ADT3_HUMAN
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 03-AUG-2022, entry version 236.
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. 294:11654-11664(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 -!- 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}.
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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 AlphaFoldDB; P12236; -.
DR SMR; P12236; -.
DR BioGRID; 106790; 352.
DR IntAct; P12236; 164.
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 GlyGen; P12236; 1 site, 1 O-linked glycan (1 site).
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; 295 antibodies from 30 providers.
DR DNASU; 293; -.
DR Ensembl; ENST00000381401.11; ENSP00000370808.5; ENSG00000169100.14.
DR GeneID; 293; -.
DR KEGG; hsa:293; -.
DR MANE-Select; ENST00000381401.11; ENSP00000370808.5; NM_001636.4; NP_001627.2.
DR CTD; 293; -.
DR DisGeNET; 293; -.
DR GeneCards; SLC25A6; -.
DR HGNC; HGNC:10992; SLC25A6.
DR HPA; ENSG00000169100; Low tissue specificity.
DR MIM; 300151; gene.
DR MIM; 403000; gene.
DR neXtProt; NX_P12236; -.
DR OpenTargets; ENSG00000169100; -.
DR PharmGKB; PA35868; -.
DR VEuPathDB; HostDB:ENSG00000169100; -.
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 SignaLink; P12236; -.
DR BioGRID-ORCS; 293; 10 hits in 580 CRISPR screens.
DR ChiTaRS; SLC25A6; human.
DR GeneWiki; SLC25A6; -.
DR GenomeRNAi; 293; -.
DR Pharos; P12236; Tchem.
DR PRO; PR:P12236; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P12236; protein.
DR Bgee; ENSG00000169100; Expressed in cartilage tissue and 210 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; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IBA:GO_Central.
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 /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: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
