DDR48_CANAL
ID DDR48_CANAL Reviewed; 212 AA.
AC Q59X49; A0A1D8PID1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Stress protein DDR48;
DE AltName: Full=DNA damage-responsive protein 48;
DE Short=DDRP 48;
GN Name=DDR48; Synonyms=DDR99; OrderedLocusNames=CAALFM_C209220WA;
GN ORFNames=CaO19.11563, CaO19.4082;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=11595734; DOI=10.1074/jbc.m104484200;
RA Lane S., Birse C., Zhou S., Matson R., Liu H.;
RT "DNA array studies demonstrate convergent regulation of virulence factors
RT by Cph1, Cph2, and Efg1 in Candida albicans.";
RL J. Biol. Chem. 276:48988-48996(2001).
RN [5]
RP INDUCTION.
RX PubMed=15273122; DOI=10.1128/aac.48.8.3064-3079.2004;
RA Karababa M., Coste A.T., Rognon B., Bille J., Sanglard D.;
RT "Comparison of gene expression profiles of Candida albicans azole-resistant
RT clinical isolates and laboratory strains exposed to drugs inducing
RT multidrug transporters.";
RL Antimicrob. Agents Chemother. 48:3064-3079(2004).
RN [6]
RP INDUCTION.
RX PubMed=15470256; DOI=10.1128/ec.3.5.1272-1286.2004;
RA Oberholzer U., Iouk T.L., Thomas D.Y., Whiteway M.;
RT "Functional characterization of myosin I tail regions in Candida
RT albicans.";
RL Eukaryot. Cell 3:1272-1286(2004).
RN [7]
RP INDUCTION.
RX PubMed=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
RA Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
RT "Transcriptional profiling in Candida albicans reveals new adaptive
RT responses to extracellular pH and functions for Rim101p.";
RL Mol. Microbiol. 54:1335-1351(2004).
RN [8]
RP INDUCTION.
RX PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA Quinn J.;
RT "Role of the Hog1 stress-activated protein kinase in the global
RT transcriptional response to stress in the fungal pathogen Candida
RT albicans.";
RL Mol. Biol. Cell 17:1018-1032(2006).
RN [9]
RP FUNCTION.
RX PubMed=18509269;
RA Dib L., Hayek P., Sadek H., Beyrouthy B., Khalaf R.A.;
RT "The Candida albicans Ddr48 protein is essential for filamentation, stress
RT response, and confers partial antifungal drug resistance.";
RL Med. Sci. Monit. 14:BR113-BR121(2008).
RN [10]
RP INDUCTION.
RX PubMed=19364863; DOI=10.1128/aac.01551-08;
RA Shirtliff M.E., Krom B.P., Meijering R.A., Peters B.M., Zhu J.,
RA Scheper M.A., Harris M.L., Jabra-Rizk M.A.;
RT "Farnesol-induced apoptosis in Candida albicans.";
RL Antimicrob. Agents Chemother. 53:2392-2401(2009).
RN [11]
RP INDUCTION.
RX PubMed=19252121; DOI=10.1128/ec.00246-08;
RA Hao B., Clancy C.J., Cheng S., Raman S.B., Iczkowski K.A., Nguyen M.H.;
RT "Candida albicans RFX2 encodes a DNA binding protein involved in DNA damage
RT responses, morphogenesis, and virulence.";
RL Eukaryot. Cell 8:627-639(2009).
RN [12]
RP INDUCTION.
RX PubMed=20870877; DOI=10.1128/ec.00159-10;
RA Synnott J.M., Guida A., Mulhern-Haughey S., Higgins D.G., Butler G.;
RT "Regulation of the hypoxic response in Candida albicans.";
RL Eukaryot. Cell 9:1734-1746(2010).
RN [13]
RP INDUCTION.
RX PubMed=20388546; DOI=10.1016/j.fgb.2010.03.009;
RA Alonso-Monge R., Roman E., Arana D.M., Prieto D., Urrialde V., Nombela C.,
RA Pla J.;
RT "The Sko1 protein represses the yeast-to-hypha transition and regulates the
RT oxidative stress response in Candida albicans.";
RL Fungal Genet. Biol. 47:587-601(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20167299; DOI=10.1016/j.jprot.2010.02.008;
RA Hernaez M.L., Ximenez-Embun P., Martinez-Gomariz M.,
RA Gutierrez-Blazquez M.D., Nombela C., Gil C.;
RT "Identification of Candida albicans exposed surface proteins in vivo by a
RT rapid proteomic approach.";
RL J. Proteomics 73:1404-1409(2010).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22523369; DOI=10.1128/ec.00107-12;
RA Cleary I.A., MacGregor N.B., Saville S.P., Thomas D.P.;
RT "Investigating the function of Ddr48p in Candida albicans.";
RL Eukaryot. Cell 11:718-724(2012).
CC -!- FUNCTION: Cell surface protein involved in the ability to sense and
CC respond to changes in the host environment. Required for stress
CC response and confers partial antifungal drug resistance. Contributes to
CC the DNA damage response. Required for the flocculation response
CC stimulated by 3-aminotriazole-induced amino acid starvation.
CC {ECO:0000269|PubMed:18509269, ECO:0000269|PubMed:22523369}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:20167299}.
CC -!- INDUCTION: Expression is induced during filamentation, biofilm
CC formation, after UV exposure, as well as by benomyl, caspofungin, and
CC ketoconazole. Also enriched in azole-resistant strains and in
CC stationary phase. Expression is repressed by SKO1, HOG1, RFX2,
CC farnesol, and in alkaline conditions. Expression is also controlled by
CC the filamentous growth regulators CPH1, CPH2, and EFG1.
CC {ECO:0000269|PubMed:11595734, ECO:0000269|PubMed:15273122,
CC ECO:0000269|PubMed:15470256, ECO:0000269|PubMed:15554973,
CC ECO:0000269|PubMed:16339080, ECO:0000269|PubMed:19252121,
CC ECO:0000269|PubMed:19364863, ECO:0000269|PubMed:20388546,
CC ECO:0000269|PubMed:20870877}.
CC -!- DISRUPTION PHENOTYPE: leads to reduced flocculation stimulated by 3-
CC aminotriazole-induced amino acid starvation.
CC {ECO:0000269|PubMed:22523369}.
CC -!- SIMILARITY: Belongs to the DDR48 family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27905.1; -; Genomic_DNA.
DR RefSeq; XP_714253.1; XM_709160.2.
DR AlphaFoldDB; Q59X49; -.
DR PRIDE; Q59X49; -.
DR GeneID; 3644061; -.
DR KEGG; cal:CAALFM_C209220WA; -.
DR CGD; CAL0000176590; DDR48.
DR VEuPathDB; FungiDB:C2_09220W_A; -.
DR eggNOG; ENOG502S5W1; Eukaryota.
DR HOGENOM; CLU_114213_0_0_1; -.
DR OMA; PSQGGWQ; -.
DR OrthoDB; 1921627at2759; -.
DR PRO; PR:Q59X49; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
PE 1: Evidence at protein level;
KW Cell wall; Reference proteome; Repeat; Secreted; Stress response.
FT CHAIN 1..212
FT /note="Stress protein DDR48"
FT /id="PRO_0000426732"
FT REPEAT 20..27
FT /note="1; approximate"
FT REPEAT 32..39
FT /note="2; approximate"
FT REPEAT 47..54
FT /note="3; approximate"
FT REPEAT 58..65
FT /note="4"
FT REPEAT 66..73
FT /note="5; approximate"
FT REPEAT 77..84
FT /note="6"
FT REPEAT 85..92
FT /note="7"
FT REPEAT 93..100
FT /note="8; approximate"
FT REPEAT 104..111
FT /note="9"
FT REPEAT 112..119
FT /note="10"
FT REPEAT 123..130
FT /note="11"
FT REPEAT 131..138
FT /note="12"
FT REPEAT 139..146
FT /note="13"
FT REPEAT 147..154
FT /note="14"
FT REPEAT 158..165
FT /note="15; approximate"
FT REPEAT 166..173
FT /note="16"
FT REPEAT 174..181
FT /note="17"
FT REPEAT 185..192
FT /note="18; approximate"
FT REPEAT 193..200
FT /note="19"
FT REPEAT 205..212
FT /note="20; approximate"
FT REGION 1..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 20..212
FT /note="20 X 8 AA approximate tandem repeats of D-S-Y-G-S-S-
FT N-[DT]"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 212 AA; 22615 MW; F605A0779D58D83E CRC64;
MVFGFGKDDD KDKNDRRDND SYGSSNRRNN DDSYGSSSFG SSNDDDNSYG SSNKRSNDSY
GSSNTDSYGS SNRRDNDSYG SSNNDSYGSS KTDSYGSSNR SGNDSYGSSN NDSYGSSNRK
GNDSYGSSNT DSYGSSNTDS YGSSNTDSYG SSNKRGNDSY GSSNDDSYGS SNDDSYGSSN
RRGNDSYGSS NDDSYGSSNR RGNSDSYGSS DY