ID ADT3_HUMAN Reviewed; 298 AA. AC P12236; Q96C49; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-JUN-2021, entry version 232. DE RecName: Full=ADP/ATP translocase 3 {ECO:0000305}; DE AltName: Full=ADP,ATP carrier protein 3 {ECO:0000303|PubMed:31341297}; DE AltName: Full=ADP,ATP carrier protein, isoform T2 {ECO:0000303|PubMed:2541251}; DE Short=ANT 2 {ECO:0000303|PubMed:2541251}; DE AltName: Full=Adenine nucleotide translocator 3 {ECO:0000303|PubMed:8486369}; DE Short=ANT 3 {ECO:0000303|PubMed:8486369}; DE AltName: Full=Solute carrier family 25 member 6 {ECO:0000305}; DE Contains: DE RecName: Full=ADP/ATP translocase 3, N-terminally processed; GN Name=SLC25A6 {ECO:0000312|HGNC:HGNC:10992}; GN Synonyms=AAC3 {ECO:0000303|PubMed:31341297}, GN ANT3 {ECO:0000303|PubMed:8486369}; ORFNames=CDABP0051 {ECO:0000303|Ref.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2541251; DOI=10.1016/0022-2836(89)90477-4; RA Cozens A.L., Runswick M.J., Walker J.E.; RT "DNA sequences of two expressed nuclear genes for human mitochondrial RT ADP/ATP translocase."; RL J. Mol. Biol. 206:261-280(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-242. RC TISSUE=Leukemia; RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., RA Margolin J.F.; RT "Pediatric leukemia cDNA sequencing project."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Cervix, Eye, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PROTEIN SEQUENCE OF 2-10, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUL-2004) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-298. RC TISSUE=Liver; RX PubMed=2829183; DOI=10.1073/pnas.85.2.377; RA Houldsworth J., Attardi G.; RT "Two distinct genes for ADP/ATP translocase are expressed at the mRNA level RT in adult human liver."; RL Proc. Natl. Acad. Sci. U.S.A. 85:377-381(1988). RN [6] RP IDENTIFICATION. RX PubMed=8486369; DOI=10.1006/geno.1993.1135; RA Slim R., Levilliers J., Luedecke H.J., Claussen U., Nguyen V.C., RA Gough N.M., Horsthemke B., Petit C.; RT "A human pseudoautosomal gene encodes the ANT3 ADP/ATP translocase and RT escapes X-inactivation."; RL Genomics 16:26-33(1993). RN [7] RP FUNCTION IN APOPTOSIS. RX PubMed=15033708; DOI=10.1196/annals.1299.022; RA Verrier F., Mignotte B., Jan G., Brenner C.; RT "Study of PTPC composition during apoptosis for identification of viral RT protein target."; RL Ann. N. Y. Acad. Sci. 1010:126-142(2003). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [9] RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION). RX PubMed=16120388; DOI=10.1016/j.mito.2004.06.012; RA Deniaud A., Brenner C., Kroemer G.; RT "Mitochondrial membrane permeabilization by HIV-1 Vpr."; RL Mitochondrion 4:223-233(2004). RN [10] RP INTERACTION WITH INFLUENZA A VIRUS PB1-F2 (MICROBIAL INFECTION). RX PubMed=16201016; DOI=10.1371/journal.ppat.0010004; RA Zamarin D., Garcia-Sastre A., Xiao X., Wang R., Palese P.; RT "Influenza virus PB1-F2 protein induces cell death through mitochondrial RT ANT3 and VDAC1."; RL PLoS Pathog. 1:40-54(2005). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105 AND LYS-268, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-52, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=27641616; DOI=10.1038/srep33516; RA Marginedas-Freixa I., Hattab C., Bouyer G., Halle F., Chene A., RA Lefevre S.D., Cambot M., Cueff A., Schmitt M., Gamain B., Lacapere J.J., RA Egee S., Bihel F., Le Van Kim C., Ostuni M.A.; RT "TSPO ligands stimulate ZnPPIX transport and ROS accumulation leading to RT the inhibition of P. falciparum growth in human blood."; RL Sci. Rep. 6:33516-33516(2016). RN [19] RP METHYLATION AT LYS-52. RX PubMed=31213526; DOI=10.1074/jbc.ra119.009045; RA Malecki J., Willemen H.L.D.M., Pinto R., Ho A.Y.Y., Moen A., Eijkelkamp N., RA Falnes P.O.; RT "Human FAM173A is a mitochondrial lysine-specific methyltransferase that RT targets adenine nucleotide translocase and affects mitochondrial RT respiration."; RL J. Biol. Chem. 0:0-0(2019). RN [20] RP GENE NAME. RX PubMed=31341297; DOI=10.1038/s41586-019-1400-3; RA Bertholet A.M., Chouchani E.T., Kazak L., Angelin A., Fedorenko A., RA Long J.Z., Vidoni S., Garrity R., Cho J., Terada N., Wallace D.C., RA Spiegelman B.M., Kirichok Y.; RT "H+ transport is an integral function of the mitochondrial ADP/ATP RT carrier."; RL Nature 571:515-520(2019). CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel CC the cell (By similarity). Cycles between the cytoplasmic-open state (c- CC state) and the matrix-open state (m-state): operates by the alternating CC access mechanism with a single substrate-binding site intermittently CC exposed to either the cytosolic (c-state) or matrix (m-state) side of CC the inner mitochondrial membrane (By similarity). In addition to its CC ADP:ATP antiporter activity, also involved in mitochondrial uncoupling CC and mitochondrial permeability transition pore (mPTP) activity CC (PubMed:15033708). Plays a role in mitochondrial uncoupling by acting CC as a proton transporter: proton transport uncouples the proton flows CC via the electron transport chain and ATP synthase to reduce the CC efficiency of ATP production and cause mitochondrial thermogenesis (By CC similarity). Proton transporter activity is inhibited by ADP:ATP CC antiporter activity, suggesting that SLC25A6/ANT3 acts as a master CC regulator of mitochondrial energy output by maintaining a delicate CC balance between ATP production (ADP:ATP antiporter activity) and CC thermogenesis (proton transporter activity) (By similarity). Proton CC transporter activity requires free fatty acids as cofactor, but does CC not transport it (By similarity). Also plays a key role in mPTP CC opening, a non-specific pore that enables free passage of the CC mitochondrial membranes to solutes of up to 1.5 kDa, and which CC contributes to cell death (PubMed:15033708). It is however unclear if CC SLC25A6/ANT3 constitutes a pore-forming component of mPTP or regulates CC it (By similarity). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000250|UniProtKB:P48962, ECO:0000269|PubMed:15033708}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P48962}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; CC Evidence={ECO:0000250|UniProtKB:P48962}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; CC Evidence={ECO:0000250|UniProtKB:P48962}; CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by CC the membrane-permeable bongkrekic acid (BKA). The cytoplasmic-open CC state (c-state) is inhibited by the membrane-impermeable toxic CC inhibitor carboxyatractyloside (CATR) (By similarity). Proton CC transporter activity is inhibited by ADP:ATP antiporter activity (By CC similarity). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000250|UniProtKB:P48962}. CC -!- SUBUNIT: Monomer (By similarity). Found in a complex with ARL2, ARL2BP CC and SLC25A6/ANT3 (By similarity). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000250|UniProtKB:P02722, ECO:0000250|UniProtKB:P32007}. CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus PB1-F2 CC protein. {ECO:0000269|PubMed:16201016}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr. CC {ECO:0000269|PubMed:16120388}. CC -!- INTERACTION: CC P12236; P63010: AP2B1; NbExp=4; IntAct=EBI-356254, EBI-432924; CC P12236; Q15323: KRT31; NbExp=3; IntAct=EBI-356254, EBI-948001; CC P12236; Q5S007: LRRK2; NbExp=2; IntAct=EBI-356254, EBI-5323863; CC P12236; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-356254, EBI-741037; CC P12236; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-356254, EBI-10172526; CC P12236; Q5JR59: MTUS2; NbExp=4; IntAct=EBI-356254, EBI-742948; CC P12236; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-356254, EBI-945833; CC P12236; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-356254, EBI-750487; CC P12236; Q13077: TRAF1; NbExp=3; IntAct=EBI-356254, EBI-359224; CC P12236; P36406: TRIM23; NbExp=3; IntAct=EBI-356254, EBI-740098; CC P12236; Q15654: TRIP6; NbExp=3; IntAct=EBI-356254, EBI-742327; CC P12236; P21796: VDAC1; NbExp=4; IntAct=EBI-356254, EBI-354158; CC P12236; P0C0U1: PB1; Xeno; NbExp=5; IntAct=EBI-356254, EBI-12579807; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein CC {ECO:0000255}. Membrane {ECO:0000269|PubMed:27641616}; Multi-pass CC membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP, CC ARL2 and SLC25A6/ANT3 is expressed in mitochondria (By similarity). May CC localize to non-mitochondrial membranes (By similarity). CC {ECO:0000250|UniProtKB:P12235}. CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes (at protein level). CC {ECO:0000269|PubMed:27641616}. CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of CC the membrane, but cross the membrane at an angle. Odd-numbered CC transmembrane helices exhibit a sharp kink, due to the presence of a CC conserved proline residue. {ECO:0000250|UniProtKB:P02722}. CC -!- PTM: Trimethylated by ANTKMT at Lys-52. {ECO:0000269|PubMed:31213526}. CC -!- MISCELLANEOUS: The gene coding for this protein is located in the CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes and escapes X- CC inactivation. {ECO:0000269|PubMed:8486369}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY007135; AAG01998.1; -; mRNA. DR EMBL; BC007295; AAH07295.1; -; mRNA. DR EMBL; BC007850; AAH07850.1; -; mRNA. DR EMBL; BC008737; AAH08737.1; -; mRNA. DR EMBL; BC008935; AAH08935.1; -; mRNA. DR EMBL; BC014775; AAH14775.1; -; mRNA. DR EMBL; BC031912; AAH31912.1; -; mRNA. DR EMBL; J03592; AAA36750.1; -; mRNA. DR CCDS; CCDS14114.1; -. DR PIR; S03894; S03894. DR RefSeq; NP_001627.2; NM_001636.3. DR SMR; P12236; -. DR BioGRID; 106790; 232. DR IntAct; P12236; 153. DR MINT; P12236; -. DR STRING; 9606.ENSP00000370808; -. DR ChEMBL; CHEMBL4105854; -. DR DrugBank; DB00720; Clodronic acid. DR DrugBank; DB01077; Etidronic acid. DR DrugCentral; P12236; -. DR TCDB; 2.A.29.1.10; the mitochondrial carrier (mc) family. DR iPTMnet; P12236; -. DR MetOSite; P12236; -. DR PhosphoSitePlus; P12236; -. DR SwissPalm; P12236; -. DR BioMuta; SLC25A6; -. DR DMDM; 113463; -. DR EPD; P12236; -. DR jPOST; P12236; -. DR MassIVE; P12236; -. DR PaxDb; P12236; -. DR PeptideAtlas; P12236; -. DR PRIDE; P12236; -. DR ProteomicsDB; 52837; -. DR TopDownProteomics; P12236; -. DR Antibodypedia; 23393; 280 antibodies. DR DNASU; 293; -. DR Ensembl; ENST00000381401; ENSP00000370808; ENSG00000169100. DR GeneID; 293; -. DR KEGG; hsa:293; -. DR CTD; 293; -. DR DisGeNET; 293; -. DR GeneCards; SLC25A6; -. DR HGNC; HGNC:10992; SLC25A6. DR HPA; ENSG00000169100; Tissue enhanced (blood). DR MIM; 300151; gene. DR MIM; 403000; gene. DR neXtProt; NX_P12236; -. DR OpenTargets; ENSG00000169100; -. DR PharmGKB; PA35868; -. DR VEuPathDB; HostDB:ENSG00000169100.13; -. DR eggNOG; KOG0749; Eukaryota. DR GeneTree; ENSGT00940000162883; -. DR HOGENOM; CLU_015166_12_0_1; -. DR InParanoid; P12236; -. DR OMA; FSGVCAY; -. DR OrthoDB; 870903at2759; -. DR PhylomeDB; P12236; -. DR TreeFam; TF300743; -. DR PathwayCommons; P12236; -. DR Reactome; R-HSA-1268020; Mitochondrial protein import. DR Reactome; R-HSA-168277; Influenza Virus Induced Apoptosis. DR Reactome; R-HSA-180897; Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabilization. DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane. DR BioGRID-ORCS; 293; 8 hits in 515 CRISPR screens. DR ChiTaRS; SLC25A6; human. DR GeneWiki; SLC25A6; -. DR GenomeRNAi; 293; -. DR Pharos; P12236; Tbio. DR PRO; PR:P12236; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P12236; protein. DR Bgee; ENSG00000169100; Expressed in saliva-secreting gland and 248 other tissues. DR ExpressionAtlas; P12236; baseline and differential. DR Genevisible; P12236; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; TAS:UniProtKB. DR GO; GO:0005471; F:ATP:ADP antiporter activity; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro. DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro. DR GO; GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.50.40.10; -; 1. DR InterPro; IPR002113; ADT_euk_type. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR PANTHER; PTHR45635; PTHR45635; 1. DR Pfam; PF00153; Mito_carr; 3. DR PRINTS; PR00927; ADPTRNSLCASE. DR PRINTS; PR00926; MITOCARRIER. DR SUPFAM; SSF103506; SSF103506; 1. DR PROSITE; PS50920; SOLCAR; 3. PE 1: Evidence at protein level; KW Acetylation; Antiport; Apoptosis; Direct protein sequencing; KW Host-virus interaction; Membrane; Methylation; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..298 FT /note="ADP/ATP translocase 3" FT /id="PRO_0000425781" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT CHAIN 2..298 FT /note="ADP/ATP translocase 3, N-terminally processed" FT /id="PRO_0000090584" FT TOPO_DOM 1..7 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 8..37 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 38..74 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305" FT TRANSMEM 75..99 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 100..109 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 110..130 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 131..178 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305" FT TRANSMEM 179..199 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 200..210 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT TRANSMEM 211..231 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 232..273 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000305" FT TRANSMEM 274..291 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P02722" FT TOPO_DOM 292..298 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000305" FT REPEAT 6..98 FT /note="Solcar 1" FT REPEAT 111..201 FT /note="Solcar 2" FT REPEAT 212..297 FT /note="Solcar 3" FT REGION 235..240 FT /note="Important for transport activity" FT /evidence="ECO:0000250|UniProtKB:P12235" FT MOTIF 235..240 FT /note="Nucleotide carrier signature motif" FT /evidence="ECO:0000250|UniProtKB:P02722" FT BINDING 80 FT /note="ADP" FT /evidence="ECO:0000250|UniProtKB:P02722" FT BINDING 92 FT /note="ADP" FT /evidence="ECO:0000250|UniProtKB:P02722" FT BINDING 235 FT /note="ADP" FT /evidence="ECO:0000250|UniProtKB:P02722" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 2 FT /note="N-acetylthreonine; in ADP/ATP translocase 3, N- FT terminally processed" FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712" FT MOD_RES 52 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:31213526, FT ECO:0007744|PubMed:24129315" FT MOD_RES 105 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 268 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 242 FT /note="S -> F" FT /evidence="ECO:0000269|Ref.2" FT /id="VAR_054819" FT CONFLICT 105..108 FT /note="KHTQ -> RHA (in Ref. 5; AAA36750)" FT /evidence="ECO:0000305" SQ SEQUENCE 298 AA; 32866 MW; 18534E9F0E49672F CRC64; MTEQAISFAK DFLAGGIAAA ISKTAVAPIE RVKLLLQVQH ASKQIAADKQ YKGIVDCIVR IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKHTQFW RYFAGNLASG GAAGATSLCF VYPLDFARTR LAADVGKSGT EREFRGLGDC LVKITKSDGI RGLYQGFSVS VQGIIIYRAA YFGVYDTAKG MLPDPKNTHI VVSWMIAQTV TAVAGVVSYP FDTVRRRMMM QSGRKGADIM YTGTVDCWRK IFRDEGGKAF FKGAWSNVLR GMGGAFVLVL YDELKKVI //