RBT4_CANAL
ID RBT4_CANAL Reviewed; 358 AA.
AC Q5AB48; A0A1D8PDY8; Q5AAV8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Secreted protein RBT4;
DE AltName: Full=PRY family protein 4;
DE AltName: Full=Repressed by TUP1 protein 4;
DE Flags: Precursor;
GN Name=RBT4; Synonyms=PRY4; OrderedLocusNames=CAALFM_C107030CA;
GN ORFNames=CaO19.13583, CaO19.6202;
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=10790384; DOI=10.1093/genetics/155.1.57;
RA Braun B.R., Johnson A.D.;
RT "TUP1, CPH1 and EFG1 make independent contributions to filamentation in
RT Candida albicans.";
RL Genetics 155:57-67(2000).
RN [5]
RP INDUCTION, AND FUNCTION.
RX PubMed=10978273; DOI=10.1093/genetics/156.1.31;
RA Braun B.R., Head W.S., Wang M.X., Johnson A.D.;
RT "Identification and characterization of TUP1-regulated genes in Candida
RT albicans.";
RL Genetics 156:31-44(2000).
RN [6]
RP INDUCTION.
RX PubMed=11395474; DOI=10.1128/jb.183.13.4090-4093.2001;
RA Leng P., Lee P.R., Wu H., Brown A.J.;
RT "Efg1, a morphogenetic regulator in Candida albicans, is a sequence-
RT specific DNA binding protein.";
RL J. Bacteriol. 183:4090-4093(2001).
RN [7]
RP INDUCTION.
RX PubMed=11259598; DOI=10.1128/mcb.21.7.2496-2505.2001;
RA Kadosh D., Johnson A.D.;
RT "Rfg1, a protein related to the Saccharomyces cerevisiae hypoxic regulator
RT Rox1, controls filamentous growth and virulence in Candida albicans.";
RL Mol. Cell. Biol. 21:2496-2505(2001).
RN [8]
RP INDUCTION.
RX PubMed=11533231; DOI=10.1128/mcb.21.19.6418-6428.2001;
RA Lane S., Zhou S., Pan T., Dai Q., Liu H.;
RT "The basic helix-loop-helix transcription factor Cph2 regulates hyphal
RT development in Candida albicans partly via TEC1.";
RL Mol. Cell. Biol. 21:6418-6428(2001).
RN [9]
RP INDUCTION.
RX PubMed=12388749; DOI=10.1091/mbc.e02-05-0272;
RA Nantel A., Dignard D., Bachewich C., Harcus D., Marcil A., Bouin A.P.,
RA Sensen C.W., Hogues H., van het Hoog M., Gordon P., Rigby T., Benoit F.,
RA Tessier D.C., Thomas D.Y., Whiteway M.;
RT "Transcription profiling of Candida albicans cells undergoing the yeast-to-
RT hyphal transition.";
RL Mol. Biol. Cell 13:3452-3465(2002).
RN [10]
RP FUNCTION.
RX PubMed=17525181; DOI=10.1167/iovs.06-0909;
RA Jackson B.E., Mitchell B.M., Wilhelmus K.R.;
RT "Corneal virulence of Candida albicans strains deficient in Tup1-regulated
RT genes.";
RL Invest. Ophthalmol. Vis. Sci. 48:2535-2539(2007).
RN [11]
RP FUNCTION AS AN ANTIGEN.
RX PubMed=18322056; DOI=10.1128/jcm.02018-07;
RA Clancy C.J., Nguyen M.L., Cheng S., Huang H., Fan G., Jaber R.A.,
RA Wingard J.R., Cline C., Nguyen M.H.;
RT "Immunoglobulin G responses to a panel of Candida albicans antigens as
RT accurate and early markers for the presence of systemic candidiasis.";
RL J. Clin. Microbiol. 46:1647-1654(2008).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [14]
RP INDUCTION.
RX PubMed=23125349; DOI=10.1128/ec.00236-12;
RA Pierce J.V., Dignard D., Whiteway M., Kumamoto C.A.;
RT "Normal adaptation of Candida albicans to the murine gastrointestinal tract
RT requires Efg1p-dependent regulation of metabolic and host defense genes.";
RL Eukaryot. Cell 12:37-49(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, AND
RP INDUCTION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
CC -!- FUNCTION: Secreted protein that acts as a virulence factor during
CC infections such as in posttraumatic corneal infections. Acts as an
CC important antigen in patients with systemic candidiasis and plays a
CC role in the protection against phagocyte attack.
CC {ECO:0000269|PubMed:10978273, ECO:0000269|PubMed:17525181,
CC ECO:0000269|PubMed:18322056, ECO:0000269|PubMed:23136884}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20167299,
CC ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23136884}.
CC -!- INDUCTION: Induced during the switch from the yeast form to filamentous
CC growth and by fluconazole. Expression is negatively regulated by CPH2,
CC EFG1, RFG1, and TUP1. {ECO:0000269|PubMed:10790384,
CC ECO:0000269|PubMed:10978273, ECO:0000269|PubMed:11259598,
CC ECO:0000269|PubMed:11395474, ECO:0000269|PubMed:11533231,
CC ECO:0000269|PubMed:12388749, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:23125349, ECO:0000269|PubMed:23136884}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26355.1; -; Genomic_DNA.
DR RefSeq; XP_718792.2; XM_713699.2.
DR AlphaFoldDB; Q5AB48; -.
DR SMR; Q5AB48; -.
DR STRING; 237561.Q5AB48; -.
DR GeneID; 3639534; -.
DR KEGG; cal:CAALFM_C107030CA; -.
DR CGD; CAL0000174557; RBT4.
DR VEuPathDB; FungiDB:C1_07030C_A; -.
DR eggNOG; KOG3017; Eukaryota.
DR HOGENOM; CLU_035730_3_0_1; -.
DR OrthoDB; 1528782at2759; -.
DR PRO; PR:Q5AB48; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR001283; CRISP-related.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01010; CRISP_2; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..358
FT /note="Secreted protein RBT4"
FT /id="PRO_0000424914"
FT DOMAIN 216..332
FT /note="SCP"
FT REGION 48..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 37449 MW; 12BF8DD776918B8E CRC64;
MKFSQVATTA AIFAGLTTAE IAYVTQTRGV TVGETATVAT TVTVGATVTG GDQGQDQVQQ
SAAPEAGDIQ QSAVPEADDI QQSAVPEAEP TADADGGNGI AITEVFTTTI MGQEIVYSGV
YYSYGEEHTY GDVQVQTLTI GGGGFPSDDQ YPTTEVSAEA SPSAVTTSSA VATPDAKVPD
STKDASQPAA TTASGSSSGS NDFSGVKDTQ FAQQILDAHN KKRARHGVPD LTWDATVYEY
AQKFADQYSC SGNLQHSGGK YGENLAVGYA DGAAALQAWY EEAGKDGLSY SYGSSSVYNH
FTQVVWKSTT KLGCAYKDCR AQNWGLYVVC SYDPAGNVMG TDPKTGKSYM AENVLRPQ
