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 25-MAY-2022, entry version 184. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; IEA:InterPro. 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 /note="ADP" FT /evidence="ECO:0000305|PubMed:24474793" FT BINDING 97 FT /note="ADP" FT /evidence="ECO:0000305|PubMed:24474793" FT BINDING 241 FT /note="ADP" 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 //