRLLNETS QLKQAMSPAE
RLKLFPRRNS SMRVPQPKLS SVTLTLQEET EDDIQDTRL
//
