ADT1_WHEAT
ID ADT1_WHEAT Reviewed; 331 AA.
AC Q41629;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=ANT-G1;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RA Iacobazzi V., Poli A., Blanco A., Palmieri F.;
RT "Nucleotide sequences of two genes (ANT-G1 and ANT-G2) encoding the adenine
RT nucleotide translocator of wheat mitochondria.";
RL (er) Plant Gene Register PGR96-016(1996).
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; X95863; CAA65119.1; -; Genomic_DNA.
DR AlphaFoldDB; Q41629; -.
DR SMR; Q41629; -.
DR STRING; 4565.Traes_6BL_53A305F99.2; -.
DR PRIDE; Q41629; -.
DR eggNOG; KOG0749; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q41629; baseline and differential.
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 3: Inferred from homology;
KW Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..331
FT /note="ADP,ATP carrier protein 1, mitochondrial"
FT /id="PRO_0000019253"
FT TRANSMEM 31..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 99..123
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 132..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 202..223
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 297..317
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 29..122
FT /note="Solcar 1"
FT REPEAT 134..226
FT /note="Solcar 2"
FT REPEAT 238..320
FT /note="Solcar 3"
FT REGION 261..266
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 261..266
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 104
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 116
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 261
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 331 AA; 35962 MW; D0C9464DD43AEAF3 CRC64;
MTQNLGISVP IMSPSPMFAN APPEKKGVKN FAIDFLMGGV SAAVSKTAAA PIERVKLLIQ
NQDEMIKAGR LSEPYKGIGD CFGRTIKDEG FGSLWRGNTA NVIRYFPTQA LNFAFKDYFK
RMFNFKKDKD GYWKWFGGNL ASGGAAGASS LFFVYSLDYA RTRLANDAKA SKGGGERQFN
GLVDVYRKTL KSDGIAGLYR GFNISCVGII VYRGLYFGLY DSLKPVLLTG TLQVCFFASF
ALGWLITNGA GLASYPIDTV RRRMMMTSGE AVKYKSSLDA FQQILKKEGA KSLFKGAGAN
ILRAIAGAGV LSGYDQLQIL FFGKKYGSGG A
