EC 5.6.1.6 - Channel-conductance-controlling ATPase

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IntEnz Enzyme Nomenclature
EC 5.6.1.6

Names

Accepted name:
channel-conductance-controlling ATPase
Other names:
cystic-fibrosis membrane-conductance-regulating protein
CFTR
Systematic name:
ATP phosphohydrolase (channel-conductance-controlling)

Reaction

Comments:

ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. The enzyme is found in animals, and in humans its absence brings about cystic fibrosis. Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis. Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains. The enzyme is also involved in the functioning of other transmembrane channels. Formerly EC 3.6.3.49.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00185
Structural data: CSA , EC2PDB
Gene Ontology: GO:0005260
UniProtKB/Swiss-Prot: (47) [show] [UniProt]

References

  1. Chen, M. and Zhang, J.T.
    Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes.
    Mol. Membr. Biol. 13 : 33-40 (1996). [PMID: 9147660]
  2. Tusnady, G.E., Bakos, E., Varadi, A. and Sarkadi, B.
    Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters.
    FEBS Lett. 402 : 1-3 (1997). [PMID: 9013845]
  3. Sheppard, D.N. and Welsh, M.J.
    Structure and function of the CFTR chloride channel.
    Physiol. Rev. 79 : S23-S45 (1999). [PMID: 9922375]
  4. Hwang, T. C., Sheppard, D. N.
    Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.
    J. Physiol. (Lond.) 587 : 2151-2161 (2009). [PMID: 19332488]

[EC 5.6.1.6 created 2000 as EC 3.6.3.49, transferred 2018 to EC 5.6.1.6]