ADT2_MOUSE
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 03-AUG-2022, entry version 192.
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},
GN Ant2 {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, Pancreas,
RC 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}.
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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; 42.
DR DIP; DIP-31399N; -.
DR IntAct; P51881; 27.
DR MINT; P51881; -.
DR STRING; 10090.ENSMUSP00000016463; -.
DR iPTMnet; P51881; -.
DR PhosphoSitePlus; P51881; -.
DR SwissPalm; P51881; -.
DR EPD; P51881; -.
DR jPOST; P51881; -.
DR PaxDb; P51881; -.
DR PeptideAtlas; P51881; -.
DR PRIDE; P51881; -.
DR ProteomicsDB; 296119; -.
DR TopDownProteomics; P51881; -.
DR Antibodypedia; 29785; 113 antibodies from 24 providers.
DR DNASU; 11740; -.
DR Ensembl; ENSMUST00000016463; ENSMUSP00000016463; ENSMUSG00000016319.
DR GeneID; 11740; -.
DR KEGG; mmu:11740; -.
DR UCSC; uc009sxs.1; mouse.
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; AYQRQYK; -.
DR OrthoDB; 870903at2759; -.
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 68 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 267 other tissues.
DR ExpressionAtlas; P51881; baseline and differential.
DR Genevisible; P51881; MM.
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; -; 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; 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
