TDA3_YEAST
ID TDA3_YEAST Reviewed; 523 AA.
AC P38758; D3DKV4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Putative oxidoreductase TDA3;
DE EC=1.-.-.-;
DE AltName: Full=Batten disease protein 3;
DE AltName: Full=Topoisomerase I damage affected protein 3;
GN Name=TDA3; Synonyms=BTN3; OrderedLocusNames=YHR009C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP FUNCTION.
RX PubMed=20219942; DOI=10.1101/gr.102764.109;
RA Koren A., Soifer I., Barkai N.;
RT "MRC1-dependent scaling of the budding yeast DNA replication timing
RT program.";
RL Genome Res. 20:781-790(2010).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=21173034; DOI=10.1101/gr.109033.110;
RA Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S.,
RA Wagner M., Rothstein R.;
RT "Selective ploidy ablation, a high-throughput plasmid transfer protocol,
RT identifies new genes affecting topoisomerase I-induced DNA damage.";
RL Genome Res. 21:477-486(2011).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BTN2.
RX PubMed=21441304; DOI=10.1091/mbc.e10-11-0878;
RA Kanneganti V., Kama R., Gerst J.E.;
RT "Btn3 is a negative regulator of Btn2-mediated endosomal protein
RT trafficking and prion curing in yeast.";
RL Mol. Biol. Cell 22:1648-1663(2011).
CC -!- FUNCTION: Putative oxidoreductase that negatively regulates the
CC retrieval of cargo from late endosomes to the Golgi. Regulates YIF1 and
CC KEX2 localization. Required for fast DNA replication.
CC {ECO:0000269|PubMed:20219942, ECO:0000269|PubMed:21441304}.
CC -!- SUBUNIT: Interacts with BTN2. {ECO:0000269|PubMed:21441304}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Note=The recruitment
CC from the cytoplasm to endosomal structures is facilitated by BTN2.
CC -!- DISRUPTION PHENOTYPE: Leads to cell death when overexpressing the
CC camptothecin mimetic TOP1-T(722)A mutant.
CC {ECO:0000269|PubMed:21173034}.
CC -!- MISCELLANEOUS: Present with 5240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TDA3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68938.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U10400; AAB68938.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06698.1; -; Genomic_DNA.
DR PIR; S46784; S46784.
DR RefSeq; NP_011873.1; NM_001179139.1.
DR AlphaFoldDB; P38758; -.
DR SMR; P38758; -.
DR BioGRID; 36436; 64.
DR DIP; DIP-4617N; -.
DR IntAct; P38758; 11.
DR STRING; 4932.YHR009C; -.
DR iPTMnet; P38758; -.
DR MaxQB; P38758; -.
DR PaxDb; P38758; -.
DR PRIDE; P38758; -.
DR EnsemblFungi; YHR009C_mRNA; YHR009C; YHR009C.
DR GeneID; 856400; -.
DR KEGG; sce:YHR009C; -.
DR SGD; S000001051; TDA3.
DR VEuPathDB; FungiDB:YHR009C; -.
DR eggNOG; KOG2852; Eukaryota.
DR GeneTree; ENSGT00530000068930; -.
DR HOGENOM; CLU_007884_14_0_1; -.
DR InParanoid; P38758; -.
DR OMA; IASGHSC; -.
DR BioCyc; YEAST:G3O-31072-MON; -.
DR PRO; PR:P38758; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38758; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endosome; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..523
FT /note="Putative oxidoreductase TDA3"
FT /id="PRO_0000202886"
FT REGION 157..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 523 AA; 57614 MW; 7D02A4C731758B6D CRC64;
MGEDFMHPPF QTYPSKNSEG KKHIVIVGGG IIGCCTAYYL TQHPSFSPST HHITIIESRR
IAGGASGKAG GLLASWAFPH QIVPLSFQLH QELSDEYDGE NNWDYRRLTT VSLEADVREE
VIENYERLSK KAYNLNVPPP KKRPGYISNK FNIGDSNSSL SSSGSSLKND SASNEEEGSD
IHVSSSVPSL HSLTNERMRS HTNSASDLDS VSPVEQLRET NIHNPLPADL DWIRRELVND
WSSLGGTDTT AQLHPYKFTH FILSKAMETG AVDLLLGKVV GLKCDEMDCV HSLKYLPSVV
KNRRNSRGHA ENPDIKLGTI FNDENAKPIE INDIQQIVLS MGPWTSKILK DCPISGLRAH
SVTIKPSEKT VSPYAILAEL KVNDREFFSP EMYARKDEVY VCGEGDTLVN IPESSDDVEV
VSEKCDELYH YVSKLSPTLS KGHLLRKQAC FLPVLNVPTS SGPLIGETNV KDLYIASGHS
CWGINNAPAT GKLMAEILLD GEATSAEISS LDPKLYFDAT ILS
