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ODC2_YEAST
ID   ODC2_YEAST              Reviewed;         307 AA.
AC   Q99297; D6W2S7; O13594;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Mitochondrial 2-oxodicarboxylate carrier 2;
GN   Name=ODC2; OrderedLocusNames=YOR222W; ORFNames=YOR50-12;
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].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8840505;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA   Galisson F., Dujon B.;
RT   "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT   XV of the yeast Saccharomyces cerevisiae.";
RL   Yeast 12:877-885(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   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).
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   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; X92441; CAA63185.1; -; Genomic_DNA.
DR   EMBL; Z75130; CAA99440.1; -; Genomic_DNA.
DR   EMBL; Z75131; CAA99442.2; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10993.1; -; Genomic_DNA.
DR   PIR; S60949; S60949.
DR   RefSeq; NP_014865.1; NM_001183641.1.
DR   AlphaFoldDB; Q99297; -.
DR   SMR; Q99297; -.
DR   BioGRID; 34616; 99.
DR   DIP; DIP-5386N; -.
DR   STRING; 4932.YOR222W; -.
DR   TCDB; 2.A.29.2.5; the mitochondrial carrier (mc) family.
DR   MaxQB; Q99297; -.
DR   PaxDb; Q99297; -.
DR   PRIDE; Q99297; -.
DR   EnsemblFungi; YOR222W_mRNA; YOR222W; YOR222W.
DR   GeneID; 854397; -.
DR   KEGG; sce:YOR222W; -.
DR   SGD; S000005748; ODC2.
DR   VEuPathDB; FungiDB:YOR222W; -.
DR   eggNOG; KOG0754; Eukaryota.
DR   GeneTree; ENSGT00730000111119; -.
DR   HOGENOM; CLU_015166_5_2_1; -.
DR   InParanoid; Q99297; -.
DR   OMA; FHFGFFG; -.
DR   BioCyc; YEAST:G3O-33721-MON; -.
DR   Reactome; R-SCE-428643; Organic anion transporters.
DR   PRO; PR:Q99297; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q99297; 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; HDA: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..307
FT                   /note="Mitochondrial 2-oxodicarboxylate carrier 2"
FT                   /id="PRO_0000090649"
FT   TRANSMEM        10..30
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..95
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          10..106
FT                   /note="Solcar 1"
FT   REPEAT          116..200
FT                   /note="Solcar 2"
FT   REPEAT          209..299
FT                   /note="Solcar 3"
SQ   SEQUENCE   307 AA;  34007 MW;  4089082A64DBA97C CRC64;
     MSSDSNAKPL PFIYQFISGA VAGISELTVM YPLDVVKTRF QLEVTTPTAA AVGKQVERYN
     GVIDCLKKIV KKEGFSRLYR GISSPMLMEA PKRATKFACN DQYQKIFKNL FNTNETTQKI
     SIAAGASAGM TEAAVIVPFE LIKIRMQDVK SSYLGPMDCL KKTIKNEGIM GLYKGIESTM
     WRNALWNGGY FGVIYQVRNS MPVAKTKGQK TRNDLIAGAI GGTVGTMLNT PFDVVKSRIQ
     SVDAVSSAVK KYNWCLPSLL VIYREEGFRA LYKGFVPKVC RLAPGGSLML VVFTGMMNFF
     RDLKYGH
 
 
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