ID   ODC1_YEAST              Reviewed;         310 AA.
AC   Q03028; D6W3N3;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Mitochondrial 2-oxodicarboxylate carrier 1;
GN   Name=ODC1; OrderedLocusNames=YPL134C; ORFNames=LPI11C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
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   [3]
RP   CHARACTERIZATION.
RX   PubMed=11013234; DOI=10.1074/jbc.m004332200;
RA   Palmieri L., Agrimi G., Runswick M.J., Fearnley I.M., Palmieri F.,
RA   Walker J.E.;
RT   "Identification in Saccharomyces cerevisiae of two isoforms of a novel
RT   mitochondrial transporter for 2-oxoadipate and 2-oxoglutarate.";
RL   J. Biol. Chem. 276:1916-1922(2001).
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).
CC   -!- FUNCTION: Transports C5-C7 oxodicarboxylates across the inner membranes
CC       of mitochondria. Can transport 2-oxoadipate, 2-oxoglutarate, adipate,
CC       glutarate, 2-oxopimelate, oxaloacetate, citrate and malate. The main
CC       physiological role is probably to supply 2-oxoadipate and 2-
CC       oxoglutarate from the mitochondrial matrix to the cytosol where they
CC       are used in the biosynthesis of lysine and glutamate, respectively, and
CC       in lysine catabolism.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- MISCELLANEOUS: Present with 2840 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; U43703; AAB68225.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11299.1; -; Genomic_DNA.
DR   PIR; S69050; S69050.
DR   RefSeq; NP_015191.1; NM_001183948.1.
DR   AlphaFoldDB; Q03028; -.
DR   SMR; Q03028; -.
DR   BioGRID; 36047; 81.
DR   DIP; DIP-8776N; -.
DR   STRING; 4932.YPL134C; -.
DR   TCDB; 2.A.29.2.8; the mitochondrial carrier (mc) family.
DR   MaxQB; Q03028; -.
DR   PaxDb; Q03028; -.
DR   PRIDE; Q03028; -.
DR   EnsemblFungi; YPL134C_mRNA; YPL134C; YPL134C.
DR   GeneID; 855969; -.
DR   KEGG; sce:YPL134C; -.
DR   SGD; S000006055; ODC1.
DR   VEuPathDB; FungiDB:YPL134C; -.
DR   eggNOG; KOG0754; Eukaryota.
DR   GeneTree; ENSGT00730000111119; -.
DR   HOGENOM; CLU_015166_5_2_1; -.
DR   InParanoid; Q03028; -.
DR   OMA; MLLVFDY; -.
DR   BioCyc; YEAST:G3O-34033-MON; -.
DR   Reactome; R-SCE-428643; Organic anion transporters.
DR   PRO; PR:Q03028; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q03028; protein.
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:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR   GO; GO:0005310; F:dicarboxylic acid transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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:0006839; P:mitochondrial 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   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   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..310
FT                   /note="Mitochondrial 2-oxodicarboxylate carrier 1"
FT                   /id="PRO_0000090648"
FT   TRANSMEM        9..29
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          9..108
FT                   /note="Solcar 1"
FT   REPEAT          120..204
FT                   /note="Solcar 2"
FT   REPEAT          213..300
FT                   /note="Solcar 3"
SQ   SEQUENCE   310 AA;  34206 MW;  8EB7D6231BC2BCEE CRC64;
     MTSIDNRPLP FIYQFTAGAI AGVSELLVMY PLDVVKTRMQ LQVTTKGHPA VVAAKAAVDH
     YTGVMDCLTK IVKKEGFSHL YKGITSPILM EAPKRAIKFS GNDTFQTFYK KIFPTPNGEM
     TQKIAIYSGA SAGAVEAFVV APFELVKIRL QDVNSQFKTP IEVVKNSVVK GGVLSLFNGL
     EATIWRHVLW NAGYFGIIFQ IRKLLPAAKT STEKTRNDLI AGAIGGTVGC LLNTPFDVVK
     SRIQRSSGPL RKYNWSLPSV LLVYREEGFK ALYKGFAPKV MRLAPGGGLL LVVFTNVMDF
     FREVKYGKKQ