TDA7_YEAST
ID TDA7_YEAST Reviewed; 636 AA.
AC P53882; D6W109;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Topoisomerase I damage affected protein 7;
GN Name=TDA7; OrderedLocusNames=YNL176C; ORFNames=N1661;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 251.
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 [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 [4]
RP INDUCTION.
RX PubMed=16278933; DOI=10.1002/yea.1302;
RA de Lichtenberg U., Wernersson R., Jensen T.S., Nielsen H.B., Fausboell A.,
RA Schmidt P., Hansen F.B., Knudsen S., Brunak S.;
RT "New weakly expressed cell cycle-regulated genes in yeast.";
RL Yeast 22:1191-1201(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628, AND IDENTIFICATION BY
RP 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 [6]
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 [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).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: During G2 phase of cell cycle. Promoter is bound by the FKH2
CC transcription factor. {ECO:0000269|PubMed:16278933}.
CC -!- DISRUPTION PHENOTYPE: Leads to cell death when overexpressing the
CC camptothecin mimetic TOP1-T(722)A mutant.
CC {ECO:0000269|PubMed:21173034}.
CC -!- SIMILARITY: Belongs to the TDA7 family. {ECO:0000305}.
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DR EMBL; Z71452; CAA96068.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10375.2; -; Genomic_DNA.
DR PIR; S63131; S63131.
DR RefSeq; NP_014223.2; NM_001183014.2.
DR AlphaFoldDB; P53882; -.
DR BioGRID; 35655; 11.
DR DIP; DIP-4330N; -.
DR IntAct; P53882; 4.
DR MINT; P53882; -.
DR STRING; 4932.YNL176C; -.
DR iPTMnet; P53882; -.
DR PaxDb; P53882; -.
DR PRIDE; P53882; -.
DR EnsemblFungi; YNL176C_mRNA; YNL176C; YNL176C.
DR GeneID; 855545; -.
DR KEGG; sce:YNL176C; -.
DR SGD; S000005120; TDA7.
DR VEuPathDB; FungiDB:YNL176C; -.
DR eggNOG; ENOG502S5S1; Eukaryota.
DR HOGENOM; CLU_029057_0_0_1; -.
DR InParanoid; P53882; -.
DR OMA; FYQHWLD; -.
DR BioCyc; YEAST:G3O-33188-MON; -.
DR PRO; PR:P53882; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53882; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Vacuole.
FT CHAIN 1..636
FT /note="Topoisomerase I damage affected protein 7"
FT /id="PRO_0000203407"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 512
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 251
FT /note="F -> C (in Ref. 1; CAA96068)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 67401 MW; C6C228AEFFA43405 CRC64;
MNSNSTIGRT TLGESDTISL SFSEPSSSLN SRSTDVVFAS TSTLVPQQGS LTSLPPVSST
ATPTYYSTSL TYDETLHTSI DVSSTSTLVS STDSSSSSEQ DTYSSQYDPA TSSYSIITPS
MSIFSSTSPM SSSSSITSEW SSLTSTTPTL SSSATSLSSS WSSLSSPSSL LVSSSLSLSL
SSSYSDTKLF SFDSRSSIFS PSTPTVISPS YTYLSSISAT SFQISTTSEL SSSWFSTISS
PSTISNKDTT FPSSSRNTST SFYSSSLSST NDFSTISKSS KLSPSASSST VSISTISVPT
SSSVSSSSSK VPSNRPSSSS SSDDTTSAYS STYTFQSLQS TTSSSIPPTT QTPSTSTIST
SPIPTSSQVF NTVAISSSED SKTIYYFYTQ TYDITDSSTT FVTGLPTTIA VAKSEVTSFS
APSSTITADM SFYQHWLDGS LDNNKNQGTS KTNTGTIVGS VVGSVGGILI CVLVVWFMLV
RKRKAKRHFK ENDSFCHEIG RRTGFPTTAQ AKEASLQAQD SGSQQRNTET ASANNPFSNE
FNFKARGNPP PVPPPRNVTA MNGSFQNMRS NFMDQENRFS YGSSFTYSSL GSSTQGGFST
LSSNSIRLGR GLDNDISHDE RNTVQNNSQG FLREII
