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Protein

Glucan 1,3-beta-glucosidase 2

Gene

EXG2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. EXG2 is not heavily involved in exoglucanase function in adhesion process.1 Publication

Catalytic activityi

Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei227 – 2271Proton donorBy similarity
Active sitei306 – 3061NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Glucan 1,3-beta-glucosidase 2 (EC:3.2.1.58)
Alternative name(s):
Exo-1,3-beta-glucanase 2
Gene namesi
Name:EXG2
ORF Names:CaO19.10469, CaO19.2952
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0006050. EXG2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of plasma membrane Source: CGD
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 456435Glucan 1,3-beta-glucosidase 2PRO_0000424855Add
BLAST
Propeptidei457 – 47923Removed in mature formSequence AnalysisPRO_0000424856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi451 – 4511N-linked (GlcNAc...)Sequence Analysis
Lipidationi456 – 4561GPI-anchor amidated serineSequence Analysis

Post-translational modificationi

Predicted to be a substrate for cleavage by KEX2.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Inductioni

Induced during cell wall regeneration and repressed by HAP43.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ5AIA1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2730.
InParanoidiQ5AIA1.
KOiK01210.
OrthoDBiEOG7JT75H.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5AIA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLFLIHLMA LCCMFVAEVA CEQFNSTSNS SSAQSSLIDF QYKGVSIGGW
60 70 80 90 100
LVLEPYITPS LFNATLSSGE TWTDLPVDEY HFCEKLGAKE AEKRLTDHWE
110 120 130 140 150
SMYNETDFKQ IKEAGLNMVR IPIGYWSFEK LEGDPYVSGA QDYLDKAIEW
160 170 180 190 200
SHANDLKVMI DLHGAPNTQN GFDNSGLRNL GYPGWQNKTE YVNHTYKVLQ
210 220 230 240 250
QMFQKYGTGK YASDYKNTII GIEVLNEPLN PNMDKLKEFY IESYNDGREI
260 270 280 290 300
QVINNTIFFQ EAFQPIGYWD SFLEKGEIKV TETSNGTNHT TTKKADFKNI
310 320 330 340 350
IIDHHHYEVF TESQVASNVS THLENIKNYA SAIGKEKAKA IVGEWSAALT
360 370 380 390 400
DCAPWLNGIG LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF
410 420 430 440 450
VEMQLYEYST NSQGWIFWCW KTEGATEWDF RALVKNGIMP QPLDNYKYVK
460 470
NGTDTSSASA IASNKMTLLL AFLLVILVI
Length:479
Mass (Da):54,548
Last modified:April 26, 2005 - v1
Checksum:i44C813A741367E97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000017 Genomic DNA. Translation: EAL02371.1.
AACQ01000015 Genomic DNA. Translation: EAL02652.1.
RefSeqiXP_721179.1. XM_716086.1.
XP_721451.1. XM_716358.1.

Genome annotation databases

GeneIDi3636816.
3637086.
KEGGical:CaO19.10469.
cal:CaO19.2952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AACQ01000017 Genomic DNA. Translation: EAL02371.1.
AACQ01000015 Genomic DNA. Translation: EAL02652.1.
RefSeqiXP_721179.1. XM_716086.1.
XP_721451.1. XM_716358.1.

3D structure databases

ProteinModelPortaliQ5AIA1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3636816.
3637086.
KEGGical:CaO19.10469.
cal:CaO19.2952.

Organism-specific databases

CGDiCAL0006050. EXG2.

Phylogenomic databases

eggNOGiCOG2730.
InParanoidiQ5AIA1.
KOiK01210.
OrthoDBiEOG7JT75H.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  2. "Inactivation of Kex2p diminishes the virulence of Candida albicans."
    Newport G., Kuo A., Flattery A., Gill C., Blake J.J., Kurtz M.B., Abruzzo G.K., Agabian N.
    J. Biol. Chem. 278:1713-1720(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PREDICTION AS A SUBSTRATE FOR KEX2 CLEAVAGE.
  3. "Genome-wide identification of fungal GPI proteins."
    De Groot P.W., Hellingwerf K.J., Klis F.M.
    Yeast 20:781-796(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PREDICTION OF GPI-ANCHOR.
  4. "Genomic response programs of Candida albicans following protoplasting and regeneration."
    Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J., Ruiz-Herrera J., Valentin E., Sentandreu R.
    Fungal Genet. Biol. 43:124-134(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  5. "Analysis of Candida albicans plasma membrane proteome."
    Cabezon V., Llama-Palacios A., Nombela C., Monteoliva L., Gil C.
    Proteomics 9:4770-4786(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  6. "Cap2-HAP complex is a critical transcriptional regulator that has dual but contrasting roles in regulation of iron homeostasis in Candida albicans."
    Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.
    J. Biol. Chem. 286:25154-25170(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Characterizing the role of cell-wall beta-1,3-exoglucanase Xog1p in Candida albicans adhesion by the human antimicrobial peptide LL-37."
    Tsai P.W., Yang C.Y., Chang H.T., Lan C.Y.
    PLoS ONE 6:E21394-E21394(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiEXG2_CANAL
AccessioniPrimary (citable) accession number: Q5AIA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: April 26, 2005
Last modified: June 24, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.