ID A0A2R9C0G7_PANPA Unreviewed; 1480 AA.
AC A0A2R9C0G7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSPPAP00000035402.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000035402.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000035402.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000035402.1}
RP IDENTIFICATION.
RG Ensembl;
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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. 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 EMBL; AJFE02025908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02025909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02025910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02025911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02025912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02025913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003808695.1; XM_003808647.1.
DR SMR; A0A2R9C0G7; -.
DR STRING; 9597.ENSPPAP00000035402; -.
DR Ensembl; ENSPPAT00000058290.1; ENSPPAP00000035402.1; ENSPPAG00000040492.1.
DR KEGG; pps:100989405; -.
DR GeneTree; ENSGT00940000158567; -.
DR OrthoDB; 3384185at2759; -.
DR Proteomes; UP000240080; Chromosome 7.
DR Bgee; ENSPPAG00000040492; Expressed in liver and 3 other cell types or tissues.
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:0097186; P:amelogenesis; 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: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: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 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 Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362037};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362037}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU362037};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 119..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 859..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 903..927
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 986..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 1105..1123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT TRANSMEM 1129..1147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362037"
FT DOMAIN 86..323
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 423..646
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 860..1155
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 1210..1443
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1452..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 168221 MW; 5A2B514B685CD195 CRC64;
MQRSPLEKAS VVSKLFFSWT RPILRKGYRQ RLELSDIYQI PSVDSADNLS EKLEREWDRE
LASKKNPKLI NALRRCFFWR FMFYGIFLYL GEVTKAVQPL LLGRIIASYD PDNKEERSIA
IYLGIGLCLL FIVRTLLLHP AIFGLHHIGM QMRIAMFSLI YKKTLKLSSR VLDKISIGQL
VSLLSNNLNK FDEGLALAHF VWIAPLQVAL LMGLIWELLQ ASAFCGLGFL IVLALFQAGL
GRMMMKYRDQ RAGKISERLV ITSEMIENIQ SVKAYCWEEA MEKMIENLRQ TELKLTRKAA
YVRYFNSSAF FFSGFFVVFL SVLPYALIKG IILRKIFTTI SFCIVLRMAV TRQFPWAVQT
WYDSLGAINK IQDFLQKQEY KTLEYNLTTT EVVMENVTAF WEEGFGELFE KAKQNNNNRK
TSNGDDSLFF SNFSLLGTPV LKDINFKIER GQLLAVAGST GAGKTSLLMM IMGELEPSEG
KIKHSGRISF CSQFSWIMPG TIKENIIFGV SYDEYRYRSV IKACQLEEDI SKFAEKDNIV
LGEGGITLSG GQRARISLAR AVYKDADLYL LDSPFGYLDV LTEKEIFESC VCKLMANKTR
ILVTSKMEHL KKADKILILH EGSSYFYGTF SELQNLRPDF SSKLMGCDSF DQFSAERRNS
ILTETLRRFS LEGDAPVSWT ETKKQSFKQT GEFGEKRKNS ILNPINSIRK FSIVQKTPLQ
MNGIEEDSDE PLERRLSLVP DSEQGEAILP RISVISTGPT LQARRRQSVL NLMTHSVNQG
QNIHRKTTAS TRKVSLAPQA NLTELDIYSR RLSQETGLEI SEEINEEDLK ECFFDDMESI
PAVTTWNTYL RYITVHKSLI FVLIWCLVIF LAEVAASLVV LWLLGNTPLQ DKGNSTHSRN
NSYAVIITST SSYYVFYIYV GVADTLLAMG FFRGLPLVHT LITVSKILHH KMLHSVLQAP
MSTLNTLKAG GILNRFSKDI AILDDLLPLT IFDFIQLLLI VIGAIAVVAV LQPYIFVATV
PVIVAFIMLR AYFLQTSQQL KQLESEGRSP IFTHLVTSLK GLWTLRAFGR QPYFETLFHK
ALNLHTANWF LYLSTLRWFQ MRIEMIFVIF FIAVTFISIL TTGEGEGRVG IILTLAMNIM
STLQWAVNSS IDVDSLMRSV SRVFKFIDMP TEGKPTKSTK PYKNGQLSKV MIIENSHVKK
DDIWPSGGQM TVKDLTAKYT EGGNAILENI SFSISPGQRV GLLGRTGSGK STLLSAFLRL
LNTEGEIQID GVSWDSITLQ QWRKAFGVIP QKVFIFSGTF RKNLDPYEQW SDQEIWKVAD
EVGLRSVIEQ FPGKLDFVLV DGGCVLSHGH KQLMCLARSV LSKAKILLLD EPSAHLDPVT
YQIIRRTLKQ AFADCTVILC EHRIEAMLEC QQFLVIEENK VRQYDSIQKL LNERSLFRQA
ISPSDRVKLF PHRNSSKCKS KPQIAALKEE TEEEVQDTRL
//
