The following text describes a protein:
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 (By similarity). Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (By similarity). 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 (By similarity).
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus. 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.
Domain:
Binds and hydrolyzes ATP via the two cytoplasmic ABC transporter nucleotide-binding domains. The two ATP-binding domains interact with each other, forming a head-to-tail dimer. Normal ATPase activity requires interaction between the two domains. The first ABC transporter nucleotide-binding domain has no ATPase activity by itself; The PDZ-binding motif mediates interactions with GOPC and with the SLC4A7, NHERF1/EBP50 complex; The disordered R region mediates channel activation when it is phosphorylated, but not in the absence of phosphorylation.
Sequence:
MQKSPLVKASVISKLFFSWTRPILKKGYRKRLEVSDIYQVPSADSADNLSEELEREWDRELASKKNPKLINALRRCFLWRFIFYGILLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLAIGLCLLFIVRTLLLHPAIFGLQHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQASAFCGLAVLIVLALFQAWLGKMMMKYRDQRAGKINERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYMRYFNSAAFFFSGFFVVFLSVLPYAFLQGIILRKIFTTISFCIVLRMAITRQFPGAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEQGFGELLEKAKLNNNNRKISNGDNKLFFSNFSLLGSPVLKDINFKIEKGQLLAVAGSTGAGKTSLLMMILGELEPSEGKIKHSGRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKQIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLRPDFSSKLMGYDSFDQFSAERRNSILTETLRRFSLEGDPSVSFNETKKQSFKQTGEFGEKRKNSILNSINSIRKFSIVPKTPLQISGIEEDSDDPVERRLSLVPDSEQSDGLLLRSNVIHTGPTFQGSRRQSVLNLITHSVNQGQSFRRTTTAPSRKMSLAPQASLTEMDIYSRRLSQDSSLEINEEINEEDLKECFFDDVENIPTVTTWNTYLRYITVHKSLILVLIWCLIIFLAEVAASLVVLWLLKNNTPQQEMNSTQSGNRSYPVIITNTSFYYIFYIYVGVADTLLALGLFRGLPLVHTLITVSKILHHKMLRSVLQAPMSTLNALKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVSVLQPYIFLATVPVIAAFIMLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGQGSVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPEEGAPVKSIKPSRDDQLSKVMIIENQHVKKDDIWPSGGQMIVKDLTAKYVDGGIAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSTPLQQWRKAFGVIPQKVFIFSGTFRKNLDPFGQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGYVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQIIRRTIKQAFADCTVILCEHRIEAMLECQRFLVIEENKVRQYDSIQKLLSEKSLFRQAISSSDRLKLFPHRNSSKHKSRSQITALKEETEEEVQETRL