ID ADT2_MOUSE Reviewed; 298 AA. AC P51881; Q61311; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 201. DE RecName: Full=ADP/ATP translocase 2 {ECO:0000305}; DE AltName: Full=ADP,ATP carrier protein 2 {ECO:0000303|PubMed:31341297}; DE AltName: Full=Adenine nucleotide translocator 2 {ECO:0000303|PubMed:10974536, ECO:0000303|PubMed:8903724}; DE Short=ANT 2 {ECO:0000303|PubMed:10974536, ECO:0000303|PubMed:8903724}; DE AltName: Full=Solute carrier family 25 member 5 {ECO:0000305}; DE Contains: DE RecName: Full=ADP/ATP translocase 2, N-terminally processed {ECO:0000305|Ref.7}; GN Name=Slc25a5 {ECO:0000312|MGI:MGI:1353496}; GN Synonyms=Aac2 {ECO:0000303|PubMed:31341297}, Ant2 GN {ECO:0000303|PubMed:10974536, ECO:0000303|PubMed:8903724}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=8903724; DOI=10.1007/s003359900007; RA Ellison J.W., Li X., Francke U., Shapiro L.J.; RT "Rapid evolution of human pseudoautosomal genes and their mouse homologs."; RL Mamm. Genome 7:25-30(1996). RN [2] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Skeletal muscle; RA Sheldon J.G.; RL Thesis (1995), University of Cambridge, United Kingdom. RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=129/Sv; RA Costet P., Laplace C.; RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE REVISION. RA Laplace C.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10974536; DOI=10.1016/s0378-1119(00)00252-3; RA Levy S.E., Chen Y.-S., Graham B.H., Wallace D.C.; RT "Expression and sequence analysis of the mouse adenine nucleotide RT translocase 1 and 2 genes."; RL Gene 254:57-66(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland; 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 [7] RP PROTEIN SEQUENCE OF 2-31; 34-43; 64-72; 81-92; 97-106 AND 189-199, CLEAVAGE RP OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Liver; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [8] RP DISRUPTION PHENOTYPE. RX PubMed=14749836; DOI=10.1038/nature02229; RA Kokoszka J.E., Waymire K.G., Levy S.E., Sligh J.E., Cai J., Jones D.P., RA MacGregor G.R., Wallace D.C.; RT "The ADP/ATP translocator is not essential for the mitochondrial RT permeability transition pore."; RL Nature 427:461-465(2004). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105, SUCCINYLATION [LARGE SCALE RP ANALYSIS] AT LYS-43; LYS-105; LYS-147; LYS-155 AND LYS-268, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast, and Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105; LYS-147; LYS-155; LYS-163; RP LYS-166 AND LYS-268, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria RT identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). RN [13] RP DISRUPTION PHENOTYPE. RX PubMed=25613378; DOI=10.1038/cdd.2014.230; RA Cho J., Seo J., Lim C.H., Yang L., Shiratsuchi T., Lee M.H., RA Chowdhury R.R., Kasahara H., Kim J.S., Oh S.P., Lee Y.J., Terada N.; RT "Mitochondrial ATP transporter Ant2 depletion impairs erythropoiesis and B RT lymphopoiesis."; RL Cell Death Differ. 22:1437-1450(2015). RN [14] RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=31489369; DOI=10.1126/sciadv.aaw4597; RA Karch J., Bround M.J., Khalil H., Sargent M.A., Latchman N., Terada N., RA Peixoto P.M., Molkentin J.D.; RT "Inhibition of mitochondrial permeability transition by deletion of the ANT RT family and CypD."; RL Sci. Adv. 5:eaaw4597-eaaw4597(2019). RN [15] RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TIMM44. RX PubMed=31618756; DOI=10.1038/s41586-019-1667-4; RA Hoshino A., Wang W.J., Wada S., McDermott-Roe C., Evans C.S., Gosis B., RA Morley M.P., Rathi K.S., Li J., Li K., Yang S., McManus M.J., Bowman C., RA Potluri P., Levin M., Damrauer S., Wallace D.C., Holzbaur E.L.F., Arany Z.; RT "The ADP/ATP translocase drives mitophagy independent of nucleotide RT exchange."; RL Nature 575:375-379(2019). RN [16] RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION RP PHENOTYPE. 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 (PubMed:31341297). Cycles between the cytoplasmic-open state CC (c-state) and the matrix-open state (m-state): operates by the CC alternating access mechanism with a single substrate-binding site CC intermittently exposed to either the cytosolic (c-state) or matrix (m- CC state) side of the inner mitochondrial membrane (By similarity). In CC addition to its ADP:ATP antiporter activity, also involved in CC mitochondrial uncoupling and mitochondrial permeability transition pore CC (mPTP) activity (PubMed:31489369, PubMed:31341297). Plays a role in CC mitochondrial uncoupling by acting as a proton transporter: proton CC transport uncouples the proton flows via the electron transport chain CC and ATP synthase to reduce the efficiency of ATP production and cause CC mitochondrial thermogenesis (PubMed:31341297). Proton transporter CC activity is inhibited by ADP:ATP antiporter activity, suggesting that CC SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output CC by maintaining a delicate balance between ATP production (ADP:ATP CC antiporter activity) and thermogenesis (proton transporter activity) CC (PubMed:31341297). Proton transporter activity requires free fatty CC acids as cofactor, but does not transport it (PubMed:31341297). CC Probably mediates mitochondrial uncoupling in tissues that do not CC express UCP1 (PubMed:31341297). Also plays a key role in mPTP opening, CC a non-specific pore that enables free passage of the mitochondrial CC membranes to solutes of up to 1.5 kDa, and which contributes to cell CC death (PubMed:31489369). It is however unclear if SLC25A5/ANT2 CC constitutes a pore-forming component of mPTP or regulates it CC (PubMed:31489369). Acts as a regulator of mitophagy independently of CC ADP:ATP antiporter activity: promotes mitophagy via interaction with CC TIMM44, leading to inhibit the presequence translocase TIMM23, thereby CC promoting stabilization of PINK1 (PubMed:31618756). As part of the CC mitotic spindle-associated MMXD complex it may play a role in CC chromosome segregation (By similarity). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000250|UniProtKB:P05141, ECO:0000269|PubMed:31341297, CC ECO:0000269|PubMed:31489369, ECO:0000269|PubMed:31618756}. 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:0000269|PubMed:31341297}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; CC Evidence={ECO:0000269|PubMed:31341297}; CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by CC the membrane-permeable bongkrekic acid (BKA) (By similarity). The CC cytoplasmic-open state (c-state) is inhibited by the membrane- CC impermeable toxic inhibitor carboxyatractyloside (CATR) (By CC similarity). Proton transporter activity is inhibited by ADP:ATP CC antiporter activity (PubMed:31341297). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000269|PubMed:31341297}. CC -!- SUBUNIT: Monomer (By similarity). Component of the MMXD complex, which CC includes CIAO1, ERCC2, CIAO2B, MMS19 and SLC25A5/ANT2. Interacts with CC AK4 (By similarity). Interacts with TIMM44; leading to inhibit the CC presequence translocase TIMM23, thereby promoting stabilization of CC PINK1 (PubMed:31618756). {ECO:0000250|UniProtKB:G2QNH0, CC ECO:0000250|UniProtKB:P02722, ECO:0000250|UniProtKB:P05141, CC ECO:0000269|PubMed:31618756}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein CC {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P05141}; Multi-pass CC membrane protein {ECO:0000255}. Note=May localize to non-mitochondrial CC membranes. {ECO:0000250|UniProtKB:P05141}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:31489369}. 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:0000250|UniProtKB:P05141}. CC -!- DISRUPTION PHENOTYPE: Mice show an apparently normal embryonic CC development except pale phenotype, but show a reduced birth rate CC (PubMed:25613378). Postnatal growth is severely retarded with CC macrocytic anemia, B lymphocytopenia, lactic acidosis and bloated CC stomach, causing lethality within 4 weeks (PubMed:25613378). Mice CC develop anemia in a cell-autonomous manner by maturation arrest of CC erythroid precursors with increased reactive oxygen species and CC premature deaths (PubMed:25613378). B-lymphocyte development is also CC affected: splenocytes show a reduction in maximal respiration capacity CC and cellular ATP levels as well as an increase in cell death CC accompanying mitochondrial permeability transition pore opening CC (PubMed:25613378). Cells display impaired mitochondrial uncoupling CC (PubMed:31341297). Cells show impaired autophagy, leading to CC accumulation of aberrant mitochondria (PubMed:31618756). Mice lacking CC Slc25a4/Ant1 and Slc25a5/Ant2 in liver still have mitochondrial CC permeability transition pore (mPTP) activity, although more Ca(2+) is CC required to activate the mPTP (PubMed:14749836). Deletion of CC Slc25a4/Ant1, Slc25a5/Ant2 and Slc25a31/Ant4 in liver completely CC inhibits mPTP (PubMed:31489369). Mice lacking Slc25a4/Ant1, CC Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack Ca(2+)-induced mPTP formation CC (PubMed:31489369). {ECO:0000269|PubMed:14749836, CC ECO:0000269|PubMed:25613378, ECO:0000269|PubMed:31341297, CC ECO:0000269|PubMed:31489369, ECO:0000269|PubMed:31618756}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {ECO:0000305}. CC -!- CAUTION: It is unclear if SLC25A4/ANT1 constitutes a pore-forming CC component of mitochondrial permeability transition pore (mPTP) CC (PubMed:14749836, PubMed:31489369). Initial reports, based on deletion CC of Slc25a4/Ant1 and Slc25a5/Ant2, suggested that ADP/ATP translocase CC rather acts as a regulator of mPTP (PubMed:14749836). However, deletion CC of all ADP/ATP translocase components (Slc25a4/Ant1, Slc25a5/Ant2 and CC Slc25a31/Ant4) completely inhibits mPTP, suggesting that ADP/ATP CC translocase constitutes a pore-forming component of mPTP CC (PubMed:31489369). Discrepancy between reports may be caused by CC overexpression of Slc25a31/Ant4 in mice lacking Slc25a4/Ant1 and CC Slc25a5/Ant2, which compensates for the loss of Slc25a4/Ant1 and CC Slc25a5/Ant2 (PubMed:31489369). {ECO:0000269|PubMed:14749836, CC ECO:0000269|PubMed:31489369}. 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; U27316; AAC52838.1; -; mRNA. DR EMBL; U10404; AAA19009.1; -; mRNA. DR EMBL; X70847; CAA50196.1; -; mRNA. DR EMBL; AF240003; AAF64471.1; -; Genomic_DNA. DR EMBL; BC004570; AAH04570.1; -; mRNA. DR EMBL; BC086756; AAH86756.1; -; mRNA. DR CCDS; CCDS30062.1; -. DR PIR; S31814; S31814. DR RefSeq; NP_031477.1; NM_007451.4. DR AlphaFoldDB; P51881; -. DR SMR; P51881; -. DR BioGRID; 198106; 48. DR DIP; DIP-31399N; -. DR IntAct; P51881; 27. DR MINT; P51881; -. DR STRING; 10090.ENSMUSP00000016463; -. DR MoonProt; P51881; -. DR GlyGen; P51881; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P51881; -. DR PhosphoSitePlus; P51881; -. DR SwissPalm; P51881; -. DR EPD; P51881; -. DR jPOST; P51881; -. DR PaxDb; 10090-ENSMUSP00000016463; -. DR PeptideAtlas; P51881; -. DR ProteomicsDB; 296119; -. DR Pumba; P51881; -. DR TopDownProteomics; P51881; -. DR Antibodypedia; 29785; 131 antibodies from 24 providers. DR DNASU; 11740; -. DR Ensembl; ENSMUST00000016463.4; ENSMUSP00000016463.4; ENSMUSG00000016319.4. DR GeneID; 11740; -. DR KEGG; mmu:11740; -. DR UCSC; uc009sxs.1; mouse. DR AGR; MGI:1353496; -. DR CTD; 292; -. DR MGI; MGI:1353496; Slc25a5. DR VEuPathDB; HostDB:ENSMUSG00000016319; -. DR eggNOG; KOG0749; Eukaryota. DR GeneTree; ENSGT00940000154400; -. DR HOGENOM; CLU_015166_12_0_1; -. DR InParanoid; P51881; -. DR OMA; GYAMWMV; -. DR OrthoDB; 1330359at2759; -. DR PhylomeDB; P51881; -. DR TreeFam; TF300743; -. DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane. DR BioGRID-ORCS; 11740; 9 hits in 73 CRISPR screens. DR ChiTaRS; Slc25a5; mouse. DR PRO; PR:P51881; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; P51881; Protein. DR Bgee; ENSMUSG00000016319; Expressed in hair follicle and 269 other cell types or tissues. DR ExpressionAtlas; P51881; baseline and differential. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0045121; C:membrane raft; ISO:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI. DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IMP:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0071817; C:MMXD complex; ISS:UniProtKB. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; ISO:MGI. DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:UniProtKB. DR GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; IDA:UniProtKB. DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:1990845; P:adaptive thermogenesis; IMP:UniProtKB. DR GO; GO:0051503; P:adenine nucleotide transport; ISO:MGI. DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IDA:UniProtKB. DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IDA:UniProtKB. DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB. DR GO; GO:1901526; P:positive regulation of mitophagy; IDA:UniProtKB. DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB. DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 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; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1. DR PANTHER; PTHR45635:SF3; ADP_ATP TRANSLOCASE 2; 1. DR Pfam; PF00153; Mito_carr; 3. DR PRINTS; PR00927; ADPTRNSLCASE. DR PRINTS; PR00926; MITOCARRIER. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50920; SOLCAR; 3. DR Genevisible; P51881; MM. PE 1: Evidence at protein level; KW Acetylation; Antiport; Chromosome partition; Direct protein sequencing; KW Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane; KW Phosphoprotein; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..298 FT /note="ADP/ATP translocase 2" FT /id="PRO_0000423221" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..298 FT /note="ADP/ATP translocase 2, N-terminally processed" FT /id="PRO_0000090580" 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 /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P02722" FT BINDING 92 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P02722" FT BINDING 235 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P02722" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P05141" FT MOD_RES 2 FT /note="N-acetylthreonine; in ADP/ATP translocase 2, N- FT terminally processed" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q09073" FT MOD_RES 23 FT /note="N6-malonyllysine" FT /evidence="ECO:0000250" FT MOD_RES 43 FT /note="N6-succinyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 52 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05141" FT MOD_RES 52 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05141" FT MOD_RES 52 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05141" FT MOD_RES 92 FT /note="N6-malonyllysine" FT /evidence="ECO:0000250" FT MOD_RES 96 FT /note="N6-malonyllysine" FT /evidence="ECO:0000250" FT MOD_RES 105 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753, FT ECO:0007744|PubMed:23806337" FT MOD_RES 105 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 147 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 147 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250" FT MOD_RES 147 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P05141" FT MOD_RES 147 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 155 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 155 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 163 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 166 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 268 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23576753" FT MOD_RES 268 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" SQ SEQUENCE 298 AA; 32931 MW; 0798E04B987EFE20 CRC64; MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW RYFAGNLASG GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFKGLGDC LVKIYKSDGI KGLYQGFNVS VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI FISWMIAQSV TAVAGLTSYP FDTVRRRMMM QSGRKGTDIM YTGTLDCWRK IARDEGSKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT //