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 [[cite:PUB00072552]].
","llm":false,"checked":false,"updated":false},{"text":"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 salt transport. Dysfunction of the CFTR channel causes the life-threatening disease, cystic fibrosis, in which trans-epithelial ion transport is disrupted [[cite:PUB00013905]]. Defective phosphorylation has been seen to be a cause for this altered activity [[cite:PUB00100468]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00072552":{"PMID":11441126,"ISBN":null,"volume":"42","issue":"7","year":2001,"title":"The human ATP-binding cassette (ABC) transporter superfamily.","URL":null,"raw_pages":"1007-17","medline_journal":"J Lipid Res","ISO_journal":"J. Lipid Res.","authors":["Dean M","Hamon Y","Chimini G."],"DOI_URL":null},"PUB00013905":{"PMID":9922375,"ISBN":null,"volume":"79","issue":"1 Suppl","year":1999,"title":"Structure and function of the CFTR chloride channel.","URL":null,"raw_pages":"S23-45","medline_journal":"Physiol Rev","ISO_journal":"Physiol. Rev.","authors":["Sheppard DN","Welsh MJ."],"DOI_URL":"http://intl-physrev.physiology.org/cgi/content/abstract/79/1/S23"},"PUB00100468":{"PMID":25330774,"ISBN":null,"volume":"15","issue":"2-3","year":2015,"title":"The major cystic fibrosis causing mutation exhibits defective propensity for phosphorylation.","URL":null,"raw_pages":"447-61","medline_journal":"Proteomics","ISO_journal":"Proteomics","authors":["Pasyk S","Molinski S","Ahmadi S","Ramjeesingh M","Huan LJ","Chin S","Du K","Yeger H","Taylor P","Moran MF","Bear CE."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":7404,"pathways":36,"proteins":2398,"proteomes":757,"sets":0,"structural_models":{"alphafold":569,"bfvd":0},"structures":26,"taxa":2607},"entry_annotations":{},"cross_references":{"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"5.6.1.6","url":"https://enzyme.expasy.org/EC/5.6.1.6"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}