ADT5_ARATH
ID ADT5_ARATH Reviewed; 330 AA.
AC Q9FM86; Q8LFZ1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable ADP,ATP carrier protein At5g56450;
DE AltName: Full=ADP/ATP translocase At5g56450;
DE AltName: Full=Adenine nucleotide translocator At5g56450;
GN OrderedLocusNames=At5g56450; ORFNames=MCD7.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=15003237; DOI=10.1016/j.tplants.2004.01.007;
RA Picault N., Hodges M., Palmieri L., Palmieri F.;
RT "The growing family of mitochondrial carriers in Arabidopsis.";
RL Trends Plant Sci. 9:138-146(2004).
CC -!- FUNCTION: ADP:ATP antiporter that catalyzes the exchange of ADP and ATP
CC across the membrane. {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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P02722}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: The transmembrane helices are not perpendicular to the
CC plane of the membrane, but cross the membrane at an angle. At least 2
CC of the odd-numbered transmembrane helices exhibit a sharp kink, due to
CC the presence of a conserved proline residue (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; AB009049; BAB11273.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96766.1; -; Genomic_DNA.
DR EMBL; BT025880; ABF85782.1; -; mRNA.
DR EMBL; AY084555; AAM61122.1; -; mRNA.
DR RefSeq; NP_200456.1; NM_125028.1.
DR AlphaFoldDB; Q9FM86; -.
DR SMR; Q9FM86; -.
DR STRING; 3702.AT5G56450.1; -.
DR PaxDb; Q9FM86; -.
DR PRIDE; Q9FM86; -.
DR ProteomicsDB; 244797; -.
DR EnsemblPlants; AT5G56450.1; AT5G56450.1; AT5G56450.
DR GeneID; 835746; -.
DR Gramene; AT5G56450.1; AT5G56450.1; AT5G56450.
DR KEGG; ath:AT5G56450; -.
DR Araport; AT5G56450; -.
DR TAIR; locus:2161083; AT5G56450.
DR eggNOG; KOG0749; Eukaryota.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; Q9FM86; -.
DR OMA; AHCWLVI; -.
DR OrthoDB; 870903at2759; -.
DR PhylomeDB; Q9FM86; -.
DR PRO; PR:Q9FM86; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FM86; baseline and differential.
DR Genevisible; Q9FM86; AT.
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:0005347; F:ATP transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IBA:GO_Central.
DR GO; GO:0048653; P:anther development; IMP:TAIR.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IEA:InterPro.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IBA:GO_Central.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; 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; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..330
FT /note="Probable ADP,ATP carrier protein At5g56450"
FT /id="PRO_0000410474"
FT TRANSMEM 27..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..127
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TRANSMEM 137..171
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TRANSMEM 203..230
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TRANSMEM 236..270
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..325
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT REPEAT 28..126
FT /note="Solcar 1"
FT REPEAT 139..228
FT /note="Solcar 2"
FT REPEAT 241..324
FT /note="Solcar 3"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..269
FT /note="Substrate recognition"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 120
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 264
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT CONFLICT 178
FT /note="A -> S (in Ref. 4; AAM61122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36931 MW; D8823FC638BCFA22 CRC64;
MCISKEDEED PSRNRRNQSP LSLPQTLKHF QKDLLAGAVM GGVVHTIVAP IERAKLLLQT
QESNIAIVGD EGHAGKRRFK GMFDFIFRTV REEGVLSLWR GNGSSVLRYY PSVALNFSLK
DLYRSILRNS SSQENHIFSG ALANFMAGSA AGCTALIVVY PLDIAHTRLA ADIGKPEARQ
FRGIHHFLST IHKKDGVRGI YRGLPASLHG VIIHRGLYFG GFDTVKEIFS EDTKPELALW
KRWGLAQAVT TSAGLASYPL DTVRRRIMMQ SGMEHPMYRS TLDCWKKIYR SEGLASFYRG
ALSNMFRSTG SAAILVFYDE VKRFLNWGGI
