Protein Details: Cystic fibrosis transmembrane conductance regulator

Protein ID

ICDB_Pro_1015

Protein Name

Cystic fibrosis transmembrane conductance regulator

Gene Name

CFTR; ABCC7

Organism

Canis lupus familiaris (Dog) (Canis familiaris)

Length

1483 amino acids

AlphaFoldDB

AF-Q5U820-F1-model_v4.pdb

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). 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 (By similarity).

Sequence

MQRSPLEKASVLSKLFFSWTRPILIKGYRQRLELSDIYQVPSTDSADHLSEKLEREWDRELASKKNPKLINALRRCFFWRFAFYGILLYLGEVTKAVQPLLLGRIIASYDPDNKQERSIAIYLAIGLCLLFIMRPLLLHPAIFGLHHIGMQIRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVTLLMGLLWDLLQASAFCGLAFLIVLALVQAGLGRMIMKYRDQRAGKINERLVITSEVIENIQSVKAYCWEEAMEKIIENIRQTELKLTRKAAHVRYFNSSAFFFSGFFVVSLSVLPYALIKTIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVMMENVTAFWEEGFGELLEKAKENSNDRKISNGDNSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKVLILHEGSCYFYGTFSELQSLRPDFSSKLMGYDSFDQFSPERRNSIITETLRRFSLEGDAAVPWNETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLPMNGIEGESEVPVERRLSLFPDCEQGEAILPRSNMINTGPTLRRQRRQSVLNLMTRSSVNQGQSIHRRTTASTRKMSLAPQANLTEMDIYSRRLSQDSGLEISEEINEEDLKECFFDDVESIPPVTTWNTYLRYITVHKNLIFVLIWCLVIFLAEVAVSLVVLWILRNLSSQDKGNSTQSVNSSYAVIFTSTSAYYIFYIYVGVADTLLALGLFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAVAVVSVLQPYIFLATVPVIAAFIILRAYFLHTSQQLKQLESEGRSPIFTHLLTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRMEIIFVIFFIAVTFISILTTGEGEGTVGIILTLAMNIMGTLQWAVNSSIEVDSLMRSVSRVFKFIDMPTEESKPPTKSFKPSKDAQLSKVTITENRHVREDDIWPSGGQMTVKDLTAKYIDGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSALLRLVNTEGEIQIDGVSWDSIPLQEWRRAFGVIPQKVFIFSGTFRKNLDPYGQWNDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGYVLSHGHKQLMCLARSVLRKAKILLLDEPSAHLDPITYQIIRRTLKQAFADCTVILSEHRIEAMLECQRFLVIEDSRLRQFESIQRLLSERSAFRQAIGPPERPGLLPHRLSSRQRSPSRIAALKEETEDEVQDTRL

PDB Structures

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

BINDING 401; /ligand="ATP"; BINDING 434; /ligand="ATP"; BINDING 458..465; /ligand="ATP"; BINDING 493; /ligand="ATP"; BINDING 1222; /ligand="ATP"; BINDING 1247..1254; /ligand="ATP"

Disease

Location

DOI ID

10.1038/nature01858

RefSeq

NP_001007144.1