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 06-JUL-2016, entry version 145. 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; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2165073; 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; 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., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the CC mitochondrial inner membrane. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein. CC -!- MISCELLANEOUS: The transmembrane helices are not perpendicular to CC the plane of the membrane, but cross the membrane at an angle. At CC least 2 of the odd-numbered transmembrane helices exhibit a sharp CC kink, due to the presence of a conserved proline residue (By CC similarity). {ECO:0000250}. CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 3 Solcar repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00282}. 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 ProteinModelPortal; P18238; -. DR SMR; P18238; 3-306. DR BioGrid; 32790; 27. DR DIP; DIP-6289N; -. DR IntAct; P18238; 10. DR MINT; MINT-688418; -. DR TCDB; 2.A.29.1.9; the mitochondrial carrier (mc) family. DR MaxQB; P18238; -. DR PRIDE; P18238; -. DR DNASU; 852380; -. DR EnsemblFungi; YBR085W; YBR085W; YBR085W. DR GeneID; 852380; -. DR KEGG; sce:YBR085W; -. DR EuPathDB; FungiDB:YBR085W; -. DR SGD; S000000289; AAC3. DR GeneTree; ENSGT00390000011543; -. DR HOGENOM; HOG000165727; -. DR InParanoid; P18238; -. DR KO; K05863; -. DR OMA; GSSQREF; -. DR OrthoDB; EOG7NCVDV; -. DR BioCyc; YEAST:G3O-29052-MONOMER; -. DR Reactome; R-SCE-422356; Regulation of insulin secretion. DR PRO; PR:P18238; -. DR Proteomes; UP000002311; Chromosome II. 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:0005471; F:ATP:ADP antiporter activity; ISA:SGD. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0009061; P:anaerobic respiration; IGI:SGD. DR GO; GO:0015886; P:heme transport; IMP:SGD. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; ISA:SGD. DR Gene3D; 1.50.40.10; -; 1. DR InterPro; IPR002113; Aden_trnslctor. DR InterPro; IPR002067; Mit_carrier. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom. 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; Complete proteome; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 307 ADP,ATP carrier protein 3. FT /FTId=PRO_0000090595. FT TRANSMEM 9 43 Helical; Name=1. {ECO:0000250}. FT TRANSMEM 80 104 Helical; Name=2. {ECO:0000250}. FT TRANSMEM 112 146 Helical; Name=3. {ECO:0000250}. FT TRANSMEM 181 208 Helical; Name=4. {ECO:0000250}. FT TRANSMEM 213 247 Helical; Name=5. {ECO:0000250}. FT TRANSMEM 276 301 Helical; Name=6. {ECO:0000250}. FT REPEAT 10 103 Solcar 1. FT REPEAT 114 206 Solcar 2. FT REPEAT 214 300 Solcar 3. FT MOTIF 241 246 Substrate recognition. {ECO:0000250}. FT BINDING 85 85 Nucleotide. {ECO:0000250}. FT HELIX 5 29 {ECO:0000244|PDB:4C9Q}. FT HELIX 31 41 {ECO:0000244|PDB:4C9Q}. FT HELIX 43 48 {ECO:0000244|PDB:4C9Q}. FT HELIX 59 69 {ECO:0000244|PDB:4C9Q}. FT HELIX 73 76 {ECO:0000244|PDB:4C9Q}. FT HELIX 79 104 {ECO:0000244|PDB:4C9Q}. FT TURN 108 110 {ECO:0000244|PDB:4C9J}. FT HELIX 112 146 {ECO:0000244|PDB:4C9Q}. FT HELIX 162 172 {ECO:0000244|PDB:4C9Q}. FT HELIX 175 178 {ECO:0000244|PDB:4C9Q}. FT TURN 179 181 {ECO:0000244|PDB:4C9Q}. FT HELIX 182 202 {ECO:0000244|PDB:4C9Q}. FT HELIX 217 233 {ECO:0000244|PDB:4C9Q}. FT HELIX 235 246 {ECO:0000244|PDB:4C9Q}. FT TURN 247 249 {ECO:0000244|PDB:4C9Q}. FT HELIX 257 268 {ECO:0000244|PDB:4C9Q}. FT HELIX 270 274 {ECO:0000244|PDB:4C9Q}. FT HELIX 277 301 {ECO:0000244|PDB:4C9Q}. FT STRAND 302 304 {ECO:0000244|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 //