CRH11_CANAL
ID CRH11_CANAL Reviewed; 453 AA.
AC Q5AFA2; A0A1D8PLP4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Extracellular glycosidase CRH11 {ECO:0000305};
DE EC=3.2.-.- {ECO:0000305};
DE AltName: Full=Congo red hypersensitive protein 11;
DE Flags: Precursor;
GN Name=CRH11; Synonyms=CRH1; OrderedLocusNames=CAALFM_C402900CA;
GN ORFNames=CaO19.10221, CaO19.2706;
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15302828; DOI=10.1128/ec.3.4.955-965.2004;
RA de Groot P.W., de Boer A.D., Cunningham J., Dekker H.L., de Jong L.,
RA Hellingwerf K.J., de Koster C., Klis F.M.;
RT "Proteomic analysis of Candida albicans cell walls reveals covalently bound
RT carbohydrate-active enzymes and adhesins.";
RL Eukaryot. Cell 3:955-965(2004).
RN [6]
RP IDENTIFICATION.
RX PubMed=15042589; DOI=10.1002/yea.1061;
RA Alberti-Segui C., Morales A.J., Xing H., Kessler M.M., Willins D.A.,
RA Weinstock K.G., Cottarel G., Fechtel K., Rogers B.;
RT "Identification of potential cell-surface proteins in Candida albicans and
RT investigation of the role of a putative cell-surface glycosidase in
RT adhesion and virulence.";
RL Yeast 21:285-302(2004).
RN [7]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16455273; DOI=10.1016/j.fgb.2005.12.002;
RA Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J.,
RA Ruiz-Herrera J., Valentin E., Sentandreu R.;
RT "Genomic response programs of Candida albicans following protoplasting and
RT regeneration.";
RL Fungal Genet. Biol. 43:124-134(2006).
RN [9]
RP DISRUPTION PHENOTYPE, INDUCTION, AND FUNCTION.
RX PubMed=17074760; DOI=10.1074/jbc.m606361200;
RA Pardini G., De Groot P.W., Coste A.T., Karababa M., Klis F.M.,
RA de Koster C.G., Sanglard D.;
RT "The CRH family coding for cell wall glycosylphosphatidylinositol proteins
RT with a predicted transglycosidase domain affects cell wall organization and
RT virulence of Candida albicans.";
RL J. Biol. Chem. 281:40399-40411(2006).
RN [10]
RP INDUCTION.
RX PubMed=16552442; DOI=10.1371/journal.ppat.0020021;
RA Bruno V.M., Kalachikov S., Subaran R., Nobile C.J., Kyratsous C.,
RA Mitchell A.P.;
RT "Control of the C. albicans cell wall damage response by transcriptional
RT regulator Cas5.";
RL PLoS Pathog. 2:E21-E21(2006).
RN [11]
RP INDUCTION.
RX PubMed=18227255; DOI=10.1099/mic.0.2007/012617-0;
RA Sosinska G.J., de Groot P.W., Teixeira de Mattos M.J., Dekker H.L.,
RA de Koster C.G., Hellingwerf K.J., Klis F.M.;
RT "Hypoxic conditions and iron restriction affect the cell-wall proteome of
RT Candida albicans grown under vagina-simulative conditions.";
RL Microbiology 154:510-520(2008).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
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=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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
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).
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=23731904; DOI=10.1016/j.ijmm.2013.05.003;
RA Yu Q., Ding X., Zhang B., Xu N., Cheng X., Qian K., Zhang B., Xing L.,
RA Li M.;
RT "The P-type ATPase Spf1 is required for endoplasmic reticulum functions and
RT cell wall integrity in Candida albicans.";
RL Int. J. Med. Microbiol. 303:257-266(2013).
CC -!- FUNCTION: Extracellular glycosidase which plays an important role in
CC fungal pathogenesis. Involved in cell wall assembly and regeneration,
CC filamentation, and adherence to host cells.
CC {ECO:0000269|PubMed:17074760}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:15302828,
CC ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:18712765,
CC ECO:0000269|PubMed:19555771, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:23243062}. Membrane
CC {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Covalently-
CC linked GPI-modified cell wall protein (GPI-CWP).
CC -!- INDUCTION: Expressed in cell walls of both yeast and hyphae cells. Up-
CC regulated by growth in hypoxic conditions, during cell wall
CC regeneration, by heat stress, as well as by calcineurin, caspofungin,
CC and fluconazole. Expression is also regulated by CAS5, RLM1, and SPF1.
CC {ECO:0000269|PubMed:15917516, ECO:0000269|PubMed:16455273,
CC ECO:0000269|PubMed:16552442, ECO:0000269|PubMed:17074760,
CC ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:19555771,
CC ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:23243062, ECO:0000269|PubMed:23731904}.
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 -!- DISRUPTION PHENOTYPE: Leads to increased susceptibility to cell wall-
CC perturbing agents. {ECO:0000269|PubMed:17074760}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017626; AOW29056.1; -; Genomic_DNA.
DR RefSeq; XP_720457.1; XM_715364.1.
DR AlphaFoldDB; Q5AFA2; -.
DR SMR; Q5AFA2; -.
DR BioGRID; 1220999; 2.
DR STRING; 237561.Q5AFA2; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 3637905; -.
DR KEGG; cal:CAALFM_C402900CA; -.
DR CGD; CAL0000181029; CRH11.
DR VEuPathDB; FungiDB:C4_02900C_A; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_2_2_1; -.
DR InParanoid; Q5AFA2; -.
DR OrthoDB; 1209387at2759; -.
DR PRO; PR:Q5AFA2; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006037; P:cell wall chitin metabolic process; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Virulence.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..430
FT /note="Extracellular glycosidase CRH11"
FT /id="PRO_0000424859"
FT PROPEP 431..453
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424860"
FT DOMAIN 28..227
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 281..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P27051"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27051"
FT LIPID 430
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 453 AA; 46733 MW; 39B0F26D12C819AB CRC64;
MKFTTLATIA STLLFAANAN ADTCNPLKSS DCSPVPALGS SFLEKFDNGL GPHFESLKKQ
GTIDSGSNGL SLTMKKRFDN PSFKSNFYIM FGRVEVVLKG AEGKGIVSSF YLQSDDLDEI
DIEMFGGDPY QWQSNYFIKG NTATYDRGGY HDIANPLKDY HTYVIDWTKD AVTWSVDGSV
IRTIPKDNAQ GFPQSPMAIY AGIWAGGDPS NQPGTIDWAG GITDYSQAPF TMGIKSVLVA
DYSSGKQYSY SDQSGSWESI KADGGKVNGR YDQAQDDIKK LESGQSVDSN DSSSSPSASS
SDSSSTSSAS SSSSSSSPSS TTSSSSSSSS SSSSSSSSSS EKSNAVPSAS VIVFIGTKGG
DKTTVTSSSG VSVPTSASVS TAAGTTSGSA NSAPASAASS TASTVFISTG DAAPSSSASE
KPSVSTTENN GAVSVAKTTS LFGFVALIGF LFV
