ID   ADT2_ARATH              Reviewed;         385 AA.
AC   P40941; Q9FY52;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=ADP/ATP translocase 2, mitochondrial {ECO:0000305};
DE   AltName: Full=ADP,ATP carrier protein 2 {ECO:0000305};
DE   AltName: Full=Adenine nucleotide translocator 2;
DE            Short=ANT 2;
DE   Flags: Precursor;
GN   Name=AAC2; Synonyms=ANT2; OrderedLocusNames=At5g13490;
GN   ORFNames=T6I14_20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=8439563; DOI=10.1016/0167-4781(93)90296-p;
RA   Schuster W., Kloska S., Brennicke A.;
RT   "An adenine nucleotide translocator gene from Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1172:205-208(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA   Picault N., Hodges M., Palmieri L., Palmieri F.;
RT   "The growing family of mitochondrial carriers in Arabidopsis.";
RL   Trends Plant Sci. 9:138-146(2004).
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).
CC       {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P48962}.
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   -!- 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). {ECO:0000250|UniProtKB:G2QNH0}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC       ECO:0000250|UniProtKB:P02722}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14671022}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC       the membrane, but cross the membrane at an angle. At least 2 of the
CC       odd-numbered transmembrane helices exhibit a sharp kink, due to the
CC       presence of a conserved proline residue.
CC       {ECO:0000250|UniProtKB:P18239}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; X68592; CAA48579.1; -; mRNA.
DR   EMBL; AL391710; CAC05426.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91901.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91902.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7052109.1; -; Genomic_DNA.
DR   EMBL; AY050857; AAK92794.1; -; mRNA.
DR   EMBL; AY079407; AAL85138.1; -; mRNA.
DR   PIR; S29852; S29852.
DR   RefSeq; NP_001031876.1; NM_001036799.2.
DR   RefSeq; NP_196853.1; NM_121352.4.
DR   AlphaFoldDB; P40941; -.
DR   SMR; P40941; -.
DR   BioGRID; 16471; 38.
DR   FunCoup; P40941; 2269.
DR   IntAct; P40941; 2.
DR   STRING; 3702.P40941; -.
DR   SwissPalm; P40941; -.
DR   PaxDb; 3702-P40941; -.
DR   ProteomicsDB; 244649; -.
DR   DNASU; 831193; -.
DR   GeneID; 831193; -.
DR   KEGG; ath:AT5G13490; -.
DR   Araport; AT5G13490; -.
DR   TAIR; AT5G13490; AAC2.
DR   eggNOG; KOG0749; Eukaryota.
DR   HOGENOM; CLU_015166_12_1_1; -.
DR   InParanoid; P40941; -.
DR   OMA; PVHERQY; -.
DR   OrthoDB; 270584at2759; -.
DR   PhylomeDB; P40941; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:P40941; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P40941; baseline and differential.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005740; C:mitochondrial envelope; TAS:TAIR.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005757; C:mitochondrial permeability transition pore complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
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:0015865; P:purine nucleotide transport; IDA:TAIR.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IBA:GO_Central.
DR   FunFam; 1.50.40.10:FF:000001; ADP,ATP carrier protein, mitochondrial; 1.
DR   Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1.
DR   InterPro; IPR002113; ADT_euk_type.
DR   InterPro; IPR002067; MCP.
DR   InterPro; IPR023395; MCP_dom_sf.
DR   InterPro; IPR018108; MCP_transmembrane.
DR   PANTHER; PTHR45635; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 1.
DR   PANTHER; PTHR45635:SF52; ADP,ATP CARRIER PROTEIN 2, MITOCHONDRIAL; 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.
PE   1: Evidence at protein level;
KW   Antiport; ATP-binding; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW   Repeat; Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..74
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           75..385
FT                   /note="ADP/ATP translocase 2, mitochondrial"
FT                   /id="PRO_0000019246"
FT   TRANSMEM        84..111
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        152..176
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        185..205
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        256..277
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        291..311
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        351..371
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   REPEAT          82..175
FT                   /note="Solcar 1"
FT   REPEAT          187..280
FT                   /note="Solcar 2"
FT   REPEAT          288..374
FT                   /note="Solcar 3"
FT   REGION          315..320
FT                   /note="Important for transport activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12235"
FT   MOTIF           315..320
FT                   /note="Nucleotide carrier signature motif"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         157
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         169
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         315
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   CONFLICT        228
FT                   /note="G -> R (in Ref. 1; CAA48579)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   385 AA;  41746 MW;  87ADF762213207BA CRC64;
     MVEQTQHPTI LQKVSGQLLS SSVSQDIRGY ASASKRPATY QKHAAYGNYS NAAFQYPLVA
     ASQIATTTSP VFVQAPGEKG FTNFAIDFMM GGVSAAVSKT AAAPIERVKL LIQNQDEMLK
     AGRLTEPYKG IRDCFGRTIR DEGIGSLWRG NTANVIRYFP TQALNFAFKD YFKRLFNFKK
     DKDGYWKWFA GNLASGGAAG ASSLLFVYSL DYARTRLAND SKSAKKGGGE RQFNGLVDVY
     KKTLKSDGIA GLYRGFNISC AGIIVYRGLY FGLYDSVKPV LLTGDLQDSF FASFALGWLI
     TNGAGLASYP IDTVRRRMMM TSGEAVKYKS SFDAFSQIVK KEGAKSLFKG AGANILRAVA
     GAGVLAGYDK LQLIVFGKKY GSGGA
//