Protein: Cystic fibrosis transmembrane conductance regulator (CFTR) (ATP-binding cassette sub-family C member 7) (Channel conductance-controlling ATPase) (EC 5.6.1.6) (cAMP-dependent chloride channel) (P26361)
Organism: Mus musculus (Mouse)
Function: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane. Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3)(-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:21884936}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Early endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Cell membrane {ECO:0000269|PubMed:20231442, ECO:0000269|PubMed:22265409}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Recycling endosome membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P13569}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P13569}. Nucleus {ECO:0000250|UniProtKB:P34158}. Note=The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane. In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia. In Sertoli cells, a processed product is detected in the nucleus. ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936). {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P34158, ECO:0000269|PubMed:21884936}.
Interaction partners:
- Na
- Tight junction protein 1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Solute carrier family 26 member 6
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- Golgi-associated PDZ and coiled-coil motif-containing protein
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit beta-1
Sequence:
MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSADSADHLSEKLEREWDREQASKKNPQLIHALRRCFFWRFLFYGILLYLGEVTKAVQPVLLGRIIASYDPENKVERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHRIGMQMRTAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFIWIAPLQVTLLMGLLWDLLQFSAFCGLGLLIILVIFQAILGKMMVKYRDQRAAKINERLVITSEIIDNIYSVKAYCWESAMEKMIENLREVELKMTRKAAYMRFFTSSAFFFSGFFVVFLSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSFGMIRKIQDFLQKQEYKVLEYNLMTTGIIMENVTAFWEEGFGELLEKVQQSNGDRKHSSDENNVSFSHLCLVGNPVLKNINLNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKMEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDSSAPWSKPKQSFRQTGEVGEKRKNSILNSFSSVRKISIVQKTPLCIDGESDDLQEKRLSLVPDSEQGEAALPRSNMIATGPTFPGRRRQSVLDLMTFTPNSGSSNLQRTRTSIRKISLVPQISLNEVDVYSRRLSQDSTLNITEEINEEDLKECFLDDVIKIPPVTTWNTYLRYFTLHKGLLLVLIWCVLVFLVEVAASLFVLWLLKNNPVNSGNNGTKISNSSYVVIITSTSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTISKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLVFIVIGAIIVVSALQPYIFLATVPGLVVFILLRAYFLHTAQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTAGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESMYTQIIKELPREGSSDVLVIKNEHVKKSDIWPSGGEMVVKDLTVKYMDDGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGDIEIDGVSWNSVTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWKDEEIWKVADEVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAHLDPITYQVIRRVLKQAFAGCTVILCEHRIEAMLDCQRFLVIEESNVWQYDSLQALLSEKSIFQQAISSSEKMRFFQGRHSSKHKPRTQITALKEETEEEVQETRL