ADT2_YEAST
ID ADT2_YEAST Reviewed; 318 AA.
AC P18239; D6VPW9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
DE AltName: Full=Adenine nucleotide translocator 2;
DE Short=ANT 2;
DE AltName: Full=Petite colonies protein 9;
GN Name=PET9; Synonyms=AAC2; OrderedLocusNames=YBL030C; ORFNames=YBL0421;
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].
RX PubMed=2844786; DOI=10.1016/s0021-9258(18)68111-6;
RA Lawson J.E., Douglas M.G.;
RT "Separate genes encode functionally equivalent ADP/ATP carrier proteins in
RT Saccharomyces cerevisiae. Isolation and analysis of AAC2.";
RL J. Biol. Chem. 263:14812-14818(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Trezeguet V., le Saux A., Lauquin G.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7725803; DOI=10.1002/yea.320101217;
RA van Dyck L., Jonniaux J.-L., Barreiros T.D.M., Kleine K., Goffeau A.;
RT "Analysis of a 17.4 kb DNA segment of yeast chromosome II encompassing the
RT ribosomal protein L19 as well as proteins with homologies to components of
RT the hnRNP and snRNP complexes and to the human proliferation-associated
RT p120 antigen.";
RL Yeast 10:1663-1673(1994).
RN [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=795470; DOI=10.1016/s0300-9084(76)80120-4;
RA Lauquin G., Lunardi J., Vignais P.V.;
RT "Effect of genetic and physiological manipulations onthe kinetic and
RT binding parameters of the adenine nucleotide translocator in Saccharomyces
RT cervisiae and Candida utilis.";
RL Biochimie 58:1213-1220(1976).
RN [8]
RP FUNCTION.
RX PubMed=2167309; DOI=10.1016/s0021-9258(18)77287-6;
RA Gawaz M., Douglas M.G., Klingenberg M.;
RT "Structure-function studies of adenine nucleotide transport in
RT mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins
RT in yeast.";
RL J. Biol. Chem. 265:14202-14208(1990).
RN [9]
RP MUTAGENESIS.
RX PubMed=8487299; DOI=10.1006/jmbi.1993.1233;
RA Nelson D.R., Lawson J.E., Klingenberg M., Douglas M.G.;
RT "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator.
RT Six arginines and one lysine are essential.";
RL J. Mol. Biol. 230:1159-1170(1993).
RN [10]
RP TOPOLOGY.
RX PubMed=7683726; DOI=10.1006/jmbi.1993.1234;
RA Nelson D.R., Douglas M.G.;
RT "Function-based mapping of the yeast mitochondrial ADP/ATP translocator by
RT selection for second site revertants.";
RL J. Mol. Biol. 230:1171-1182(1993).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [12] {ECO:0007744|PDB:4C9G, ECO:0007744|PDB:4C9H}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH
RP CARBOXYATRACTYLOSIDE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP TOPOLOGY, AND MUTAGENESIS OF ASP-109; LYS-112; ASP-212; LYS-215; ASP-306
RP AND GLN-309.
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:24474793). 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:24474793}.
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:0000269|PubMed:24474793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000269|PubMed:24474793};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA) (PubMed:24474793). The
CC cytoplasmic-open state (c-state) is inhibited by the membrane-
CC impermeable toxic inhibitor carboxyatractyloside (CATR)
CC (PubMed:24474793). {ECO:0000269|PubMed:24474793}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:795470}; 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. At least 2 of the
CC odd-numbered transmembrane helices exhibit a sharp kink, due to the
CC presence of a conserved proline residue. {ECO:0000269|PubMed:24474793}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; X77291; CAA54501.1; -; Genomic_DNA.
DR EMBL; J04021; AAA34381.1; -; Genomic_DNA.
DR EMBL; M34075; AAA97484.1; -; Genomic_DNA.
DR EMBL; X74427; CAA52446.1; -; Genomic_DNA.
DR EMBL; Z35791; CAA84850.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07089.1; -; Genomic_DNA.
DR PIR; A31978; A31978.
DR RefSeq; NP_009523.1; NM_001178270.1.
DR PDB; 4C9G; X-ray; 2.49 A; A=1-318.
DR PDB; 4C9H; X-ray; 3.20 A; A/B=1-318.
DR PDBsum; 4C9G; -.
DR PDBsum; 4C9H; -.
DR AlphaFoldDB; P18239; -.
DR SMR; P18239; -.
DR BioGRID; 32667; 225.
DR DIP; DIP-2917N; -.
DR IntAct; P18239; 70.
DR MINT; P18239; -.
DR STRING; 4932.YBL030C; -.
DR TCDB; 2.A.29.1.7; the mitochondrial carrier (mc) family.
DR iPTMnet; P18239; -.
DR MaxQB; P18239; -.
DR PaxDb; P18239; -.
DR PRIDE; P18239; -.
DR EnsemblFungi; YBL030C_mRNA; YBL030C; YBL030C.
DR GeneID; 852250; -.
DR KEGG; sce:YBL030C; -.
DR SGD; S000000126; PET9.
DR VEuPathDB; FungiDB:YBL030C; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000176325; -.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; P18239; -.
DR OMA; YDGIVEC; -.
DR BioCyc; YEAST:G3O-28933-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:P18239; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18239; protein.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:UniProtKB.
DR GO; GO:0015866; P:ADP transport; IDA:SGD.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0009061; P:anaerobic respiration; IGI:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0015867; P:ATP transport; IDA: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:0006839; P:mitochondrial transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IDA: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..318
FT /note="ADP,ATP carrier protein 2"
FT /id="PRO_0000090594"
FT TRANSMEM 23..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 91..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 123..143
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 193..214
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 228..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:24474793"
FT TRANSMEM 288..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:24474793"
FT REPEAT 21..114
FT /note="Solcar 1"
FT REPEAT 125..217
FT /note="Solcar 2"
FT REPEAT 225..311
FT /note="Solcar 3"
FT REGION 252..257
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 252..257
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 96
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT BINDING 108
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT BINDING 252
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:24474793"
FT MUTAGEN 109
FT /note="D->K: Loss of transport activity; when associated
FT with K-212 and K-306. Restored transport activity; when
FT associated with D-112; K-212; D-215; K-306 and D-309."
FT /evidence="ECO:0000269|PubMed:24474793"
FT MUTAGEN 112
FT /note="K->D: Loss of transport activity; when associated
FT with D-215 and D-309. Restored transport activity; when
FT associated with K-109; K-212; D-215; K-306 and D-309."
FT /evidence="ECO:0000269|PubMed:24474793"
FT MUTAGEN 212
FT /note="D->K: Loss of transport activity; when associated
FT with K-109 and K-306. Restored transport activity; when
FT associated with D-109; D-112; D-215; K-306 and D-309."
FT /evidence="ECO:0000269|PubMed:24474793"
FT MUTAGEN 215
FT /note="K->D: Loss of transport activity; when associated
FT with D-112 and D-309. Restored transport activity; when
FT associated with K-109; D-112; K-212; K-306 and D-309."
FT /evidence="ECO:0000269|PubMed:24474793"
FT MUTAGEN 306
FT /note="D->K: Loss of transport activity; when associated
FT with K-109 and K-212. Restored transport activity; when
FT associated with D-109; D-112; K-212; D-215 and D-309."
FT /evidence="ECO:0000269|PubMed:24474793"
FT MUTAGEN 309
FT /note="Q->D: Loss of transport activity; when associated
FT with D-112 and D-215. Restored transport activity; when
FT associated with K-109; D-112; K-212; D-215 and K-306."
FT /evidence="ECO:0000269|PubMed:24474793"
FT CONFLICT 58
FT /note="L -> I (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="R -> K (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="A -> S (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="L -> V (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="T -> K (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="V -> L (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> L (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> G (in Ref. 2; AAA97484)"
FT /evidence="ECO:0000305"
FT HELIX 25..52
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 123..156
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:4C9G"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 193..213
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 229..244
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:4C9G"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:4C9G"
FT HELIX 288..308
FT /evidence="ECO:0007829|PDB:4C9G"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4C9H"
SQ SEQUENCE 318 AA; 34426 MW; A9805DC33D9E24AC CRC64;
MSSNAQVKTP LPPAPAPKKE SNFLIDFLMG GVSAAVAKTA ASPIERVKLL IQNQDEMLKQ
GTLDRKYAGI LDCFKRTATQ EGVISFWRGN TANVIRYFPT QALNFAFKDK IKAMFGFKKE
EGYAKWFAGN LASGGAAGAL SLLFVYSLDY ARTRLAADSK SSKKGGARQF NGLIDVYKKT
LKSDGVAGLY RGFLPSVVGI VVYRGLYFGM YDSLKPLLLT GSLEGSFLAS FLLGWVVTTG
ASTCSYPLDT VRRRMMMTSG QAVKYDGAFD CLRKIVAAEG VGSLFKGCGA NILRGVAGAG
VISMYDQLQM ILFGKKFK
