ADT_PARKE
ID ADT_PARKE Reviewed; 339 AA.
AC P31692;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ADP,ATP carrier protein;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
OS Parachlorella kessleri (Green alga) (Chlorella kessleri).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Parachlorella.
OX NCBI_TaxID=3074;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1748677; DOI=10.1016/s0021-9258(18)54389-1;
RA Hilgarth C., Sauer N., Tanner W.;
RT "Glucose increases the expression of the ATP/ADP translocator and the
RT glyceraldehyde-3-phosphate dehydrogenase genes in Chlorella.";
RL J. Biol. Chem. 266:24044-24047(1991).
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 (PubMed:1748677). Cycles between the cytoplasmic-open state
CC (c-state) and the matrix-open state (m-state): operates by the
CC alternating access mechanism with a single substrate-binding site
CC intermittently exposed to either the cytosolic (c-state) or matrix (m-
CC state) side of the inner mitochondrial membrane (By similarity).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000269|PubMed:1748677}.
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. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:P02722}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; M76669; AAA33027.1; -; Genomic_DNA.
DR PIR; A41677; A41677.
DR AlphaFoldDB; P31692; -.
DR SMR; P31692; -.
DR PRIDE; P31692; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IEA:InterPro.
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; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..339
FT /note="ADP,ATP carrier protein"
FT /id="PRO_0000090589"
FT TRANSMEM 41..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 110..134
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 144..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 212..232
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 245..265
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TRANSMEM 305..322
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT REPEAT 39..133
FT /note="Solcar 1"
FT REPEAT 145..234
FT /note="Solcar 2"
FT REPEAT 246..328
FT /note="Solcar 3"
FT REGION 269..274
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 269..274
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 115
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 127
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 269
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 339 AA; 36686 MW; 54779734A33B3942 CRC64;
MLSSALYQQA GLSGLLRASA MGPQTPFIAS PKETQADPMA FVKDLLAGGT AGAISKTAVA
PIERVKLLLQ TQDSNPMIKS GQVPRYTGIV NCFVRVSSEQ GVASFWRGNL ANVVRYFPTQ
AFNFAFKDTI KGLFPKYSPK TDFWRFFVVN LASGGLAGAG SLLIVYPLDF ARTRLAADVG
SGKSREFTGL VDCLSKVVKR GGPMALYQGF GVSVQGIIVY RGAYFGLYDT AKGVLFKDER
TANFFAKWAV AQAVTAGAGV LSYPFDTVRR RLMMQSGGER QYNGTIDCWR KVAQQEGMKA
FFKGAWSNVL RGAGGAFVLV LYDEIKKFIN PNAVSSASE
