Adenine nucleotide translocator

ADP/ATP translocases
Cytoplasmic view of the binding pocket of ATP–ADP translocase 1, PDB: 1OKC​.
Identifiers
SymbolAden_trnslctor
PfamPF00153
InterProIPR002113
TCDB2.A.29.1.2
OPM superfamily21
OPM protein2c3e
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4
Identifiers
SymbolSLC25A4
Alt. symbolsPEO3, PEO2, ANT1
NCBI gene291
HGNC10990
OMIM103220
RefSeqNM_001151
UniProtP12235
Other data
LocusChr. 4 q35
Search for
StructuresSwiss-model
DomainsInterPro
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 5
Identifiers
SymbolSLC25A5
Alt. symbolsANT2
NCBI gene292
HGNC10991
OMIM300150
RefSeqNM_001152
UniProtP05141
Other data
LocusChr. X q24-q26
Search for
StructuresSwiss-model
DomainsInterPro
solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 6
Identifiers
SymbolSLC25A6
Alt. symbolsANT3
NCBI gene293
HGNC10992
OMIM403000
RefSeqNM_001636
UniProtP12236
Other data
LocusChr. Y p
Search for
StructuresSwiss-model
DomainsInterPro

Adenine nucleotide translocator (ANT), also known as the ADP/ATP translocase (ANT), ADP/ATP carrier protein (AAC) or mitochondrial ADP/ATP carrier, exchanges free ATP with free ADP across the inner mitochondrial membrane.[1][2] ANT is the most abundant protein in the inner mitochondrial membrane and belongs to the mitochondrial carrier family.[3]

Free ADP is transported from the cytoplasm to the mitochondrial matrix, while ATP produced from oxidative phosphorylation is transported from the mitochondrial matrix to the cytoplasm, thus providing the cell with its main energy currency.[4] ADP/ATP translocases are exclusive to eukaryotes and are thought to have evolved during eukaryogenesis.[5] Human cells express four ADP/ATP translocases: SLC25A4, SLC25A5, SLC25A6 and SLC25A31, which constitute more than 10% of the protein in the inner mitochondrial membrane.[6] These proteins are classified under the mitochondrial carrier superfamily.

  1. ^ Klingenberg M (October 2008). "The ADP and ATP transport in mitochondria and its carrier". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1778 (10): 1978–2021. doi:10.1016/j.bbamem.2008.04.011. PMID 18510943.
  2. ^ Kunji ER, Aleksandrova A, King MS, Majd H, Ashton VL, Cerson E, Springett R, Kibalchenko M, Tavoulari S, Crichton PG, Ruprecht JJ (October 2016). "The transport mechanism of the mitochondrial ADP/ATP carrier". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Channels and transporters in cell metabolism. 1863 (10): 2379–93. doi:10.1016/j.bbamcr.2016.03.015. PMID 27001633.
  3. ^ Palmieri F, Monné M (October 2016). "Discoveries, metabolic roles and diseases of mitochondrial carriers: A review". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Channels and transporters in cell metabolism. 1863 (10): 2362–78. doi:10.1016/j.bbamcr.2016.03.007. hdl:11563/126168. PMID 26968366.
  4. ^ Stryer L, Berg JM, Tymoczko JL (2007). Biochemistry. San Francisco: W.H. Freeman. p. 553. ISBN 978-0-7167-8724-2.
  5. ^ Radzvilavicius AL, Blackstone NW (October 2015). "Conflict and cooperation in eukaryogenesis: implications for the timing of endosymbiosis and the evolution of sex". Journal of the Royal Society, Interface. 12 (111): 20150584. doi:10.1098/rsif.2015.0584. PMC 4614496. PMID 26468067.
  6. ^ Brandolin G, Dupont Y, Vignais PV (April 1985). "Substrate-induced modifications of the intrinsic fluorescence of the isolated adenine nucleotide carrier protein: demonstration of distinct conformational states". Biochemistry. 24 (8): 1991–7. doi:10.1021/bi00329a029. PMID 2990548.