RBR3_CANAL
ID RBR3_CANAL Reviewed; 1562 AA.
AC Q5A5M7; A0A1D8PRA0; Q5A5F8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cell wall protein RBR3;
DE AltName: Full=Repressed by RIM101 protein 3;
DE Flags: Precursor;
GN Name=RBR3; Synonyms=IFF1; OrderedLocusNames=CAALFM_C703290CA;
GN ORFNames=CaO19.12589, CaO19.5124;
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=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 [5]
RP IDENTIFICATION IN THE HYR1/IFF FAMILY, AND PREDICTION OF GPI-ANCHOR.
RX PubMed=17371861; DOI=10.1128/iai.00102-07;
RA Bates S., de la Rosa J.M., MacCallum D.M., Brown A.J., Gow N.A., Odds F.C.;
RT "Candida albicans Iff11, a secreted protein required for cell wall
RT structure and virulence.";
RL Infect. Immun. 75:2922-2928(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21841123; DOI=10.1128/ec.05044-11;
RA Boisrame A., Cornu A., Da Costa G., Richard M.L.;
RT "Unexpected role for a serine/threonine-rich domain in the Candida albicans
RT Iff protein family.";
RL Eukaryot. Cell 10:1317-1330(2011).
CC -!- FUNCTION: GPI-anchored cell wall protein involved in cell wall
CC organization, hyphal growth, as well as in host-fungal interaction and
CC virulence. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:21841123}. Membrane {ECO:0000250}; Lipid-anchor,
CC GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall
CC protein (GPI-CWP). {ECO:0000250}.
CC -!- INDUCTION: Expression is repressed by RIM101.
CC {ECO:0000269|PubMed:15189998}.
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 -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017629; AOW30673.1; -; Genomic_DNA.
DR RefSeq; XP_711686.2; XM_706594.2.
DR AlphaFoldDB; Q5A5M7; -.
DR STRING; 237561.Q5A5M7; -.
DR GeneID; 3646728; -.
DR KEGG; cal:CAALFM_C703290CA; -.
DR CGD; CAL0000184067; RBR3.
DR VEuPathDB; FungiDB:C7_03290C_A; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_023496_1_0_1; -.
DR OrthoDB; 1483197at2759; -.
DR PRO; PR:Q5A5M7; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt.
DR InterPro; IPR031573; Cell_wall_rpt.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
DR Pfam; PF15789; Hyr1; 10.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1538
FT /note="Cell wall protein RBR3"
FT /id="PRO_0000426733"
FT PROPEP 1539..1562
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000426734"
FT REGION 338..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1538
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1562 AA; 157106 MW; 1B7843C8F38A409A CRC64;
MIIFRKSFFT FWLLLNSVLA LVITQNRVDR GTLDLSVGDI TINSGASWSI INNAISTLVG
SLTVQPNAGL YITSTSPLLS LQVTLTSLLS TIQNNGIIAF NSSPSLTSST YNLVGLSLVN
TGEMYFSASG VLPSVMALTA ASWSNSGLMA FYQNQRSSGV VSLGTPLGSI TNNGQICLNN
EVYQQTTSIN GSGCFTANRD STIYIANVLL PVSTSQNFYL ADSQSSIIVQ AILTPQVFNV
YGFGNGNMVG VTLPLLGNIL NPAYSYNPST GILRLRNLLV YQDFNIGPGY NPSLFSIVTD
NGAGLPSTIL GSVSYSGPVP PRALPASCKI ACKPVPTAPG TNPTEYTTTI TTTNSAGKPL
TETGVVDIST DSNGSWFSST TIFPTSSSSS SSSSTVSSTA PSSSSTKPSS SSQPSSTPPP
SSSSKASSTT PSSSSQSSST TPSSSSKPSS TVPPTGSSQS SSTIPSSSTQ PSSTAPSSLS
SPSSSTTPSS SSQSSFSAQS SIGQTSSSTV SSSSSQPSSS QPSSSQSSSA TTSSSSQFSS
SAPPSSTQSS FTAESSNSQL SSTTPSSSTE ASSTVPSSSS QLSSSVPLTN SVSLSSVSSS
DNGSSSASSP SSSQSSIAST AESSSTFPSS SDQQSSSIQS PSSQESSVSS TPTSSLQSST
NTISSSQDSS SFSPTTSDNS STNSASSLST LSSSDTSVSN PSTSNVSSTD NTQSSVASAT
PTDSAISATS SDITTEFTTT WEVTNSDGSV STESGIVSES GTSFTTITTF PPPTTSSDIT
TEFTTTWEVT NSDGSVSTES GIVSESGTSF TTITTFPPPT TSSDITTEFT TTWEVTNSDG
SVSTESGIVS ESGTSFTTIT TFPPPTTSSD ITTEFTTTWE VTNSDGSVST ESGIVSESGT
SFTTITTFPP PTSSSVAADV TTEFTTTWEV TNSDGSVSTE SGIVSESGTS FTTITTFELP
VVCKRDDISC GPATSATNSD TAAQDPTSDA TAIESEFTTT WTTTNSDGSV ETNSGVVSQS
GSSLTTITTF APDATSEYTT SWTTTNSDGS VATNSGVVSQ SGTSFTTITT FEPPVVCKRD
DISCGPATSA MNSDTAAQQL TSGMTATETE FASTWVVTKS DGSVFTESGI VGQSGTSFTT
LTTFAPTTSS GAVQTEYTST WEVTNTDGSV STKSGIIDQS GTYFTTLSTF APTTISGAIE
TEFTSTWVAT DTDGLVSTKS GIVSQSGTSI ATLTIFPEPA GTVYPVTTLF TTEYVTTCPN
GELSTATGVV VVSTDSKGIE QTVTSVVPST VYTKETVTSI ITHCIKNKCF ESTTTLVSSV
PCPTQVPGVF TSTDNGHGVP IASIDVTTGA ATVSNTIKAQ DSTGFTSAGN AITTAITATG
AVTTSVGGQG STDYSNAGNT IAAGSGSDSG SGSGSGSGSG SSSNTVGIVN PKVSSAASGI
TVAAASASAG QSWPYSSGGS GNGVLPSGAN NVGSNQTPTV SGGNSNPSTV TGAAVGAGGV
VSGSPSYSGN SLLISFVSSQ SGAISSSTGV TIPIATENSG SKFSVGKSAF IAIILTTFIG
FI
