Cftr
entrez
24255
canonical
uniprot
P34158
canonical
ensembl
ENSRNOG00000055103
resolver
ensp
ENSRNOP00000072565
resolver
ensp
ENSRNOP00000094868
resolver
enst
ENSRNOT00000085043
resolver
genesymbol
Cftr
resolver
genesymbol_syn
Abcc7
resolver
uniprot
A0A0G2K3B1
resolver
uniprot
Q2IBD3
resolver
uniprot_entry
A0A0G2K3B1_RAT
resolver
uniprot_entry
CFTR_RAT
resolver
uniprot_sec
Q2IBD3
resolver
amino_acid_sequence
MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQASKKKPQLIHALRRCFVWRFVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKIQDFLQTQEYKVLEYNLMFTGLVMENVTAFWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEFGEKRKNSILSSFSSVKKISIVQKTPLSIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLAPRISLKEEDIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESICTKIMKELHSEDSPNALVIKNEHVKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKMKLFHGRHSSKQKPRTQITAVKEETEEEVQETRL
uniprot
proteins
ec_number
5.6.1.6
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P13569, ECO:0000250|UniProtKB:P26361}.
uniprot
proteins
mass_dalton
167830
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13569}.; PTM: Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel. Dephosphorylation decreases the ATPase activity (in vitro). Phosphorylation at PKA sites activates the channel. Phosphorylation at PKC sites enhances the response to phosphorylation by PKA. Phosphorylated by AMPK; this inhibits channel activity. {ECO:0000250|UniProtKB:P13569}.; PTM: Ubiquitinated, leading to its degradation in the lysosome. Deubiquitination by USP10 in early endosomes enhances its endocytic recycling to the cell membrane. Ubiquitinated by RNF185 during ER stress. Ubiquitinated by MARCHF2 (By similarity). {ECO:0000250|UniProtKB:P13569}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCC family
uniprot
proteins
protein_family
CFTR transporter (TC 3.A.1.202) subfamily
uniprot
proteins
pubmed
11707463
uniprot
proteins
pubmed
12519745
uniprot
proteins
pubmed
1282491
uniprot
proteins
pubmed
12917688
uniprot
proteins
pubmed
14679199
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
29453757
uniprot
proteins
pubmed
30659401
uniprot
proteins
pubmed
7526924
uniprot
proteins
sequence_length
1476
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P26361}; 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:0000250|UniProtKB:P26361}; 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:0000269|PubMed:29453757}. Note=The channel is internalized from the cell surface into an endosomal recycling compartment, from where it is recycled to the cell membrane (By similarity). In the oviduct and bronchus, detected on the apical side of epithelial cells, but not associated with cilia (By similarity). In Sertoli cells, a processed product is detected in the nucleus (PubMed:29453757). ER stress induces GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (By similarity). {ECO:0000250|UniProtKB:P13569, ECO:0000269|PubMed:29453757}.
uniprot
proteins
transmembrane_region
TRANSMEM 78..98; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 123..146; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 196..216; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 223..243; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 299..319; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 340..358; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 854..874; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 914..934; /note="Discontinuously helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 986..1006; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 1009..1029; /note="Helical; Name=10"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 1091..1111; /note="Helical; Name=11"; /evidence="ECO:0000250|UniProtKB:P13569"; TRANSMEM 1126..1146; /note="Helical; Name=12"; /evidence="ECO:0000250|UniProtKB:P13569
uniprot
proteins