ADT_ORYSJ
ID ADT_ORYSJ Reviewed; 382 AA.
AC P31691; Q6ZGX0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ADP,ATP carrier protein, mitochondrial;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
DE Flags: Precursor;
GN OrderedLocusNames=Os02g0718900, LOC_Os02g48720; ORFNames=OJ2056_H01.33;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Yamahoushi;
RX PubMed=8499614; DOI=10.1007/bf00039005;
RA Hashimoto H., Uchimiya H., Kato A.;
RT "Isolation and characterization of a rice cDNA clone encoding ATP/ADP
RT translocator.";
RL Plant Mol. Biol. 22:163-164(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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:0000250|UniProtKB:P31167}; 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; D12637; BAA02161.1; -; mRNA.
DR EMBL; AP004098; BAD12908.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80629.1; -; Genomic_DNA.
DR PIR; S33630; S33630.
DR RefSeq; XP_015625645.1; XM_015770159.1.
DR AlphaFoldDB; P31691; -.
DR SMR; P31691; -.
DR STRING; 4530.OS02T0718900-01; -.
DR PaxDb; P31691; -.
DR PRIDE; P31691; -.
DR EnsemblPlants; Os02t0718900-01; Os02t0718900-01; Os02g0718900.
DR EnsemblPlants; Os02t0718900-02; Os02t0718900-02; Os02g0718900.
DR GeneID; 4330539; -.
DR Gramene; Os02t0718900-01; Os02t0718900-01; Os02g0718900.
DR Gramene; Os02t0718900-02; Os02t0718900-02; Os02g0718900.
DR KEGG; osa:4330539; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; P31691; -.
DR OMA; GYGKWLA; -.
DR OrthoDB; 870903at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; P31691; baseline and differential.
DR Genevisible; P31691; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IBA:GO_Central.
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:0009409; P:response to cold; TAS:AgBase.
DR GO; GO:0009651; P:response to salt stress; TAS:AgBase.
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 2: Evidence at transcript level;
KW Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..71
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 72..382
FT /note="ADP,ATP carrier protein, mitochondrial"
FT /id="PRO_0000019250"
FT TRANSMEM 82..109
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 150..174
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 183..203
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 253..274
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 288..308
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 348..368
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 80..173
FT /note="Solcar 1"
FT REPEAT 185..277
FT /note="Solcar 2"
FT REPEAT 285..371
FT /note="Solcar 3"
FT REGION 312..317
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 312..317
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 155
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 167
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 312
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 382 AA; 41511 MW; 8AE5C543489A4A69 CRC64;
MAEQANQPTV LQKFGGQFHL GSSFSEGVRA RNICPSVSSY DRRFTTRSYM TQGLVNGGIN
VPMMSSSPIF ANAPAEKGGK NFMIDFLMGG VSAAVSKTAA APIERVKLLI QNQDEMIKAG
RLSEPYKGIG DCFGRTIKDE GFASLWRGNT ANVIRYFPTQ ALNFAFKDYF KRLFNFKKDK
DGYWKWFGGN LASGGAAGAS SLFFVYSLDY ARTRLANDAK AAKGGGERQF NGLVDVYRKT
LKSDGIAGLY RGFNISCVGI IVYRGLYFGM YDSLKPVVLT GSLQDNFFAS FALGWLITNG
AGLASYPIDT VRRRMMMTSG EAVKYKSSMD AFSQILKNEG AKSLFKGAGA NILRAIAGAG
VLSGYDQLQI LFFGKKYGSG GA
