SLC25A4

Solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4

PDB rendering based on 1okc.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1okc, 2c3e

Identifiers

Symbols

SLC25A4 ; 1; AAC1; ANT; ANT 1; ANT1; MTDPS12; PEO2; PEO3; T1

External IDs

OMIM: 103220 MGI: 1353495 HomoloGene: 36058 IUPHAR: 1062 ChEMBL: 1879 GeneCards: SLC25A4 Gene

Gene ontology
Molecular function	• protein binding • adenine transmembrane transporter activity
Cellular component	• nucleus • mitochondrion • mitochondrial inner membrane • integral component of plasma membrane
Biological process	• mitochondrial genome maintenance • generation of precursor metabolites and energy • energy reserve metabolic process • transport • apoptotic mitochondrial changes • adenine transport • viral process • small molecule metabolic process • regulation of insulin secretion • transmembrane transport • negative regulation of necroptotic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
186.06 – 186.07 Mb

Chr 8:
46.21 – 46.21 Mb

PubMed search

ADP/ATP translocase 1 is an enzyme that in humans is encoded by the SLC25A4 gene or adenine nucleotide translocator, ANT.^[1]^[2]

Interactions

SLC25A4 has been shown to interact with Bcl-2-associated X protein.^[3]

References

↑ Fan YS, Yang HM, Lin CC (Jun 1992). "Assignment of the human muscle adenine nucleotide translocator gene (ANT1) to 4q35 by fluorescence in situ hybridization". Cytogenet Cell Genet 60 (1): 29–30. doi:10.1159/000133288. PMID 1582253.
↑ "Entrez Gene: SLC25A4 solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4".
↑ Marzo, I; Brenner C, Zamzami N, Jürgensmeier J M, Susin S A, Vieira H L, Prévost M C, Xie Z, Matsuyama S, Reed J C, Kroemer G (Sep 1998). "Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis". Science (UNITED STATES) 281 (5385): 2027–31. doi:10.1126/science.281.5385.2027. ISSN 0036-8075. PMID 9748162.

Vieira HL, Haouzi D, El Hamel C et al. (2001). "Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator.". Cell Death Differ. 7 (12): 1146–54. doi:10.1038/sj.cdd.4400778. PMID 11175251.
Ferri KF, Jacotot E, Blanco J et al. (2001). "Mitochondrial control of cell death induced by HIV-1-encoded proteins.". Ann. N. Y. Acad. Sci. 926: 149–64. doi:10.1111/j.1749-6632.2000.tb05609.x. PMID 11193032.
Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi:10.1089/104454904773819789. PMID 15142377.
Andersen JL, Planelles V (2005). "The role of Vpr in HIV-1 pathogenesis.". Curr. HIV Res. 3 (1): 43–51. doi:10.2174/1570162052772988. PMID 15638722.
Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology 2: 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
Zhao RY, Bukrinsky M, Elder RT (2005). "HIV-1 viral protein R (Vpr) & host cellular responses". Indian J. Med. Res. 121 (4): 270–86. PMID 15817944.
Muthumani K, Choo AY, Premkumar A et al. (2006). "Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism". Cell Death Differ. 12 Suppl 1: 962–70. doi:10.1038/sj.cdd.4401583. PMID 15832179.
Li L, Li HS, Pauza CD et al. (2006). "Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions". Cell Res. 15 (11–12): 923–34. doi:10.1038/sj.cr.7290370. PMID 16354571.
Moon HS, Yang JS (2006). "Role of HIV Vpr as a regulator of apoptosis and an effector on bystander cells". Mol. Cells 21 (1): 7–20. PMID 16511342.
Cozens AL, Runswick MJ, Walker JE (1989). "DNA sequences of two expressed nuclear genes for human mitochondrial ADP/ATP translocase". J. Mol. Biol. 206 (2): 261–80. doi:10.1016/0022-2836(89)90477-4. PMID 2541251.
Li K, Warner CK, Hodge JA et al. (1989). "A human muscle adenine nucleotide translocator gene has four exons, is located on chromosome 4, and is differentially expressed". J. Biol. Chem. 264 (24): 13998–4004. PMID 2547778.
Neckelmann N, Li K, Wade RP et al. (1987). "cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes". Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7580–4. doi:10.1073/pnas.84.21.7580. PMC 299343. PMID 2823266.
Houldsworth J, Attardi G (1988). "Two distinct genes for ADP/ATP translocase are expressed at the mRNA level in adult human liver". Proc. Natl. Acad. Sci. U.S.A. 85 (2): 377–81. doi:10.1073/pnas.85.2.377. PMC 279551. PMID 2829183.
Wijmenga C, Winokur ST, Padberg GW et al. (1993). "The human skeletal muscle adenine nucleotide translocator gene maps to chromosome 4q35 in the region of the facioscapulohumeral muscular dystrophy locus". Hum. Genet. 92 (2): 198–203. doi:10.1007/BF00219692. PMID 8103757.
Bakker HD, Scholte HR, Van den Bogert C et al. (1993). "Deficiency of the adenine nucleotide translocator in muscle of a patient with myopathy and lactic acidosis: a new mitochondrial defect". Pediatr. Res. 33 (4 Pt 1): 412–7. doi:10.1203/00006450-199304000-00019. PMID 8479824.
Kaukonen JA, Amati P, Suomalainen A et al. (1996). "An autosomal locus predisposing to multiple deletions of mtDNA on chromosome 3p". Am. J. Hum. Genet. 58 (4): 763–9. PMC 1914672. PMID 8644740.
Marzo I, Brenner C, Zamzami N et al. (1998). "Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis". Science 281 (5385): 2027–31. doi:10.1126/science.281.5385.2027. PMID 9748162.
Kaukonen J, Zeviani M, Comi GP et al. (1999). "A third locus predisposing to multiple deletions of mtDNA in autosomal dominant progressive external ophthalmoplegia". Am. J. Hum. Genet. 65 (1): 256–61. doi:10.1086/302445. PMC 1378100. PMID 10364542.
Jacotot E, Ravagnan L, Loeffler M et al. (2000). "The HIV-1 Viral Protein R Induces Apoptosis via a Direct Effect on the Mitochondrial Permeability Transition Pore". J. Exp. Med. 191 (1): 33–46. doi:10.1084/jem.191.1.33. PMC 2195797. PMID 10620603.

PDB gallery

1okc: STRUCTURE OF MITOCHONDRIAL ADP/ATP CARRIER IN COMPLEX WITH CARBOXYATRACTYLOSIDE

2c3e: THE BOVINE MITOCHONDRIAL ADP-ATP CARRIER

External links

SLC25A4 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

Membrane proteins, carrier proteins: membrane transport proteins solute carrier (TC 2A)

By group

SLC1–10

(1):	high affinity glutamate and neutral amino-acid transporter SLC1A1 2 3 4 5 6 7

(2):	facilitative GLUT transporter SLC2A1 2 3 4 5 6 7 8 9 10 11 12 13 14

(3):	heavy subunits of heterodimeric amino-acid transporters SLC3A1 2

(4):	bicarbonate transporter SLC4A1 2 3 4 5 6 7 8 9 10 11

(5):	sodium glucose cotransporter SLC5A1 2 3 4 5 6 7 8 9 10 11 12

(6):	sodium- and chloride- dependent sodium:neurotransmitter symporters SLC6A1 SLC6A2 SLC6A3 SLC6A4 SLC6A5 SLC6A6 SLC6A7 SLC6A8 SLC6A9 SLC6A10 SLC6A11 SLC6A12 SLC6A13 SLC6A14 SLC6A15 SLC6A16 SLC6A17 SLC6A18 SLC6A19 SLC6A20

(7):	cationic amino-acid transporter/glycoprotein-associated SLC7A1 SLC7A2 SLC7A3 SLC7A4 glycoprotein-associated/light or catalytic subunits of heterodimeric amino-acid transporters SLC7A5 SLC7A6 SLC7A7 SLC7A8 SLC7A9 SLC7A10 SLC7A11 SLC7A13 SLC7A14

(8):	Na+/Ca2+ exchanger SLC8A1 SLC8A2 SLC8A3

(9):	Na+/H+ exchanger SLC9A1 SLC9A2 SLC9A3 SLC9A4 SLC9A5 SLC9A6 SLC9A7 SLC9A8 SLC9A9 SLC9A10 SLC9A11

(10):	sodium bile salt cotransport SLC10A1 SLC10A2 SLC10A3 SLC10A4 SLC10A5 SLC10A6 SLC10A7 10A1 10A2 10A3 10A7

SLC11–20

(11):	proton coupled metal ion transporter SLC11A1 SLC11A211A3

(12):	electroneutral cation-Cl cotransporter SLC12A1 SLC12A2 SLC12A3 SLC12A4 SLC12A5 SLC12A6 SLC12A7 SLC12A8 SLC12A9

(13):	human Na+-sulfate/carboxylate cotransporter SLC13A1 SLC13A2 SLC13A3 SLC13A4 SLC13A5

(14):	urea transporter SLC14A1 SLC14A2

(15):	proton oligopeptide cotransporter SLC15A1 SLC15A2 SLC15A3 SLC15A4

(16):	monocarboxylate transporter SLC16A1 SLC16A2 SLC16A3 SLC16A4 SLC16A5 SLC16A6 SLC16A7 SLC16A8 SLC16A9 SLC16A10 SLC16A11 SLC16A12 SLC16A13 SLC16A14

(17):	Vesicular glutamate transporter 1 SLC17A1 SLC17A2 SLC17A3 SLC17A4 SLC17A5 SLC17A6 SLC17A7 SLC17A8 SLC17A9

(18):	vesicular monoamine transporter SLC18A1 SLC18A2 SLC18A3

(19):	folate/thiamine transporter SLC19A1 SLC19A2 SLC19A3

(20):	type III Na+-phosphate cotransporter SLC20A1 SLC20A2

SLC21–30

(21):	Organic anion-transporting polypeptide SLCO1A2 SLCO1B1 SLCO1B3 SLCO1B4 SLCO1C1 SLCO2A1 SLCO2B1 SLCO3A1 SLCO4A1 SLCO4C1 SLCO5A1(SLCO6A1)

(22):	organic cation/anion/zwitterion transporter SLC22A1 SLC22A2 SLC22A3 SLC22A4 SLC22A5 SLC22A6 SLC22A7 SLC22A8 SLC22A9 SLC22A10 SLC22A11 SLC22A12 SLC22A13 SLC22A14 SLC22A15 SLC22A16 SLC22A17 SLC22A18 SLC22A19 SLC22A20

(23):	Na+-dependent ascorbic acid transporter SLC23A1 SLC23A2 SLC23A3 SLC23A4

(24):	Na+/(Ca2+-K+) exchanger SLC24A1 SLC24A2 SLC24A3 SLC24A4 SLC24A5 SLC24A6

(25):	mitochondrial carrier SLC25A1 SLC25A2 SLC25A3 SLC25A4 SLC25A5 SLC25A6 SLC25A7 SLC25A8 SLC25A9 SLC25A10 SLC25A11 SLC25A12 SLC25A13 SLC25A14 SLC25A15 SLC25A16 SLC25A17 SLC25A18 SLC25A19 SLC25A20 SLC25A21 SLC25A22 SLC25A23 SLC25A24 SLC25A25 SLC25A26 SLC25A27 SLC25A28 SLC25A29 SLC25A30 SLC25A31 SLC25A32 SLC25A33 SLC25A34 SLC25A35 SLC25A36 SLC25A37 SLC25A38 SLC25A39 SLC25A40 SLC25A41 SLC25A42 SLC25A43 SLC25A44 SLC25A45 SLC25A46

(26):	multifunctional anion exchanger SLC26A1 SLC26A2 SLC26A3 SLC26A4 SLC26A5 SLC26A6 SLC26A7 SLC26A8 SLC26A9 SLC26A10 SLC26A11

(27):	fatty acid transport proteins SLC27A1 SLC27A2 SLC27A3 SLC27A4 SLC27A5 SLC27A6

(28):	Na+-coupled nucleoside transport (SLC28A1 SLC28A2 SLC28A3

(29):	facilitative nucleoside transporter SLC29A1 SLC29A2 SLC29A3 SLC29A4

(30):	zinc efflux SLC30A1 SLC30A2 SLC30A3 SLC30A4 SLC30A5 SLC30A6 SLC30A7 SLC30A8 SLC30A9 SLC30A10

SLC31–40

(31):	copper transporter SLC31A1

(32):	Vesicular glutamate transporter 1 SLC32A1

(33):	Acetyl-CoA transporter SLC33A1

(34):	type II Na+-phosphate cotransporter SLC34A1 SLC34A2 SLC34A3

(35):	nucleoside-sugar transporter SLC35A1 SLC35A2 SLC35A3 SLC35A4 SLC35A5 SLC35B1 SLC35B2 SLC35B3 SLC35B4 SLC35C1 SLC35C2 SLC35D1 SLC35D2 SLC35D3 SLC35E1 SLC35E2 SLC35E3 SLC35E4

(36):	proton-coupled amino-acid transporter SLC36A1 SLC36A2 SLC36A3 SLC36A436A2

(37):	sugar-phosphate/phosphate exchanger SLC37A1 SLC37A2 SLC37A3 SLC37A4

(38):	System A & N, sodium-coupled neutral amino-acid transporter SLC38A1 SLC38A2 SLC38A3 SLC38A4 SLC38A5 SLC38A6 SLC38A10

(39):	metal ion transporter SLC39A1 SLC39A2 SLC39A3 SLC39A4 SLC39A5 SLC39A6 SLC39A7 SLC39A8 SLC39A9 SLC39A10 SLC39A11 SLC39A12 SLC39A13 SLC39A14

(40):	basolateral iron transporter SLC40A1

SLC41–48

(41):	Magnesium transporter E SLC41A1 SLC41A2 SLC41A3

(42):	Ammonia transporter RhAG RhBG RhCG

(43):	Na+-independent, system-L like amino-acid transporter SLC43A1 SLC43A2 SLC43A3

(44):	Choline-like transporter SLC44A1 SLC44A2 SLC44A3 SLC44A4 SLC44A5

(45):	Putative sugar transporter SLC45A1 SLC45A2 SLC54A3 SLC45A4

(46):	Folate transporter SLC46A1 SLC46A2

(47):	multidrug and toxin extrusion SLC47A1 SLC47A2

(48):	Heme transporter

SLCO1–4

O1A2 O1B1 O1B3 O2B1 O431 O4A1

Ion pumps

Symporter, Cotransporter	Na+/K+,l- Na/Pi3 Na+/Cl- Na/glucose Na+/I- Cl-/K+ 4 5

Antiporter (exchanger)	Na+/H+ Na+/Ca2+ Na+/(Ca2+-K+) - Cl-/HCO3- (Band 3) Cl-formate exchanger Cl-oxalate exchanger

see also solute carrier disorders

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

SLC25A4

Interactions

References

Further reading

External links