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Search results 1 to 7 out of 7 for Cftr

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: Cystic fibrosis transmembrane conductance regulator (CFTR) that belongs tothe ATP-binding cassette (ABC) transporter superfamily. It is a member of the ABC-C subfamily, which also contains the SUR receptors and the multidrug-resistance associated proteins (MRP) []. The CFTR protein encodes a chloride ion channel, which is controlled by phosphorylation. It has a majorrole in electrolyte and fluid secretion. CFTR is important in the determination of fluid flow, ion concentration and transepithelial salttransport. Dysfunction of the CFTR channel causes the life-threateningdisease, cystic fibrosis, in which trans-epithelial ion transport is disrupted []. This entry represents the CFTR regulator domain [, , ].
Protein Domain
Type: Family
Description: Ubiquitin carboxyl-terminal hydrolase 10 (USP10) isa hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR []. It regulates the localisation and stability of p53 by de-ubiquitinatiing p53 []. It is also implicated in vesicular transport and trafficking of membrane proteins [].
Protein Domain
Type: Family
Description: GOPC, also known as PIST or CAL, is primarily localized to the Golgi apparatus. It binds the G protein-coupled receptor beta1AR and modulates beta1AR intracellular trafficking []. GOPC also interacts with cystic fibrosis transmembrane regulator (CFTR), retains CFTR in the cell and targets it for degradation [].
Protein Domain
Type: Family
Description: The testis anion transporter TAT1 (solute carrier family 26 member 8; SLC26A8) mediates chloride, sulfate and oxalate transport and is specifically expressed in male germ cells and mature sperms [, ]. It is essential for correct sperm tail differentiation and motility, and hence male fertility []. TAT1 and CFTR (cystic fibrosis transmembrane conductance regulator) seem to cooperate in the regulation of the Cl-/HCO3- fluxes required for motility and capacitation of sperm [].
Protein Domain
Type: Family
Description: The ABC transporter family is a group of membrane proteins that use the hydrolysis of ATP to power the translocation of a wide variety of substrates across cellular membranes. ABC transporters minimally consist of two conserved regions: a highly conserved nucleotide-binding domain (NBD) and a less conserved transmembrane domain (TMD). Eukaryotic ABC proteins are usually organised either as full transporters (containing two NBDs and two TMDs), or as half transporters (containing one NBD and one TMD), that have to form homo- or heterodimers in order to constitute a functional protein [].Cystic fibrosis transmembrane conductance regulator (CFTR, also known as ABCC7) is an eukaryotic protein belonging to the ABC-C subfamily of the ABC transporter family. CFTR protein is a chloride ion channel controlled by phosphorylation. It has a major role in electrolyte and fluid secretion. CFTR is important in the determination of fluid flow, ion concentration and transepithelial salttransport. Dysfunction of the CFTR channel causes the life-threateningdisease, cystic fibrosis, in which trans-epithelial ion transport is disrupted []. Defective phosphorylation has been seen to be a cause for this altered activity [].
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase IC (also known as ATP8B1 or ATPIC) belongs to subfamily IV of the P-type ATPases family, whose members transport phospholipids across the membrane. ATP8B1 can bind either CDC50A or CDC50B as its accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity [, , ].In hepatocytes, ATP8B1 localises in the canalicular membrane, where it may maintain the membrane integrity and to the function of ABCB4, an ABC floppase that play a role in bile export []. In the epithelial Caco-2 cells, ATP8B1 is required for apical protein expression and microvillus formation in polarised epithelial cells []. Mutations in ATP8B1 cause two forms of intrahepatic cholestasis, progressive familial intrahepatic cholestasis (PFIC) and benign recurrent intrahepatic cholestasis (BFIC) []. It is involved in the correct apical membrane localization of CDC42, CFTR and SLC10A2 [].
Protein Domain
Type: Family
Description: The DnaJ proteins, also known as heat shock protein 40 (Hsp40 or Hsc40), are proteins originally identified in Escherichia coli that act as cochaperones to the molecular chaperone DnaK (Hsp70), which is responsible for several cellular processes such as rescuing misfolded proteins, folding polypeptide chains, transport of polypeptides through membranes, assembly and disassembly of protein complexes, and control of regulatory proteins [].Structurally, the DnaJ protein consists of an N-terminal conserved domain (called 'J' domain) of about 70 amino acids, a glycine-rich region ('G' domain') of about 30 residues, a central domain containing four repeats of a CXXCXGXG motif ('CRR' domain) and a C-terminal region of 120 to 170 residues.This entry represents a group of DnaJ domain containing proteins, including DNJA1/2/4 from humans, Scj1/Mas5/Xdj1/Apj1 from budding yeasts, and DNAJ2/3/19 from Arabidopsis. [].In humans, DNAJA1, DNAJA2 and HSC70 have been shown to play key roles in both the folding and degradation of wild-type and mutant CFTR (cystic fibrosis transmembrane conductance regulator) [, ]. They also function as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis [].