ID   ADT1_ARATH              Reviewed;         381 AA.
AC   P31167; Q9M9K2;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=ADP,ATP carrier protein 1, mitochondrial;
DE   AltName: Full=ADP/ATP translocase 1;
DE   AltName: Full=Adenine nucleotide translocator 1;
DE            Short=ANT 1;
DE   Flags: Precursor;
GN   Name=AAC1; Synonyms=ANT1; OrderedLocusNames=At3g08580;
GN   ORFNames=F17O14.5;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-381.
RC   STRAIN=cv. Columbia;
RX   PubMed=16653021; DOI=10.1104/pp.100.2.1069;
RA   Saint-Guily A., Lim P.Y., Chevalier C., Yamaguchi J., Akazawa T.;
RT   "Complementary DNA sequence of an adenylate translocator from Arabidopsis
RT   thaliana.";
RL   Plant Physiol. 100:1069-1071(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-190.
RC   STRAIN=cv. Columbia;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
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).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
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; AC012562; AAG51358.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74648.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74649.1; -; Genomic_DNA.
DR   EMBL; AY034933; AAK59440.1; -; mRNA.
DR   EMBL; AY042814; AAK68754.1; -; mRNA.
DR   EMBL; AY054248; AAL06907.1; -; mRNA.
DR   EMBL; AY074529; AAL69497.1; -; mRNA.
DR   EMBL; BT000381; AAN15700.1; -; mRNA.
DR   EMBL; BT002387; AAO00747.1; -; mRNA.
DR   EMBL; X65549; CAA46518.1; -; mRNA.
DR   EMBL; Z26399; CAA81237.1; -; mRNA.
DR   PIR; S21313; S21313.
DR   RefSeq; NP_187470.1; NM_111692.3.
DR   RefSeq; NP_850541.1; NM_180210.2.
DR   AlphaFoldDB; P31167; -.
DR   SMR; P31167; -.
DR   BioGRID; 5340; 48.
DR   IntAct; P31167; 7.
DR   MINT; P31167; -.
DR   STRING; 3702.P31167; -.
DR   TCDB; 2.A.29.1.5; the mitochondrial carrier (mc) family.
DR   iPTMnet; P31167; -.
DR   PaxDb; 3702-AT3G08580-2; -.
DR   ProteomicsDB; 244762; -.
DR   EnsemblPlants; AT3G08580.1; AT3G08580.1; AT3G08580.
DR   EnsemblPlants; AT3G08580.2; AT3G08580.2; AT3G08580.
DR   GeneID; 820005; -.
DR   Gramene; AT3G08580.1; AT3G08580.1; AT3G08580.
DR   Gramene; AT3G08580.2; AT3G08580.2; AT3G08580.
DR   KEGG; ath:AT3G08580; -.
DR   Araport; AT3G08580; -.
DR   TAIR; AT3G08580; AAC1.
DR   eggNOG; KOG0749; Eukaryota.
DR   HOGENOM; CLU_015166_12_1_1; -.
DR   InParanoid; P31167; -.
DR   OMA; NILISWM; -.
DR   OrthoDB; 102867at2759; -.
DR   PhylomeDB; P31167; -.
DR   PRO; PR:P31167; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P31167; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005740; C:mitochondrial envelope; TAS:TAIR.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; 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:0003729; F:mRNA binding; IDA:TAIR.
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:0015865; P:purine nucleotide transport; IDA:TAIR.
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:SF47; ADP,ATP CARRIER PROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45635; ADP,ATP CARRIER PROTEIN 1-RELATED-RELATED; 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; P31167; AT.
PE   1: Evidence at protein level;
KW   Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Repeat; Transit peptide; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..70
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           71..381
FT                   /note="ADP,ATP carrier protein 1, mitochondrial"
FT                   /id="PRO_0000019245"
FT   TRANSMEM        80..107
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        148..172
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        252..273
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        287..307
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   TRANSMEM        347..367
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P18239"
FT   REPEAT          78..171
FT                   /note="Solcar 1"
FT   REPEAT          183..276
FT                   /note="Solcar 2"
FT   REPEAT          284..370
FT                   /note="Solcar 3"
FT   REGION          311..316
FT                   /note="Important for transport activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12235"
FT   MOTIF           311..316
FT                   /note="Nucleotide carrier signature motif"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         153
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         165
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   BINDING         311
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250|UniProtKB:P02722"
FT   CONFLICT        3
FT                   /note="D -> H (in Ref. 4; CAA46518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="G -> N (in Ref. 4; CAA46518)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="Q -> T (in Ref. 4; CAA46518)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41476 MW;  FF39C3D1E1ED5B58 CRC64;
     MVDQVQHPTI AQKAAGQFMR SSVSKDVQVG YQRPSMYQRH ATYGNYSNAA FQFPPTSRML
     ATTASPVFVQ TPGEKGFTNF ALDFLMGGVS AAVSKTAAAP IERVKLLIQN QDEMIKAGRL
     SEPYKGIGDC FGRTIKDEGF GSLWRGNTAN VIRYFPTQAL NFAFKDYFKR LFNFKKDRDG
     YWKWFAGNLA SGGAAGASSL LFVYSLDYAR TRLANDAKAA KKGGGGRQFD GLVDVYRKTL
     KTDGIAGLYR GFNISCVGII VYRGLYFGLY DSVKPVLLTG DLQDSFFASF ALGWVITNGA
     GLASYPIDTV RRRMMMTSGE AVKYKSSLDA FKQILKNEGA KSLFKGAGAN ILRAVAGAGV
     LSGYDKLQLI VFGKKYGSGG A
//