UTR2_CANAL
ID UTR2_CANAL Reviewed; 470 AA.
AC Q5AJC0; A0A1D8PJ91;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Extracellular glycosidase UTR2;
DE EC=3.2.-.-;
DE AltName: Full=Cell-surface factor 4;
DE Flags: Precursor;
GN Name=UTR2; Synonyms=CSF4; OrderedLocusNames=CAALFM_C301730CA;
GN ORFNames=CaO19.1671, CaO19.9240;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
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 [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND 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 [9]
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 [10]
RP INDUCTION.
RX PubMed=20859005;
RA Kaneko Y., Ohno H., Kohno S., Miyazaki Y.;
RT "Micafungin alters the expression of genes related to cell wall integrity
RT in Candida albicans biofilms.";
RL Jpn. J. Infect. Dis. 63:355-357(2010).
RN [11]
RP FUNCTION.
RX PubMed=20361054; DOI=10.1371/journal.ppat.1000827;
RA Mochon A.B., Jin Y., Kayala M.A., Wingard J.R., Clancy C.J., Nguyen M.H.,
RA Felgner P., Baldi P., Liu H.;
RT "Serological profiling of a Candida albicans protein microarray reveals
RT permanent host-pathogen interplay and stage-specific responses during
RT candidemia.";
RL PLoS Pathog. 6:E1000827-E1000827(2010).
RN [12]
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 [13]
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 [14]
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 [15]
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 [16]
RP INDUCTION.
RX PubMed=22530691; DOI=10.1042/bj20112166;
RA Jiang L., Alber J., Wang J., Du W., Yang X., Li X., Sanglard D., Geyer J.;
RT "The Candida albicans plasma membrane protein Rch1p, a member of the
RT vertebrate SLC10 carrier family, is a novel regulator of cytosolic Ca2+
RT homoeostasis.";
RL Biochem. J. 444:497-502(2012).
RN [17]
RP INDUCTION.
RX PubMed=22713118; DOI=10.1111/j.1567-1364.2012.00822.x;
RA Nagao J., Cho T., Uno J., Ueno K., Imayoshi R., Nakayama H., Chibana H.,
RA Kaminishi H.;
RT "Candida albicans Msi3p, a homolog of the Saccharomyces cerevisiae Sse1p of
RT the Hsp70 family, is involved in cell growth and fluconazole tolerance.";
RL FEMS Yeast Res. 12:728-737(2012).
RN [18]
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).
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. Plays a role of cell
CC surface antigen in acute candidemia patients.
CC {ECO:0000269|PubMed:15042589, ECO:0000269|PubMed:17074760,
CC ECO:0000269|PubMed:20361054}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:16455273,
CC ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:18712765,
CC ECO:0000269|PubMed:20641015, 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: Up-regulated by heat stress, calcineurin, micafungin, and
CC fluconazole. Protein abundance is increased at pH 4 compared to pH 7.
CC Expression is also regulated by RCH1. {ECO:0000269|PubMed:16455273,
CC ECO:0000269|PubMed:17074760, ECO:0000269|PubMed:18227255,
CC ECO:0000269|PubMed:20859005, ECO:0000269|PubMed:20864472,
CC ECO:0000269|PubMed:21602216, ECO:0000269|PubMed:21622905,
CC ECO:0000269|PubMed:22530691, ECO:0000269|PubMed:22713118,
CC ECO:0000269|PubMed:23243062}.
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, defect in filamentation, reduction in adherence to
CC mammalian cells in an in vitro adhesion assay, and a prolongation of
CC survival in an immunocompetent mouse model of disseminated candidiasis.
CC {ECO:0000269|PubMed:15042589, ECO:0000269|PubMed:17074760}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017625; AOW28214.1; -; Genomic_DNA.
DR RefSeq; XP_721748.1; XM_716655.1.
DR AlphaFoldDB; Q5AJC0; -.
DR SMR; Q5AJC0; -.
DR BioGRID; 1219685; 2.
DR STRING; 237561.Q5AJC0; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR GeneID; 3636591; -.
DR KEGG; cal:CAALFM_C301730CA; -.
DR CGD; CAL0000175165; UTR2.
DR VEuPathDB; FungiDB:C3_01730C_A; -.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR HOGENOM; CLU_040459_0_0_1; -.
DR InParanoid; Q5AJC0; -.
DR OMA; CYDPPSG; -.
DR OrthoDB; 1209387at2759; -.
DR PRO; PR:Q5AJC0; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
DR GO; GO:0030428; C:cell septum; IMP:CGD.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IEA:EnsemblFungi.
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: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:0044406; P:adhesion of symbiont to host; IMP:CGD.
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 GO; GO:0070783; P:growth of unicellular organism as a thread of attached cells; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..440
FT /note="Extracellular glycosidase UTR2"
FT /id="PRO_0000424857"
FT PROPEP 441..470
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424858"
FT DOMAIN 95..282
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 347..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 440
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 51706 MW; 7385EA9162E8A272 CRC64;
MRFSTLHFAF LATLSSIFTV VAASDTTTCS SSKHCPEDKP CCSQFGICGT GAYCLGGCDI
RYSYNLTACM PMPRMSTFQE SFDSKDKVKE IELQSDYLGN STEADWVYTG WVDYYDNSLL
IQMPNHTTGT VVSSTKYLWY GKVGATLKTS HDGGVVTAFI LFSDVQDEID YEFVGYNLTN
PQSNYYSQGI LNYNNSRNSS VNNTFEYYHN YEMDWTEDKI EWYIDGEKVR TLNKNDTWNE
TSNRYDYPQT PSRIQFSLWP GGDSSNAKGT IEWAGGLINW DSEDIKKYGY YYAHIKEIYA
TAYDIPNDVK LDGNSTKESD YHAFLYNSTD GDASNIMLTT KKTWLGSDDA TGFDPQNDDE
DSSSNKAQET TITSVSGSST ITSVKTDSTK KTANVPAQNT AAAAQATAKS STGTNTYDPS
AGVGGFVQDS KSTDSGSSGS SSQGVANSLN ESVISGIFAS ICLGILSFFM
