ADT1_YEAST
ID ADT1_YEAST Reviewed; 309 AA.
AC P04710; D6VZN1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
DE AltName: Full=Adenine nucleotide translocator 1;
DE Short=ANT 1;
GN Name=AAC1; OrderedLocusNames=YMR056C; ORFNames=YM9796.09C;
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=3023860; DOI=10.1128/mcb.6.2.626-634.1986;
RA Adrian G.S., McCammon M.T., Montgomery D.L., Douglas M.G.;
RT "Sequences required for delivery and localization of the ADP/ATP
RT translocator to the mitochondrial inner membrane.";
RL Mol. Cell. Biol. 6:626-634(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 265-309.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1651171; DOI=10.1016/0092-8674(81)90014-3;
RA Hoyt M.A., Totis L., Roberts B.T.;
RT "S. cerevisiae genes required for cell cycle arrest in response to loss of
RT microtubule function.";
RL Cell 66:507-517(1991).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [6]
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).
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:2167309). 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:2167309}.
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:2167309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000;
CC Evidence={ECO:0000269|PubMed:2167309};
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 -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P18239}; 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. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:G2QNH0}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
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DR EMBL; M12514; AAA97486.1; -; Genomic_DNA.
DR EMBL; Z49703; CAA89766.1; -; Genomic_DNA.
DR EMBL; M64706; AAA16884.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09955.1; -; Genomic_DNA.
DR PIR; A24849; A24849.
DR RefSeq; NP_013772.1; NM_001182554.1.
DR AlphaFoldDB; P04710; -.
DR SMR; P04710; -.
DR BioGRID; 35232; 46.
DR DIP; DIP-2551N; -.
DR IntAct; P04710; 5.
DR MINT; P04710; -.
DR STRING; 4932.YMR056C; -.
DR TCDB; 2.A.29.1.3; the mitochondrial carrier (mc) family.
DR iPTMnet; P04710; -.
DR MaxQB; P04710; -.
DR PaxDb; P04710; -.
DR PRIDE; P04710; -.
DR DNASU; 855078; -.
DR EnsemblFungi; YMR056C_mRNA; YMR056C; YMR056C.
DR GeneID; 855078; -.
DR KEGG; sce:YMR056C; -.
DR SGD; S000004660; AAC1.
DR VEuPathDB; FungiDB:YMR056C; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000176325; -.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; P04710; -.
DR OMA; AYQRQYK; -.
DR BioCyc; YEAST:G3O-32761-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:P04710; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P04710; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:SGD.
DR GO; GO:0009060; P:aerobic respiration; IGI:SGD.
DR GO; GO:0006783; P:heme biosynthetic process; 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:0006839; P:mitochondrial transport; IGI: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 Antiport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..309
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000090593"
FT TRANSMEM 13..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 81..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 114..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 184..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 219..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT TRANSMEM 279..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P18239"
FT REPEAT 11..104
FT /note="Solcar 1"
FT REPEAT 116..208
FT /note="Solcar 2"
FT REPEAT 216..302
FT /note="Solcar 3"
FT REGION 243..248
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 243..248
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 86
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 98
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 243
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
SQ SEQUENCE 309 AA; 34121 MW; BEC8999DFBB1CA51 CRC64;
MSHTETQTQQ SHFGVDFLMG GVSAAIAKTG AAPIERVKLL MQNQEEMLKQ GSLDTRYKGI
LDCFKRTATH EGIVSFWRGN TANVLRYFPT QALNFAFKDK IKSLLSYDRE RDGYAKWFAG
NLFSGGAAGG LSLLFVYSLD YARTRLAADA RGSKSTSQRQ FNGLLDVYKK TLKTDGLLGL
YRGFVPSVLG IIVYRGLYFG LYDSFKPVLL TGALEGSFVA SFLLGWVITM GASTASYPLD
TVRRRMMMTS GQTIKYDGAL DCLRKIVQKE GAYSLFKGCG ANIFRGVAAA GVISLYDQLQ
LIMFGKKFK
