CRH12_CANAL
ID CRH12_CANAL Reviewed; 504 AA.
AC Q5AK54; A0A1D8PP35;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Extracellular glycosidase CRH12;
DE EC=3.2.-.-;
DE AltName: Full=Congo red hypersensitive protein 12;
DE Flags: Precursor;
GN Name=CRH12; Synonyms=CRH1, CRH2; OrderedLocusNames=CAALFM_C504800WA;
GN ORFNames=CaO19.11448, CaO19.3966;
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=11532938; DOI=10.1093/emboj/20.17.4742;
RA Murad A.M., Leng P., Straffon M., Wishart J., Macaskill S., MacCallum D.,
RA Schnell N., Talibi D., Marechal D., Tekaia F., d'Enfert C., Gaillardin C.,
RA Odds F.C., Brown A.J.;
RT "NRG1 represses yeast-hypha morphogenesis and hypha-specific gene
RT expression in Candida albicans.";
RL EMBO J. 20:4742-4752(2001).
RN [5]
RP INDUCTION.
RX PubMed=11737641; DOI=10.1046/j.1365-2958.2001.02713.x;
RA Murad A.M., d'Enfert C., Gaillardin C., Tournu H., Tekaia F., Talibi D.,
RA Marechal D., Marchais V., Cottin J., Brown A.J.;
RT "Transcript profiling in Candida albicans reveals new cellular functions
RT for the transcriptional repressors CaTup1, CaMig1 and CaNrg1.";
RL Mol. Microbiol. 42:981-993(2001).
RN [6]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12734798; DOI=10.1002/yea.988;
RA Lee S.A., Wormsley S., Kamoun S., Lee A.F., Joiner K., Wong B.;
RT "An analysis of the Candida albicans genome database for soluble secreted
RT proteins using computer-based prediction algorithms.";
RL Yeast 20:595-610(2003).
RN [7]
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 [8]
RP DISRUPTION PHENOTYPE, 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 [9]
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).
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
CC {ECO:0000269|PubMed:16455273}. Membrane {ECO:0000250}; Lipid-anchor,
CC GPI-anchor {ECO:0000250}. Note=Covalently-linked GPI-modified cell wall
CC protein (GPI-CWP).
CC -!- INDUCTION: Unlike CRH11, CRH12 is down-regulated during cell wall
CC regeneration. Also regulated by NRG1, TUP1, and RIM101.
CC {ECO:0000269|PubMed:11532938, ECO:0000269|PubMed:11737641,
CC ECO:0000269|PubMed:15554973, ECO:0000269|PubMed:16455273}.
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 -!- 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; CP017627; AOW29885.1; -; Genomic_DNA.
DR RefSeq; XP_721875.1; XM_716782.2.
DR AlphaFoldDB; Q5AK54; -.
DR SMR; Q5AK54; -.
DR STRING; 237561.Q5AK54; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 3636447; -.
DR KEGG; cal:CAALFM_C504800WA; -.
DR CGD; CAL0000195515; CRH12.
DR VEuPathDB; FungiDB:C5_04800W_A; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_2_1_1; -.
DR InParanoid; Q5AK54; -.
DR OMA; GRYHEMH; -.
DR OrthoDB; 1209387at2759; -.
DR PRO; PR:Q5AK54; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..479
FT /note="Extracellular glycosidase CRH12"
FT /id="PRO_0000424861"
FT PROPEP 480..504
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424862"
FT DOMAIN 19..270
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 304..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 479
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 56950 MW; FC6BD4FF9CD4C68B CRC64;
MYKQILTFLI LFLRYILSEF PDDPYEDDDT SDDNNSDYEG QKCNPYRDKA CLVNDEALGK
KIFESFAEGT KYFTITSSTR GVRFGSEGLA LTIQDEFDNP ALVSSFYIMY GKVEAEIKGA
AGKGIISSFY LQSDDLDEID VVEIFGSDPY EFQTNFFIKG NTTTYDRGRY HEMHPSPLSE
FHKYGIEWSP DLITWYLDDK PVRMLGRRNK HGLPCSPMFL KFSLWSVEDD DEGTIAWAGG
AASFSEGPFT MHIKNLKVQD YSKALTYSYG NLRDGNWLDL RADGGYLYEG HKYCLPPKML
DKLKPTPKQE TDDDQVLTSS KSQRVATTIS EDKNTVSYYP PSATNSHTTW DRLSEWETEQ
DETGTDDTEN SDNEEEESIT AIPISKSRKG STRRLDISTQ LPPLSQNESK IAEIKNITTT
KHIHNTTTSL QISKIKSKKV GVTTTIYSSS TPQSTSKSRM PYNIFFNYPG KENSRFKSGV
SSILATSFSS VVIAEILVIV VLLL
