EXG2_CANAL
ID EXG2_CANAL Reviewed; 479 AA.
AC Q5AIA1; A0A1D8PCS8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Glucan 1,3-beta-glucosidase 2;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase 2;
DE Flags: Precursor;
GN Name=EXG2; OrderedLocusNames=CAALFM_C102630CA;
GN ORFNames=CaO19.10469, CaO19.2952;
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 AS A SUBSTRATE FOR KEX2 CLEAVAGE.
RX PubMed=12419804; DOI=10.1074/jbc.m209713200;
RA Newport G., Kuo A., Flattery A., Gill C., Blake J.J., Kurtz M.B.,
RA Abruzzo G.K., Agabian N.;
RT "Inactivation of Kex2p diminishes the virulence of Candida albicans.";
RL J. Biol. Chem. 278:1713-1720(2003).
RN [5]
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 [6]
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19824013; DOI=10.1002/pmic.200800988;
RA Cabezon V., Llama-Palacios A., Nombela C., Monteoliva L., Gil C.;
RT "Analysis of Candida albicans plasma membrane proteome.";
RL Proteomics 9:4770-4786(2009).
RN [8]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [9]
RP FUNCTION.
RX PubMed=21713010; DOI=10.1371/journal.pone.0021394;
RA Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.;
RT "Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in
RT Candida albicans adhesion by the human antimicrobial peptide LL-37.";
RL PLoS ONE 6:E21394-E21394(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=23136884; DOI=10.1111/mmi.12087;
RA Rohm M., Lindemann E., Hiller E., Ermert D., Lemuth K., Trkulja D.,
RA Sogukpinar O., Brunner H., Rupp S., Urban C.F., Sohn K.;
RT "A family of secreted pathogenesis-related proteins in Candida albicans.";
RL Mol. Microbiol. 87:132-151(2013).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. EXG2 is not heavily
CC involved in the exoglucanase function of the adhesion process.
CC {ECO:0000269|PubMed:21713010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Secreted.
CC -!- INDUCTION: Induced during cell wall regeneration and repressed by
CC HAP43. {ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:21592964}.
CC -!- PTM: Predicted to be a substrate for cleavage by KEX2.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW25944.1; -; Genomic_DNA.
DR RefSeq; XP_721451.2; XM_716358.2.
DR AlphaFoldDB; Q5AIA1; -.
DR SMR; Q5AIA1; -.
DR STRING; 237561.Q5AIA1; -.
DR GeneID; 3636816; -.
DR KEGG; cal:CAALFM_C102630CA; -.
DR CGD; CAL0000181572; EXG2.
DR VEuPathDB; FungiDB:C1_02630C_A; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR HOGENOM; CLU_004624_0_1_1; -.
DR InParanoid; Q5AIA1; -.
DR OMA; WTFVGEW; -.
DR OrthoDB; 896412at2759; -.
DR PRO; PR:Q5AIA1; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..456
FT /note="Glucan 1,3-beta-glucosidase 2"
FT /id="PRO_0000424855"
FT PROPEP 457..479
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424856"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 306
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT LIPID 456
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 54534 MW; 49580CA741366197 CRC64;
MMLFLIHLMA LCCMFVAEVA CEQFNSTSNS SSAQSSLIDF QYKGVSIGGW LVLEPYITPS
LFNATLSSGE TWTDLPVDEY HFCEKLGAKE AEKRLTDHWE SMYNETDFKQ IKEAGLNMVR
IPIGYWSFEK LEGDPYVSGA QDYLDKAIEW SHANDLKVMI DLHGAPNTQN GFDNSGLRNL
GYPGWQNKTE YVNHTYKVLQ QMFQKYGTGK YASDYKNTII GIEVLNEPLN PNMDKLKEFY
IESYNDGREI QVINNTIFFQ EAFQPIGYWD SFLEKGEIKV TETSNGTNHT TTKKADFKNI
IIDHHHYEVF TESQVASNVS THLENIKNYA SAIGKEKAKA IVGEWSAALT DCAPWLNGVG
LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF VEMQLYEYST NSQGWIFWCW
KTEGATEWDF RALVKNGIMP QPLDNYKYVK NGTDTSSASA IASNKMTLLL AFLLVILVI
