RBT1_CANAL
ID RBT1_CANAL Reviewed; 721 AA.
AC Q59TP1; A0A1D8PLU6; Q59TK9;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cell wall protein RBT1;
DE AltName: Full=Repressed by TUP1 protein 1;
DE Flags: Precursor;
GN Name=RBT1; Synonyms=RBT99; OrderedLocusNames=CAALFM_C403520CA;
GN ORFNames=CaO19.1327, CaO19.8907;
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 FUNCTION, AND INDUCTION.
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=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 [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=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 [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=14585977; DOI=10.1128/mcb.23.22.8189-8201.2003;
RA Bennett R.J., Uhl M.A., Miller M.G., Johnson A.D.;
RT "Identification and characterization of a Candida albicans mating
RT pheromone.";
RL Mol. Cell. Biol. 23:8189-8201(2003).
RN [10]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [11]
RP INDUCTION.
RX PubMed=15189998; DOI=10.1128/ec.3.3.776-784.2004;
RA Lotz H., Sohn K., Brunner H., Muhlschlegel F.A., Rupp S.;
RT "RBR1, a novel pH-regulated cell wall gene of Candida albicans, is
RT repressed by RIM101 and activated by NRG1.";
RL Eukaryot. Cell 3:776-784(2004).
RN [12]
RP INDUCTION.
RX PubMed=15269278; DOI=10.1091/mbc.e04-02-0144;
RA Harcus D., Nantel A., Marcil A., Rigby T., Whiteway M.;
RT "Transcription profiling of cyclic AMP signaling in Candida albicans.";
RL Mol. Biol. Cell 15:4490-4499(2004).
RN [13]
RP INDUCTION.
RX PubMed=16002644; DOI=10.1128/ec.4.7.1175-1190.2005;
RA Zhao R., Daniels K.J., Lockhart S.R., Yeater K.M., Hoyer L.L., Soll D.R.;
RT "Unique aspects of gene expression during Candida albicans mating and
RT possible G(1) dependency.";
RL Eukaryot. Cell 4:1175-1190(2005).
RN [14]
RP INDUCTION.
RX PubMed=16002646; DOI=10.1128/ec.4.7.1203-1210.2005;
RA Enjalbert B., Whiteway M.;
RT "Release from quorum-sensing molecules triggers hyphal formation during
RT Candida albicans resumption of growth.";
RL Eukaryot. Cell 4:1203-1210(2005).
RN [15]
RP FUNCTION.
RX PubMed=18069889; DOI=10.1371/journal.ppat.0030184;
RA White S.J., Rosenbach A., Lephart P., Nguyen D., Benjamin A., Tzipori S.,
RA Whiteway M., Mecsas J., Kumamoto C.A.;
RT "Self-regulation of Candida albicans population size during GI
RT colonization.";
RL PLoS Pathog. 3:E184-E184(2007).
RN [16]
RP INDUCTION.
RX PubMed=18424510; DOI=10.1128/ec.00357-07;
RA Kebaara B.W., Langford M.L., Navarathna D.H., Dumitru R., Nickerson K.W.,
RA Atkin A.L.;
RT "Candida albicans Tup1 is involved in farnesol-mediated inhibition of
RT filamentous-growth induction.";
RL Eukaryot. Cell 7:980-987(2008).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=18765290; DOI=10.1016/j.fgb.2008.08.003;
RA Plaine A., Walker L., Da Costa G., Mora-Montes H.M., McKinnon A., Gow N.A.,
RA Gaillardin C., Munro C.A., Richard M.L.;
RT "Functional analysis of Candida albicans GPI-anchored proteins: roles in
RT cell wall integrity and caspofungin sensitivity.";
RL Fungal Genet. Biol. 45:1404-1414(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18712765; DOI=10.1002/pmic.200800110;
RA Castillo L., Calvo E., Martinez A.I., Ruiz-Herrera J., Valentin E.,
RA Lopez J.A., Sentandreu R.;
RT "A study of the Candida albicans cell wall proteome.";
RL Proteomics 8:3871-3881(2008).
RN [19]
RP FUNCTION.
RX PubMed=19837954; DOI=10.1128/ec.00245-09;
RA Ene I.V., Bennett R.J.;
RT "Hwp1 and related adhesins contribute to both mating and biofilm formation
RT in Candida albicans.";
RL Eukaryot. Cell 8:1909-1913(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20641015; DOI=10.1002/yea.1775;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Brul S., de Koster C.G., Klis F.M.;
RT "Mass spectrometric analysis of the secretome of Candida albicans.";
RL Yeast 27:661-672(2010).
RN [21]
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20864472; DOI=10.1099/mic.0.044206-0;
RA Sosinska G.J., de Koning L.J., de Groot P.W., Manders E.M., Dekker H.L.,
RA Hellingwerf K.J., de Koster C.G., Klis F.M.;
RT "Mass spectrometric quantification of the adaptations in the wall proteome
RT of Candida albicans in response to ambient pH.";
RL Microbiology 157:136-146(2011).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21602216; DOI=10.1099/mic.0.049395-0;
RA Heilmann C.J., Sorgo A.G., Siliakus A.R., Dekker H.L., Brul S.,
RA de Koster C.G., de Koning L.J., Klis F.M.;
RT "Hyphal induction in the human fungal pathogen Candida albicans reveals a
RT characteristic wall protein profile.";
RL Microbiology 157:2297-2307(2011).
CC -!- FUNCTION: GPI-anchored cell wall protein required for mating
CC efficiency, biofilm formation, and virulence. Involved in normal
CC disseminated infection, but not in intestinal colonization.
CC {ECO:0000269|PubMed:10978273, ECO:0000269|PubMed:14585977,
CC ECO:0000269|PubMed:18069889, ECO:0000269|PubMed:19837954}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:18712765,
CC ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:21622905}. Membrane;
CC Lipid-anchor, GPI-anchor.
CC -!- INDUCTION: Expression is negatively regulated by the TUP1
CC transcriptional repressor. Also regulated by EFG1, RFG1 and RIM101.
CC Induced during hyphal growth, during mating process, under alkaline
CC conditions, and by farnesol. Repressed by fluconazole.
CC {ECO:0000269|PubMed:10790384, ECO:0000269|PubMed:10978273,
CC ECO:0000269|PubMed:11259598, ECO:0000269|PubMed:11595734,
CC ECO:0000269|PubMed:12388749, ECO:0000269|PubMed:14585977,
CC ECO:0000269|PubMed:15189998, ECO:0000269|PubMed:15269278,
CC ECO:0000269|PubMed:16002644, ECO:0000269|PubMed:16002646,
CC ECO:0000269|PubMed:18424510, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21622905}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to calcofluor white
CC (CFW). {ECO:0000269|PubMed:18765290}.
CC -!- SIMILARITY: Belongs to the HWP1 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW29110.1; -; Genomic_DNA.
DR RefSeq; XP_709966.2; XM_704874.2.
DR AlphaFoldDB; Q59TP1; -.
DR BioGRID; 1228470; 11.
DR STRING; 237561.Q59TP1; -.
DR GeneID; 3645377; -.
DR KEGG; cal:CAALFM_C403520CA; -.
DR CGD; CAL0000185934; RBT1.
DR VEuPathDB; FungiDB:C4_03520C_A; -.
DR eggNOG; ENOG502QSI5; Eukaryota.
DR HOGENOM; CLU_356004_0_0_1; -.
DR OrthoDB; 1362040at2759; -.
DR PRO; PR:Q59TP1; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR InterPro; IPR018789; Flo11.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR Pfam; PF13928; Flocculin_t3; 2.
DR SMART; SM01213; Flo11; 1.
DR PROSITE; PS51824; FLO11; 1.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..696
FT /note="Cell wall protein RBT1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422906"
FT PROPEP 697..721
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439092"
FT DOMAIN 55..278
FT /note="Flo11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT REGION 278..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 696
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 721 AA; 73619 MW; EB0EBDA055F59BB3 CRC64;
MRFATAQLAA LAYYILSTEA TFPLLGDIFN CIPHNTPPVC TDLGLYHDSS ISLGGSKNKR
EAEIANKDGT IEKRTFGSAG VNAGFNAAFV VSNAKKLSDG SYGIDCNFKS DSSVQLNSAF
GKKVKQLSIT GTGYSDISLL GNVANPFEWS ASLKVKAEIV KGKCCLPSGF RIVTDFESNC
PEFDAIKQFF GSSQIIYKVN AVSNAIGTFD ASALFNAQVK AFPAKRELDE FEELSNDGVT
HSKRTLGLLL GLLKKVTGGC DTLQQFCWDC QCDTPSPSTT TVSTSSAPST SPESSAPSTT
TVTTSSSPVT SPESSVPETT TVTTSSVPET TPESSAPETT TVTTSSVPST TPESSAPETT
PESSAPESSV PESSAPETTP ESSAPESSVP ESSAPETETE TTPTAHLTTT TAQTTTVITV
TSCSNNACSK TEVTTGVVVV TSEDTIYTTF CPLTETTPVP SSVDSTSVTS APETTPESTA
PESSAPESSA PESSAPVTET PTGPVSTVTE QSKTIVTITS CSNNACSESK VTTGVVVVTS
EDTVYTTFCP LTETTPATES ASESSAPATE SVPATESAPV APESSAPGTE TAPATESAPA
TESSPVAPGT ETTPATPGAE STPVTPVAPE SSAPAVESSP VAPGVETTPV APVAPSTTAK
TSALVSTTEG TIPTTLESVP AIQPSANSSY TIASVSSFEG AGNNMRLTYG AAIIGLAAFL
I
