DDR48_YEAST
ID DDR48_YEAST Reviewed; 430 AA.
AC P18899; D6VZZ5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Stress protein DDR48;
DE AltName: Full=DNA damage-responsive protein 48;
DE Short=DDRP 48;
DE AltName: Full=Flocculent-specific protein;
DE AltName: Full=YP 75;
GN Name=DDR48; Synonyms=FSP; OrderedLocusNames=YMR173W; ORFNames=YM8010.03;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2111448; DOI=10.1128/mcb.10.6.3174-3184.1990;
RA Treger J.M., McEntee K.;
RT "Structure of the DNA damage-inducible gene DDR48 and evidence for its role
RT in mutagenesis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:3174-3184(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8089083; DOI=10.1093/oxfordjournals.jbchem.a124396;
RA Tonouchi A., Fujita A., Kuhara S.;
RT "Molecular cloning of the gene encoding a highly expressed protein in SFL1
RT gene-disrupted flocculating yeast.";
RL J. Biochem. 115:683-688(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-31, CLEAVAGE OF INITIATOR METHIONINE,
RP BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, AND INDUCTION.
RX PubMed=8444852; DOI=10.1016/s0021-9258(18)53461-x;
RA Sheng S., Schuster S.M.;
RT "Purification and characterization of Saccharomyces cerevisiae DNA damage-
RT responsive protein 48 (DDRP 48).";
RL J. Biol. Chem. 268:4752-4758(1993).
RN [6]
RP PROTEIN SEQUENCE OF 2-12.
RX PubMed=2114092; DOI=10.1042/bj2680401;
RA Carabaza A., Arino J., Fox J.W., Villar-Palasi C., Guinovart J.J.;
RT "Purification, characterization and partial amino acid sequence of glycogen
RT synthase from Saccharomyces cerevisiae.";
RL Biochem. J. 268:401-407(1990).
RN [7]
RP INDUCTION.
RX PubMed=3023840; DOI=10.1128/mcb.6.1.90-96.1986;
RA McClanahan T., McEntee K.;
RT "DNA damage and heat shock dually regulate genes in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 6:90-96(1986).
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-183; SER-191; SER-314 AND
RP SER-322, AND 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 INDUCTION.
RX PubMed=23125229; DOI=10.1093/molbev/mss253;
RA Dhar R., Sagesser R., Weikert C., Wagner A.;
RT "Yeast adapts to a changing stressful environment by evolving cross-
RT protection and anticipatory gene regulation.";
RL Mol. Biol. Evol. 30:573-588(2013).
CC -!- FUNCTION: DNA damage-responsive protein that may be required for
CC maintaining the rate of spontaneous mutagenesis. Shows low ATP and GTP
CC hydrolysis activity. Dispensable for acquisition of thermotolerance and
CC does not play a significant role in recovery or protection of cells
CC from acute heat shock. {ECO:0000269|PubMed:2111448}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.29 mM for ATP {ECO:0000269|PubMed:8444852};
CC KM=0.58 mM for GTP {ECO:0000269|PubMed:8444852};
CC -!- INDUCTION: Expression is induced by DNA damage, as well as by salt,
CC oxidative, and heat-shock stress. {ECO:0000269|PubMed:23125229,
CC ECO:0000269|PubMed:3023840, ECO:0000269|PubMed:8444852}.
CC -!- PTM: Probably highly glycosylated. {ECO:0000269|PubMed:8444852}.
CC -!- DISRUPTION PHENOTYPE: Shows a slightly altered sensitivity to killing
CC by 4-nitroquinoline-1-oxide and to heat shock; and a 6- to 14-fold
CC reduction of the spontaneous mutation rate of reversion of a HIS4
CC mutation. {ECO:0000269|PubMed:2111448}.
CC -!- SIMILARITY: Belongs to the DDR48 family. {ECO:0000305}.
CC -!- CAUTION: sequence is a contaminating peptide from a S.cerevisiae
CC glycogen synthase purification. {ECO:0000305|PubMed:2114092}.
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DR EMBL; M36110; AAA34563.1; -; Genomic_DNA.
DR EMBL; S73336; AAB31954.1; -; Genomic_DNA.
DR EMBL; Z49808; CAA89906.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10069.1; -; Genomic_DNA.
DR PIR; S55120; HHBYD8.
DR RefSeq; NP_013897.1; NM_001182678.1.
DR AlphaFoldDB; P18899; -.
DR BioGRID; 35351; 77.
DR DIP; DIP-4424N; -.
DR IntAct; P18899; 6.
DR MINT; P18899; -.
DR STRING; 4932.YMR173W; -.
DR iPTMnet; P18899; -.
DR MaxQB; P18899; -.
DR PaxDb; P18899; -.
DR PRIDE; P18899; -.
DR TopDownProteomics; P18899; -.
DR EnsemblFungi; YMR173W_mRNA; YMR173W; YMR173W.
DR GeneID; 855210; -.
DR KEGG; sce:YMR173W; -.
DR SGD; S000004784; DDR48.
DR VEuPathDB; FungiDB:YMR173W; -.
DR eggNOG; ENOG502QUR8; Eukaryota.
DR HOGENOM; CLU_040090_0_0_1; -.
DR InParanoid; P18899; -.
DR OMA; NGNKYDI; -.
DR BioCyc; YEAST:G3O-32861-MON; -.
DR PRO; PR:P18899; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P18899; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW Reference proteome; Repeat; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2114092,
FT ECO:0000269|PubMed:8444852"
FT CHAIN 2..430
FT /note="Stress protein DDR48"
FT /id="PRO_0000079849"
FT REPEAT 74..81
FT /note="1"
FT REPEAT 82..89
FT /note="2"
FT REPEAT 90..97
FT /note="3"
FT REPEAT 98..105
FT /note="4"
FT REPEAT 106..113
FT /note="5"
FT REPEAT 114..121
FT /note="6"
FT REPEAT 124..131
FT /note="7; approximate"
FT REPEAT 132..139
FT /note="8"
FT REPEAT 141..148
FT /note="9"
FT REPEAT 149..156
FT /note="10"
FT REPEAT 157..164
FT /note="11"
FT REPEAT 165..172
FT /note="12"
FT REPEAT 175..182
FT /note="13; approximate"
FT REPEAT 183..190
FT /note="14"
FT REPEAT 191..198
FT /note="15"
FT REPEAT 201..208
FT /note="16; approximate"
FT REPEAT 209..216
FT /note="17"
FT REPEAT 217..224
FT /note="18"
FT REPEAT 225..232
FT /note="19"
FT REPEAT 233..240
FT /note="20"
FT REPEAT 243..250
FT /note="21; approximate"
FT REPEAT 251..258
FT /note="22"
FT REPEAT 260..267
FT /note="23"
FT REPEAT 268..275
FT /note="24"
FT REPEAT 278..285
FT /note="25; approximate"
FT REPEAT 287..294
FT /note="26"
FT REPEAT 296..303
FT /note="27"
FT REPEAT 306..313
FT /note="28; approximate"
FT REPEAT 314..321
FT /note="29"
FT REPEAT 322..329
FT /note="30"
FT REPEAT 332..339
FT /note="31; approximate"
FT REPEAT 340..347
FT /note="32"
FT REPEAT 348..355
FT /note="33"
FT REPEAT 358..365
FT /note="34; approximate"
FT REPEAT 366..373
FT /note="35"
FT REPEAT 375..382
FT /note="36"
FT REPEAT 393..400
FT /note="37; approximate"
FT REPEAT 407..414
FT /note="38"
FT REGION 1..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..414
FT /note="38 X 8 AA approximate tandem repeats of S-[NS]-N-
FT [ND]-D-S-Y-G"
FT COMPBIAS 8..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 9
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="E -> Q (in Ref. 1; AAA34563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 46233 MW; 650212489A8828AC CRC64;
MGLFDKVKQF ANSNNNNNDS GNNNQGDYVT KAENMIGEDR VNQFKSKIGE DRFDKMESKV
RQQFSNTSIN DNDSNNNDSY GSNNNDSYGS NNNDSYGSNN NDSYGSNNND SYGSNNDDSY
GSSNKKKSSY GSNNDDSYGS SNNNDSYGSN NNDSYGSNNN DSYGSNNDDS YGSSNKNKSS
YGSNNDDSYG SNNDDSYGSS NKKKSSYGSS NNDSYGSNND DSYGSNNNDS YGSNNDDSYG
SSNKKKSSYG SNNDDSYGSS NNNDSYGSNN DDSYGSSNKN KSSYGSSSND DSYGSSNNDD
SYGSSNKKKS SYGSNNDDSY GSNNDDSYGS SNKKKSSYGS SNNDSYGSNN DDSYGSSNKK
KSSYGSNNDD SYGSSNNNDS YGSNNDDSYG SSNRNKNSYG SSNYGSSNND DSYGSSNRGG
RNQYGGDDDY
