ADT3_YEAST
ID ADT3_YEAST Reviewed; 307 AA.
AC P18238; D6VQ85;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=ADP,ATP carrier protein 3;
DE AltName: Full=ADP/ATP translocase 3;
DE AltName: Full=Adenine nucleotide translocator 3;
DE Short=ANT 3;
GN Name=AAC3; OrderedLocusNames=YBR085W; ORFNames=YBR0753;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2165073; DOI=10.1016/s0021-9258(19)38402-9;
RA Kolarov J., Kolarova N., Nelson N.;
RT "A third ADP/ATP translocator gene in yeast.";
RL J. Biol. Chem. 265:12711-12716(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5] {ECO:0007744|PDB:4C9J, ECO:0007744|PDB:4C9Q}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 3-307 IN COMPLEX WITH
RP CARBOXYATRACTYLOSIDE, AND TOPOLOGY.
RX PubMed=24474793; DOI=10.1073/pnas.1320692111;
RA Ruprecht J.J., Hellawell A.M., Harding M., Crichton P.G., McCoy A.J.,
RA Kunji E.R.;
RT "Structures of yeast mitochondrial ADP/ATP carriers support a domain-based
RT alternating-access transport mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E426-E434(2014).
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:2165073). 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:2165073}.
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:0000305|PubMed:2165073};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000305|PubMed:2165073};
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 -!- INTERACTION:
CC P18238; P18238: AAC3; NbExp=2; IntAct=EBI-2300, EBI-2300;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24474793}.
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:G2QNH0}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; M34076; AAA97485.1; -; Genomic_DNA.
DR EMBL; Z35954; CAA85031.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07205.1; -; Genomic_DNA.
DR PIR; A36582; A36582.
DR RefSeq; NP_009642.3; NM_001178433.3.
DR PDB; 4C9J; X-ray; 3.40 A; A/B=3-307.
DR PDB; 4C9Q; X-ray; 3.20 A; A/B=3-307.
DR PDBsum; 4C9J; -.
DR PDBsum; 4C9Q; -.
DR AlphaFoldDB; P18238; -.
DR BMRB; P18238; -.
DR SMR; P18238; -.
DR BioGRID; 32790; 206.
DR DIP; DIP-6289N; -.
DR IntAct; P18238; 20.
DR MINT; P18238; -.
DR STRING; 4932.YBR085W; -.
DR TCDB; 2.A.29.1.9; the mitochondrial carrier (mc) family.
DR MaxQB; P18238; -.
DR PaxDb; P18238; -.
DR PRIDE; P18238; -.
DR DNASU; 852380; -.
DR EnsemblFungi; YBR085W_mRNA; YBR085W; YBR085W.
DR GeneID; 852380; -.
DR KEGG; sce:YBR085W; -.
DR SGD; S000000289; AAC3.
DR VEuPathDB; FungiDB:YBR085W; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000176325; -.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; P18238; -.
DR OMA; GYGKWLA; -.
DR BioCyc; YEAST:G3O-29052-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR Reactome; R-SCE-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR PRO; PR:P18238; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18238; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; ISA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009061; P:anaerobic respiration; IGI:SGD.
DR GO; GO:0015886; P:heme transport; IMP:SGD.
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:0055085; P:transmembrane transport; ISA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Antiport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..307
FT /note="ADP,ATP carrier protein 3"
FT /id="PRO_0000090595"
FT TRANSMEM 12..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 80..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 182..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 217..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 277..297
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 10..103
FT /note="Solcar 1"
FT REPEAT 114..206
FT /note="Solcar 2"
FT REPEAT 214..300
FT /note="Solcar 3"
FT REGION 241..246
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 241..246
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 85
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT BINDING 97
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT BINDING 241
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT HELIX 5..29
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 79..104
FT /evidence="ECO:0007829|PDB:4C9Q"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4C9J"
FT HELIX 112..146
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:4C9Q"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 182..202
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 217..233
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:4C9Q"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:4C9Q"
FT HELIX 277..301
FT /evidence="ECO:0007829|PDB:4C9Q"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:4C9J"
SQ SEQUENCE 307 AA; 33313 MW; D0C1329FEC1B4DC8 CRC64;
MSSDAKQQET NFAINFLMGG VSAAIAKTAA SPIERVKILI QNQDEMIKQG TLDKKYSGIV
DCFKRTAKQE GLISFWRGNT ANVIRYFPTQ ALNFAFKDKI KLMFGFKKEE GYGKWFAGNL
ASGGAAGALS LLFVYSLDFA RTRLAADAKS SKKGGARQFN GLTDVYKKTL KSDGIAGLYR
GFMPSVVGIV VYRGLYFGMF DSLKPLVLTG SLDGSFLASF LLGWVVTTGA STCSYPLDTV
RRRMMMTSGQ AVKYNGAIDC LKKIVASEGV GSLFKGCGAN ILRSVAGAGV ISMYDQLQMI
LFGKKFK
