ATP-binding cassette transporter family C


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ATP-binding cassette transporters are ubiquitous membrane proteins characterized by active ATP-dependent movement of a range of substrates, including ions, lipids, peptides, steroids. Individual subunits are typically made up of two groups of 6TM-spanning domains, with two nucleotide-binding domains (NBD). The majority of eukaryotic ABC transporters are ‘full’ transporters incorporating both TM and NBD entities. Some ABCs, notably the ABCD and ABCG families are half-transporters with only a single membrane spanning domain and one NBD, and are only functional as homo- or heterodimers. Eukaryotic ABC transporters convey substrates from the cytoplasm, either out of the cell or into intracellular organelles. Their role in the efflux of exogenous compounds, notably chemotherapeutic agents, has led to considerable interest.


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A further group of ABC transporter-like proteins have been identified to lack membrane spanning regions and are not believed to be functional transporters, but appear to have a role in protein translation [1-2]: ABCE1 (P61221, also known as OABP or 2'-5' oligoadenylate-binding protein); ABCF1 (Q8NE71, also known as ABC50 or TNF-α-stimulated ABC protein); ABCF2 (Q9UG63, also known as iron-inhibited ABC transporter 2) and ABCF3 (Q9NUQ8).

Further reading

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NC-IUPHAR subcommittee and family contributors

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How to cite this family page

Database page citation:

Mary Vore. ATP-binding cassette transporter family. Accessed on 26/03/2017. IUPHAR/BPS Guide to PHARMACOLOGY,

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Kelly E, Marrion N, Peters JA, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Southan C, Davies JA and CGTP Collaborators (2015) The Concise Guide to PHARMACOLOGY 2015/16: Transporters. Br J Pharmacol. 172: 6110-6202.