ADT2_MAIZE
ID ADT2_MAIZE Reviewed; 387 AA.
AC P12857;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ADP,ATP carrier protein 2, mitochondrial;
DE AltName: Full=ADP/ATP translocase 2;
DE AltName: Full=Adenine nucleotide translocator 2;
DE Short=ANT 2;
DE Flags: Precursor;
GN Name=ANT2; Synonyms=ANT-G2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. MUTIND-FR7205034;
RX PubMed=1863785; DOI=10.1007/bf00039511;
RA Winning B.M., Day C.D., Sarah C.J., Leaver C.J.;
RT "Nucleotide sequence of two cDNAs encoding the adenine nucleotide
RT translocator from Zea mays L.";
RL Plant Mol. Biol. 17:305-307(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-387.
RC STRAIN=cv. B37N;
RX PubMed=2547608; DOI=10.1111/j.1432-1033.1989.tb14929.x;
RA Leaver C.J., Bathgate B., Baker A.;
RT "Two genes encode the adenine nucleotide translocator of maize
RT mitochondria. Isolation, characterisation and expression of the structural
RT genes.";
RL Eur. J. Biochem. 183:303-310(1989).
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; X59086; CAA41812.1; -; mRNA.
DR EMBL; X15712; CAA33743.1; -; Genomic_DNA.
DR PIR; S16568; S16568.
DR RefSeq; NP_001105434.1; NM_001111964.1.
DR RefSeq; XP_008677791.1; XM_008679569.1.
DR AlphaFoldDB; P12857; -.
DR SMR; P12857; -.
DR STRING; 4577.GRMZM2G135186_P03; -.
DR PaxDb; P12857; -.
DR PRIDE; P12857; -.
DR EnsemblPlants; Zm00001eb189380_T001; Zm00001eb189380_P001; Zm00001eb189380.
DR EnsemblPlants; Zm00001eb189380_T003; Zm00001eb189380_P003; Zm00001eb189380.
DR EnsemblPlants; Zm00001eb189380_T004; Zm00001eb189380_P004; Zm00001eb189380.
DR GeneID; 542389; -.
DR Gramene; Zm00001eb189380_T001; Zm00001eb189380_P001; Zm00001eb189380.
DR Gramene; Zm00001eb189380_T003; Zm00001eb189380_P003; Zm00001eb189380.
DR Gramene; Zm00001eb189380_T004; Zm00001eb189380_P004; Zm00001eb189380.
DR KEGG; zma:542389; -.
DR MaizeGDB; 17145; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_1_1; -.
DR OMA; GYGKWLA; -.
DR OrthoDB; 870903at2759; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; P12857; baseline and differential.
DR Genevisible; P12857; ZM.
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 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..77
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 78..387
FT /note="ADP,ATP carrier protein 2, mitochondrial"
FT /id="PRO_0000019249"
FT TRANSMEM 87..114
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 155..179
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 188..208
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 258..279
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 293..313
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 353..373
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 85..178
FT /note="Solcar 1"
FT REPEAT 190..282
FT /note="Solcar 2"
FT REPEAT 290..376
FT /note="Solcar 3"
FT REGION 317..322
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 317..322
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 160
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 172
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 317
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT CONFLICT 242
FT /note="Y -> I (in Ref. 2; CAA33743)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="A -> G (in Ref. 2; CAA33743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 42333 MW; 020E616DC5EC2664 CRC64;
MADQANQPTV LHKLGGQFHL SSSFSEGVRA RNICPSFSPY ERRFATRNYM TQSLWGPSMS
VSGGINVPVM PTPLFANAPA EKGGKNFMID FMMGGVSAAV SKTAAAPIER VKLLIQNQDE
MIKSGRLSEP YKGIADCFKR TIKDEGFSSL WRGNTANVIR YFPTQALNFA FKDYFKRLFN
FKKDRDGYWK WFAGNLASGG AAGASSLFFV YSLDYARTRL ANDAKAAKGG GDRQFNGLVD
VYRKTLKSDG IAGLYRGFNI SCVGIIVYRG LYFGLYDSIK PVVLTGSLQD NFFASFALGW
LITNGAGLAS YPIDTVRRRM MMTSGEAVKY KSSLDAFQQI LKKEGPKSLF KGAGANILRA
IAGAGVLSGY DQLQILFFGK KYGSGGA
