ADT2_SOLTU
ID ADT2_SOLTU Reviewed; 386 AA.
AC P27081;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 109.
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; Fragment;
GN Name=ANT1; Synonyms=AAC;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Desiree; TISSUE=Tuber;
RX PubMed=1302631; DOI=10.1111/j.1365-313x.1992.tb00145.x;
RA Winning B.M., Sarah C.J., Purdue P.E., Day C.D., Leaver C.J.;
RT "The adenine nucleotide translocator of higher plants is synthesized as a
RT large precursor that is processed upon import into mitochondria.";
RL Plant J. 2:763-773(1992).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57557; CAA40782.1; -; mRNA.
DR PIR; S14874; S14874.
DR AlphaFoldDB; P27081; -.
DR SMR; P27081; -.
DR STRING; 4113.PGSC0003DMT400081472; -.
DR PRIDE; P27081; -.
DR EnsemblPlants; RHC01H1G1004.2.1; RHC01H1G1004.2.1; RHC01H1G1004.2.
DR Gramene; RHC01H1G1004.2.1; RHC01H1G1004.2.1; RHC01H1G1004.2.
DR eggNOG; KOG0749; Eukaryota.
DR InParanoid; P27081; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P27081; 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 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..76
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 77..386
FT /note="ADP,ATP carrier protein, mitochondrial"
FT /id="PRO_0000019252"
FT TRANSMEM 85..112
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 153..177
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 186..206
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 257..278
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 292..312
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 352..372
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 83..176
FT /note="Solcar 1"
FT REPEAT 188..281
FT /note="Solcar 2"
FT REPEAT 289..375
FT /note="Solcar 3"
FT REGION 316..321
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 316..321
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 158
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 170
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 316
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT NON_TER 1
SQ SEQUENCE 386 AA; 41829 MW; FF08A500ECDFBB93 CRC64;
ADNQHPTVYQ KVASQMHLSS SLSQDVHARY GGIQRPALSQ RRFPYGNYSN AGLQTCQATQ
DLSLIAANAS PVFVQAPQEK GLAAFATDFL MGGVSAAVSK TAAAPIERVK LLIQNQDEMI
KAGRLSEPYK GIGDCFSRTI KDEGFAALWR GNTANVIRYF PTQALNFAFK DYFKRLFNFK
KDRDGYWKWF AGNLASGGGA GASSLLFVYS LDYARTRLAN DAKAAKKGGG GRQFDGLVDV
YRKTLKSDGV AGLYRGFNIS CVGIIVYRGL YFGMYDSLKP VLLTGKMEDS FFASFALGWL
ITNGAGLASY PIDTVRRRMM MTSGEAVKYK SSFDAFNQIL KNEGPKSLFK GAGANVLRAV
AGAGVLAGYD KLQVIVFGKK YGSGGG
