ID   DDR2_YEAST              Reviewed;          61 AA.
AC   P89113; D6W215;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Protein DDR2;
DE   Flags: Precursor;
GN   Name=DDR2; OrderedLocusNames=YOL052C-A; ORFNames=YOL052BC, YOL053C-A;
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].
RX   PubMed=8954934; DOI=10.1006/bbrc.1996.1840;
RA   Kobayashi N., McClanahan T.K., Simon J.R., Treger J.M., McEntee K.;
RT   "Structure and functional analysis of the multistress response gene DDR2
RT   from Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 229:540-547(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90843 / S288c / FY73;
RX   PubMed=8789261;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<67::aid-yea884>3.0.co;2-f;
RA   Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
RT   "Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
RL   Yeast 12:67-76(1996).
RN   [3]
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   [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   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).
CC   -!- FUNCTION: May play an important role in the response of cells to
CC       diverse environmental stresses.
CC   -!- INDUCTION: By multistress. Expression is controlled by the MSN2 and
CC       MSN4 transcriptional regulators.
CC   -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: To yeast HOR7. {ECO:0000305}.
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DR   EMBL; U82215; AAB40031.1; -; Genomic_DNA.
DR   EMBL; Z74794; CAA99059.1; -; Genomic_DNA.
DR   EMBL; Z74795; CAA99061.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10731.1; -; Genomic_DNA.
DR   PIR; S69290; S69290.
DR   RefSeq; NP_014589.1; NM_001183307.1.
DR   AlphaFoldDB; P89113; -.
DR   BioGRID; 34351; 36.
DR   DIP; DIP-7584N; -.
DR   IntAct; P89113; 2.
DR   MINT; P89113; -.
DR   STRING; 4932.YOL052C-A; -.
DR   PaxDb; P89113; -.
DR   EnsemblFungi; YOL052C-A_mRNA; YOL052C-A; YOL052C-A.
DR   GeneID; 854104; -.
DR   KEGG; sce:YOL052C-A; -.
DR   SGD; S000005413; DDR2.
DR   VEuPathDB; FungiDB:YOL052C-A; -.
DR   HOGENOM; CLU_209340_0_0_1; -.
DR   OMA; LHAQNGQ; -.
DR   BioCyc; YEAST:G3O-33463-MON; -.
DR   PRO; PR:P89113; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P89113; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:SGD.
DR   GO; GO:0034605; P:cellular response to heat; IEP:SGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:SGD.
DR   GO; GO:0009267; P:cellular response to starvation; IEP:SGD.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..61
FT                   /note="Protein DDR2"
FT                   /id="PRO_0000021096"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   61 AA;  5955 MW;  F89BAAF9F466BD05 CRC64;
     MKVSQVFISA ISVFGLATSV NAQNASNTTS NAAPALHAQN GQLLNAGVVG AAVGGALAFL
     I