ADT1_GOSHI
ID ADT1_GOSHI Reviewed; 386 AA.
AC O22342;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=ANT1;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Texas Marker 1; TISSUE=Fiber;
RA Shin H., Brown R.M. Jr.;
RT "Two cDNA sequences for the adenine nucleotide translocator, CANT1 and
RT CANT2, from cotton fibers (Gossypium hirsutum).";
RL (er) Plant Gene Register PGR97-130(1997).
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; AF006489; AAB72047.1; -; mRNA.
DR PIR; T09709; T09709.
DR RefSeq; NP_001314189.1; NM_001327260.1.
DR AlphaFoldDB; O22342; -.
DR SMR; O22342; -.
DR PRIDE; O22342; -.
DR GeneID; 107926278; -.
DR KEGG; ghi:107926278; -.
DR Proteomes; UP000189702; Genome assembly.
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:0000250"
FT CHAIN 77..386
FT /note="ADP,ATP carrier protein 1, mitochondrial"
FT /id="PRO_0000019247"
FT TRANSMEM 86..113
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 154..178
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 187..207
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 84..177
FT /note="Solcar 1"
FT REPEAT 189..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 159
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 171
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"
SQ SEQUENCE 386 AA; 42093 MW; A05F76C73FECDEE6 CRC64;
MDQVQHPSVM QKVAGQLFRS SHSQDFQGYN GSFRSPALYQ RRAAYGNYSN AALQHPVRAF
GDLSMVPSTA SAICVQAPAE KGFSSFAIDF LMGGVSAAVS KTAAAPIERV KLLIQNQDEM
IKSGRLSEPY KGIGDCFKRT IKDEGFGSLW RGNTANVIRY FPTQALNFAF KDYFKRLFNF
KKDRDGYWKW FAGNLASGGA AGASSLLFVY SLDYARTRLA NDAKAAKKGG ERQFNGLVDV
YRKTLKSDGI AGLYRGFNIS CVGIIVYRGL YFGMYDSLKP VLLTGSMQDS FFASFVLGWL
ITNGAALASY PIDTVRRRMM MTSGKAVKYK SSLDAFSQIL KNEGGKSLFK GAGSNILRAI
AGAGVLAGYD KLQLIVFGKK YGSGGA
