ADT_CHLRE
ID ADT_CHLRE Reviewed; 308 AA.
AC P27080;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ADP,ATP carrier protein;
DE AltName: Full=ADP/ATP translocase;
DE AltName: Full=Adenine nucleotide translocator;
DE Short=ANT;
GN Name=ABT;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FUD44-R2;
RX PubMed=8455552; DOI=10.1007/bf00282794;
RA Sharpe J.A., Day A.;
RT "Structure, evolution and expression of the mitochondrial ADP/ATP
RT translocator gene from Chlamydomonas reinhardtii.";
RL Mol. Gen. Genet. 237:134-144(1993).
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; X65194; CAA46311.1; -; mRNA.
DR PIR; S30259; S30259.
DR RefSeq; XP_001695177.1; XM_001695125.1.
DR AlphaFoldDB; P27080; -.
DR SMR; P27080; -.
DR STRING; 3055.EDP01885; -.
DR PRIDE; P27080; -.
DR ProMEX; P27080; -.
DR EnsemblPlants; PNW78206; PNW78206; CHLRE_09g386650v5.
DR EnsemblPlants; PNW78207; PNW78207; CHLRE_09g386650v5.
DR GeneID; 5720839; -.
DR Gramene; PNW78206; PNW78206; CHLRE_09g386650v5.
DR Gramene; PNW78207; PNW78207; CHLRE_09g386650v5.
DR KEGG; cre:CHLRE_09g386650v5; -.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR OMA; NTHIMIS; -.
DR OrthoDB; 870903at2759; -.
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 2: Evidence at transcript level;
KW Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..308
FT /note="ADP,ATP carrier protein"
FT /id="PRO_0000090588"
FT TRANSMEM 8..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 76..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 179..200
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 214..234
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 274..294
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 6..99
FT /note="Solcar 1"
FT REPEAT 110..203
FT /note="Solcar 2"
FT REPEAT 211..297
FT /note="Solcar 3"
FT REGION 238..243
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 238..243
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 81
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 93
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 238
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 308 AA; 33528 MW; D477CF0E72B7A53F CRC64;
MAKEEKNFMV DFLAGGLSAA VSKTAAAPIE RVKLLIQNQD EMIKQGRLAS PYKGIGECFV
RTVREEGFGS LWRGNTANVI RYFPTQALNF AFKDKFKRMF GFNKDKEYWK WFAGNMASGG
AAGAVSLSFV YSLDYARTRL ANDAKSAKKG GGDRQFNGLV DVYRKTIASD GIAGLYRGFN
ISCVGIVVYR GLYFGMYDSL KPVVLVGPLA NNFLAAFLLG WGITIGAGLA SYPIDTIRRR
MMMTSGSAVK YNSSFHCFQE IVKNEGMKSL FKGAGANILR AVAGAGVLAG YDQLQVILLG
KKYGSGEA
