TDA5_YEAST
ID TDA5_YEAST Reviewed; 326 AA.
AC Q06417; D6VZ62;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Uncharacterized oxidoreductase TDA5;
DE EC=1.-.-.-;
DE AltName: Full=Topoisomerase I damage affected protein 5;
GN Name=TDA5; OrderedLocusNames=YLR426W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=12077312; DOI=10.1073/pnas.132275199;
RA Birrell G.W., Brown J.A., Wu H.I., Giaever G., Chu A.M., Davis R.W.,
RA Brown J.M.;
RT "Transcriptional response of Saccharomyces cerevisiae to DNA-damaging
RT agents does not identify the genes that protect against these agents.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8778-8783(2002).
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]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP FUNCTION.
RX PubMed=16121259; DOI=10.1371/journal.pgen.0010024;
RA Lee W., St Onge R.P., Proctor M., Flaherty P., Jordan M.I., Arkin A.P.,
RA Davis R.W., Nislow C., Giaever G.;
RT "Genome-wide requirements for resistance to functionally distinct DNA-
RT damaging agents.";
RL PLoS Genet. 1:235-246(2005).
RN [7]
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).
CC -!- FUNCTION: Involved in the resistance to DNA-damaging agents.
CC {ECO:0000269|PubMed:12077312, ECO:0000269|PubMed:16121259}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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 2130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U20939; AAB67505.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09728.1; -; Genomic_DNA.
DR PIR; S53413; S53413.
DR RefSeq; NP_013530.1; NM_001182314.1.
DR AlphaFoldDB; Q06417; -.
DR SMR; Q06417; -.
DR BioGRID; 31686; 290.
DR DIP; DIP-4567N; -.
DR IntAct; Q06417; 7.
DR MINT; Q06417; -.
DR STRING; 4932.YLR426W; -.
DR PaxDb; Q06417; -.
DR PRIDE; Q06417; -.
DR TopDownProteomics; Q06417; -.
DR EnsemblFungi; YLR426W_mRNA; YLR426W; YLR426W.
DR GeneID; 851146; -.
DR KEGG; sce:YLR426W; -.
DR SGD; S000004418; TDA5.
DR VEuPathDB; FungiDB:YLR426W; -.
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00940000169042; -.
DR HOGENOM; CLU_010194_5_1_1; -.
DR InParanoid; Q06417; -.
DR OMA; YANFLPG; -.
DR BioCyc; YEAST:G3O-32486-MON; -.
DR Reactome; R-SCE-193144; Estrogen biosynthesis.
DR Reactome; R-SCE-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-SCE-5365859; RA biosynthesis pathway.
DR Reactome; R-SCE-8964572; Lipid particle organization.
DR PRO; PR:Q06417; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06417; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; HMP:SGD.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..326
FT /note="Uncharacterized oxidoreductase TDA5"
FT /id="PRO_0000247778"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 74..98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36677 MW; 2663A29F1C6D7FD5 CRC64;
MNIDCLCRWV VLPLLRYPLL VALVLRWSLS DSISICLTIY TLLINAFLIA NSYIKRSGQV
AWKSLREFKN GIVLITGGSK GLGRAIVSQL LQDYSNLTIL NVDICPSSVR NTRVKDLICD
LSDDEEVAAL LNLLKRKYKN EIRLIVNNAG VRANFTGFNG MERDNLDKIF KINTFAPLQF
IQELAPSRHS TRQCYIVNIA SILGILTPAK VAAYAASKAA LIAFHQSYSF ELQNEGVRNI
RTLLVTPGQL NTEMFAGFKP PRQFFAPVID ITTLAAKIVR YCELGQRGQL NEPFYCSFAH
LLMCVPYSLQ RIVRSFSRID CCLPDE
