CSA1_CANAL
ID CSA1_CANAL Reviewed; 1018 AA.
AC G1UB63; A0A1D8PQH2;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Cell wall protein 1;
DE AltName: Full=Surface antigen protein 1;
DE AltName: Full=Wall protein 1;
DE Flags: Precursor;
GN Name=CSA1; Synonyms=WAP1; OrderedLocusNames=CAALFM_C700090CA;
GN ORFNames=CaO19.7114;
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 IDENTIFICATION IN THE RBT5 FAMILY, 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 SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10652105; DOI=10.1046/j.1365-2958.2000.01715.x;
RA Lamarre C., Deslauriers N., Bourbonnais Y.;
RT "Expression cloning of the Candida albicans CSA1 gene encoding a mycelial
RT surface antigen by sorting of Saccharomyces cerevisiae transformants with
RT monoclonal antibody-coated magnetic beads.";
RL Mol. Microbiol. 35:444-453(2000).
RN [7]
RP INDUCTION.
RX PubMed=12455696; DOI=10.1128/ec.1.5.787-798.2002;
RA Bensen E.S., Filler S.G., Berman J.;
RT "A forkhead transcription factor is important for true hyphal as well as
RT yeast morphogenesis in Candida albicans.";
RL Eukaryot. Cell 1:787-798(2002).
RN [8]
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 [9]
RP HEME-BINDING, AND FUNCTION.
RX PubMed=15306022; DOI=10.1111/j.1365-2958.2004.04199.x;
RA Weissman Z., Kornitzer D.;
RT "A family of Candida cell surface haem-binding proteins involved in haemin
RT and haemoglobin-iron utilization.";
RL Mol. Microbiol. 53:1209-1220(2004).
RN [10]
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 [11]
RP INDUCTION.
RX PubMed=15790671; DOI=10.1093/jac/dki089;
RA Sigle H.C., Thewes S., Niewerth M., Korting H.C., Schafer-Korting M.,
RA Hube B.;
RT "Oxygen accessibility and iron levels are critical factors for the
RT antifungal action of ciclopirox against Candida albicans.";
RL J. Antimicrob. Chemother. 55:663-673(2005).
RN [12]
RP FUNCTION, AND DOMAIN.
RX PubMed=17042757; DOI=10.1111/j.1567-1364.2006.00131.x;
RA Perez A., Pedros B., Murgui A., Casanova M., Lopez-Ribot J.L.,
RA Martinez J.P.;
RT "Biofilm formation by Candida albicans mutants for genes coding fungal
RT proteins exhibiting the eight-cysteine-containing CFEM domain.";
RL FEMS Yeast Res. 6:1074-1084(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19555771; DOI=10.1016/j.fgb.2009.06.005;
RA Maddi A., Bowman S.M., Free S.J.;
RT "Trifluoromethanesulfonic acid-based proteomic analysis of cell wall and
RT secreted proteins of the ascomycetous fungi Neurospora crassa and Candida
RT albicans.";
RL Fungal Genet. Biol. 46:768-781(2009).
RN [14]
RP INDUCTION.
RX PubMed=21843869; DOI=10.1016/j.chom.2011.07.005;
RA Chen C., Pande K., French S.D., Tuch B.B., Noble S.M.;
RT "An iron homeostasis regulatory circuit with reciprocal roles in Candida
RT albicans commensalism and pathogenesis.";
RL Cell Host Microbe 10:118-135(2011).
RN [15]
RP INDUCTION, AND FUNCTION.
RX PubMed=21205162; DOI=10.1111/j.1567-1364.2010.00714.x;
RA Perez A., Ramage G., Blanes R., Murgui A., Casanova M., Martinez J.P.;
RT "Some biological features of Candida albicans mutants for genes coding
RT fungal proteins containing the CFEM domain.";
RL FEMS Yeast Res. 11:273-284(2011).
RN [16]
RP INDUCTION.
RX PubMed=22145027; DOI=10.1371/journal.pone.0028151;
RA Ding C., Vidanes G.M., Maguire S.L., Guida A., Synnott J.M., Andes D.R.,
RA Butler G.;
RT "Conserved and divergent roles of Bcr1 and CFEM proteins in Candida
RT parapsilosis and Candida albicans.";
RL PLoS ONE 6:E28151-E28151(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23243062; DOI=10.1128/ec.00278-12;
RA Heilmann C.J., Sorgo A.G., Mohammadi S., Sosinska G.J., de Koster C.G.,
RA Brul S., de Koning L.J., Klis F.M.;
RT "Surface stress induces a conserved cell wall stress response in the
RT pathogenic fungus Candida albicans.";
RL Eukaryot. Cell 12:254-264(2013).
RN [18]
RP INDUCTION.
RX PubMed=23563485; DOI=10.1128/ec.00071-13;
RA Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
RT "Identification of genes upregulated by the transcription factor Bcr1 that
RT are involved in impermeability, impenetrability, and drug resistance of
RT Candida albicans a/alpha biofilms.";
RL Eukaryot. Cell 12:875-888(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=23728625; DOI=10.1099/mic.0.065599-0;
RA Sorgo A.G., Brul S., de Koster C.G., de Koning L.J., Klis F.M.;
RT "Iron restriction-induced adaptations in the wall proteome of Candida
RT albicans.";
RL Microbiology 159:1673-1682(2013).
CC -!- FUNCTION: Heme-binding protein involved in heme-iron utilization. The
CC ability to acquire iron from host tissues is a major virulence factor
CC of pathogenic microorganisms. Required for biofilm formation.
CC {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:17042757,
CC ECO:0000269|PubMed:21205162}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10652105,
CC ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:23243062,
CC ECO:0000269|PubMed:23728625}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Preferentially expressed during the mycelial growth phase
CC with only low levels of transcript detected in the yeast form. Induced
CC by iron starvation and ciclopirox. Positively regulated by BCR1 and
CC RIM101, and repressed by TUP1. Expression is also regulated by EFG1,
CC CPH1, HAP43, and SEF1. {ECO:0000269|PubMed:10652105,
CC ECO:0000269|PubMed:10790384, ECO:0000269|PubMed:10978273,
CC ECO:0000269|PubMed:12455696, ECO:0000269|PubMed:15554973,
CC ECO:0000269|PubMed:15790671, ECO:0000269|PubMed:21205162,
CC ECO:0000269|PubMed:21843869, ECO:0000269|PubMed:22145027,
CC ECO:0000269|PubMed:23243062, ECO:0000269|PubMed:23563485,
CC ECO:0000269|PubMed:23728625}.
CC -!- DOMAIN: The CFEM domain is involved in heme-binding. It contains 8
CC cysteines and is found in proteins from several pathogenic fungi,
CC including both human and plant pathogens.
CC {ECO:0000250|UniProtKB:Q59UT5, ECO:0000269|PubMed:17042757}.
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.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RBT5 family. {ECO:0000305}.
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DR EMBL; CP017629; AOW30388.1; -; Genomic_DNA.
DR RefSeq; XP_720404.1; XM_715311.1.
DR AlphaFoldDB; G1UB63; -.
DR SMR; G1UB63; -.
DR STRING; 237561.G1UB63; -.
DR GeneID; 3638009; -.
DR KEGG; cal:CAALFM_C700090CA; -.
DR CGD; CAL0000201940; CSA1.
DR VEuPathDB; FungiDB:C7_00090C_A; -.
DR eggNOG; ENOG502SD7M; Eukaryota.
DR HOGENOM; CLU_010164_0_0_1; -.
DR InParanoid; G1UB63; -.
DR OrthoDB; 1627841at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0046658; C:anchored component of plasma membrane; IMP:CGD.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005933; C:cellular bud; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR InterPro; IPR008427; Extracellular_membr_CFEM_dom.
DR Pfam; PF05730; CFEM; 4.
DR SMART; SM00747; CFEM; 4.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Heme; Iron; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal; Virulence.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..989
FT /note="Cell wall protein 1"
FT /id="PRO_0000424777"
FT PROPEP 990..1018
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424778"
FT REGION 54..117
FT /note="CFEM 1"
FT /evidence="ECO:0000303|PubMed:17042757"
FT REGION 147..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..308
FT /note="CFEM 2"
FT /evidence="ECO:0000303|PubMed:17042757"
FT REGION 338..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..478
FT /note="CFEM 3"
FT /evidence="ECO:0000303|PubMed:17042757"
FT REGION 507..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..640
FT /note="CFEM 4"
FT /evidence="ECO:0000303|PubMed:17042757"
FT REGION 677..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 989
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1018 AA; 103515 MW; BA25AF72061A001A CRC64;
MLPSIVISIV LASFVSAESS ITEAPTTTAE DNPYTIYPSV AKTASINGFA DRIYDQLPEC
AKPCMFQNTG VTPCPYWDTG CLCIMPTFAG AIGSCIAEKC KGQDVVSATS LGTSICSVAG
VWDPYWMVPA NVQSSLSAAA TAVASSSEQP VETSSEPAGS SQSVESSQPA ETSSSEPAET
SSSEPAETSS ETSSEQPASS EPAETSSEES STITSAPSTP EDNPYTIYPS VAKTASINGF
ADRIYDQLPE CAKPCMFQNT GVTPCPYWDT GCLCIMPTFA GAIGSCIAEK CKGQDVVSAT
SLGTSICSVA GVWDPYWMVP ANVQSSLSAA ATAVPSSSEQ SVETSSESAE SSQSVESSQP
AETSSEQPSE TSSETSSQQL SSITSAPDSS ATSSSSTTST FIRTASINGF ADKLYDQLPE
CAKPCMFQNT GITPCPYWDA GCLCVMPQFA GAIGSCVADS CKGQDIVSVT SLGTSVCSVA
GVNAPYWMLP ASVKSSLSVA ATAVPTSDSA SETASQEPSE TSSEQPSETA SQQPAETSSE
ESSTITSAPS TPEDNPYTIY PSVAKTASIN GFADRIYDQL PECAKPCMFQ NTGVTPCPYW
DTGCLCIMPT FAGAIGSCIA EKCKGQDVVS ATSLGSSICS VAGVWDPYWM LPANVQSSLN
AAATAVATSD SASEVASASE SASQVPQETS AASSQSANNS VASAAPSNSS VSAAPSSNSS
GVPAAPSNNS SGASVVPSQS ANNSSASAAP SNNSSSAISE SVAPSSYGNS TIAQPSTSTK
SDAASITGPI TTDKVITNES GIVFTSTVII THVSEYCDQT SAAAVQSSAC EEQSSAKSEQ
ASASSEQVKV ITSVVWCESS IQSIESVKTS AEAAHKTEVI ASCASELSSL SSAKSEAMKT
VSSLVEVQKS AVAKQTSLAA VQSSAASVQL SAAHAQKSSE AVEVAQTAVA EASKAGDEIS
TEIVNITKTV SSGKETGVSQ ATVAANTHSV AIANMANTKF ASTMSLLVAS FVFVGLFI
