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Q5AIA1

- EXG2_CANAL

UniProt

Q5AIA1 - EXG2_CANAL

Protein

Glucan 1,3-beta-glucosidase 2

Gene

EXG2

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (26 Apr 2005)
      Previous versions | rss
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    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

    1. glucan exo-1,3-beta-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
    ProteomesiUP000000559: Unassembled WGS sequence

    Organism-specific databases

    CGDiCAL0006050. EXG2.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of plasma membrane Source: CGD
    2. cell surface Source: CGD
    3. extracellular region Source: UniProtKB-SubCell

    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

    Interactioni

    Protein-protein interaction databases

    STRINGi5476.CAL0006050.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5AIA1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG2730.
    KOiK01210.

    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

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    MMLFLIHLMA LCCMFVAEVA CEQFNSTSNS SSAQSSLIDF QYKGVSIGGW    50
    LVLEPYITPS LFNATLSSGE TWTDLPVDEY HFCEKLGAKE AEKRLTDHWE 100
    SMYNETDFKQ IKEAGLNMVR IPIGYWSFEK LEGDPYVSGA QDYLDKAIEW 150
    SHANDLKVMI DLHGAPNTQN GFDNSGLRNL GYPGWQNKTE YVNHTYKVLQ 200
    QMFQKYGTGK YASDYKNTII GIEVLNEPLN PNMDKLKEFY IESYNDGREI 250
    QVINNTIFFQ EAFQPIGYWD SFLEKGEIKV TETSNGTNHT TTKKADFKNI 300
    IIDHHHYEVF TESQVASNVS THLENIKNYA SAIGKEKAKA IVGEWSAALT 350
    DCAPWLNGIG LGSRYEGTAP YTNDRVGSCA EFNKSPDKWS KKQKKDYRRF 400
    VEMQLYEYST NSQGWIFWCW KTEGATEWDF RALVKNGIMP QPLDNYKYVK 450
    NGTDTSSASA IASNKMTLLL AFLLVILVI 479
    Length:479
    Mass (Da):54,548
    Last modified:April 26, 2005 - v1
    Checksum:i44C813A741367E97
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AACQ01000017 Genomic DNA. Translation: EAL02371.1 .
    AACQ01000015 Genomic DNA. Translation: EAL02652.1 .
    RefSeqi XP_721179.1. XM_716086.1.
    XP_721451.1. XM_716358.1.

    3D structure databases

    ProteinModelPortali Q5AIA1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5476.CAL0006050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3636816.
    3637086.
    KEGGi cal:CaO19.10469.
    cal:CaO19.2952.

    Organism-specific databases

    CGDi CAL0006050. EXG2.

    Phylogenomic databases

    eggNOGi COG2730.
    KOi K01210.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001547. Glyco_hydro_5.
    IPR018087. Glyco_hydro_5_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00150. Cellulase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 62 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