Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucan 1,3-beta-glucosidase

Gene

XOG1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Major glucan 1,3-beta-glucosidase required for cell wall integrity. Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. Can also function biosynthetically as a transglycosylase. Functions to deliver glucan from the cell to the extracellular matrix. Does not appear to impact cell wall glucan content of biofilm cells, nor is it necessary for filamentation or biofilm formation. Involved in cell-substrate and cell-cell adhesion. Adhesion to host-cell surfaces is the first critical step during mucosal infection. XOG1 is target of human antimicrobial peptide LL-37 for inhibition of cell adhesion.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Binding of human antimicrobial peptide LL-37 decreases the catalytic activity, which leads to the decrease of cell adhesion.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=23.0 mM for laminaribiose1 Publication
  2. KM=12.7 mM for laminaritriose1 Publication
  3. KM=5.0 mM for laminaritetraose1 Publication
  4. KM=2.6 mM for laminaripentaose1 Publication
  5. KM=2.7 mM for laminarihexaose1 Publication
  6. KM=2.4 mM for laminariheptaose1 Publication
  7. KM=3.9 mM for laminarin1 Publication
  8. KM=17.9 mM for pustulan1 Publication
  9. KM=260 mM for gentiobiose1 Publication
  10. KM=120 mM for gentiotriose1 Publication
  11. KM=70 mM for cellobiose1 Publication
  12. KM=9.4 mM for cellotetraose1 Publication
  13. KM=12.0 mM for cellohexaose1 Publication
  14. KM=2.4 mM for p-nitrophenyl-beta-glucoside (pNPG)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei65Substrate1 Publication1
    Binding sitei67Substrate1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei230Proton donorBy similarity1
    Binding sitei230Substrate1 Publication1
    Binding sitei293Substrate1 Publication1
    Binding sitei300Substrate1 Publication1
    Active sitei330Nucleophile1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionGlycosidase, Hydrolase, Transferase
    Biological processCell adhesion, Cell wall biogenesis/degradation, Virulence

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.2.1.58 1096

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P29717

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GH5 Glycoside Hydrolase Family 5

    mycoCLAP, a database of fungal genes encoding lignocellulose-active proteins

    More...
    mycoCLAPi
    EXG5A_CANAL

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Glucan 1,3-beta-glucosidase (EC:2.4.1.-1 Publication, EC:3.2.1.583 Publications)
    Alternative name(s):
    Exo-1,3-beta-glucanase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:XOG1
    Synonyms:EXG, EXG1, XOG
    Ordered Locus Names:CAALFM_C102990CA
    ORF Names:Ca49C10.05, CaO19.10507, CaO19.2990
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri237561 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000559 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Candida Genome Database

    More...
    CGDi
    CAL0000190583 XOG1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell wall, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Leads to enhanced susceptibility to the commonly used antifungal, fluconazole, during biofilm growth only.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi182F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296. 1 Publication1
    Mutagenesisi267F → A: Decreases catalytic activity. Impairs catalytic activity; when associated with Ala-296 or Ser-330. 1 Publication1
    Mutagenesisi296F → A: Impairs catalytic activity; when associated with Ala-182. 1 Publication1
    Mutagenesisi296F → W or I: Decreases catalytic activity. 1 Publication1
    Mutagenesisi330E → Q: Impairs catalytic activity. 1 Publication1
    Mutagenesisi330E → S: Impairs catalytic activity; when associated with Ala-267. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB01816 Castanospermine

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Or 25Sequence analysisAdd BLAST21
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000787822 – 382 PublicationsAdd BLAST17
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000787939 – 438Glucan 1,3-beta-glucosidaseAdd BLAST400

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi313 ↔ 4351 Publication
    Disulfide bondi338 ↔ 3641 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P29717

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    P29717

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression is maximal during the early rapid growth phase and increases during biofilm growth. Induced by caspofungin. Transcripts is also regulated by RCK2, SIT4, and HTG4.6 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer. Interacts with the human antimicrobial peptide LL-37.3 Publications

    GO - Molecular functioni

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1438
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P29717

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P29717

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P29717

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000114462

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P29717

    KEGG Orthology (KO)

    More...
    KOi
    K01210

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    APEWHFQ

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C22A6

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001547 Glyco_hydro_5
    IPR018087 Glyco_hydro_5_CS
    IPR017853 Glycoside_hydrolase_SF

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00150 Cellulase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51445 SSF51445, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00659 GLYCOSYL_HYDROL_F5, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P29717-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MQLSFILTSS VFILLLEFVK ASVISNPFKP NGNLKFKRGG GHNVAWDYDN
    60 70 80 90 100
    NVIRGVNLGG WFVLEPYMTP SLFEPFQNGN DQSGVPVDEY HWTQTLGKEA
    110 120 130 140 150
    ASRILQKHWS TWITEQDFKQ ISNLGLNFVR IPIGYWAFQL LDNDPYVQGQ
    160 170 180 190 200
    VQYLEKALGW ARKNNIRVWI DLHGAPGSQN GFDNSGLRDS YNFQNGDNTQ
    210 220 230 240 250
    VTLNVLNTIF KKYGGNEYSD VVIGIELLNE PLGPVLNMDK LKQFFLDGYN
    260 270 280 290 300
    SLRQTGSVTP VIIHDAFQVF GYWNNFLTVA EGQWNVVVDH HHYQVFSGGE
    310 320 330 340 350
    LSRNINDHIS VACNWGWDAK KESHWNVAGE WSAALTDCAK WLNGVNRGAR
    360 370 380 390 400
    YEGAYDNAPY IGSCQPMLDI SQWSDEHKTD TRRYIEAQLD AFEYTGGWVF
    410 420 430
    WSWKTENAPE WSFQTLTYNG LFPQPVTDRQ FPNQCGFH
    Length:438
    Mass (Da):50,056
    Last modified:March 15, 2017 - v5
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6FEAEA80C1B0121C
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti102S → L in CAA21969 (Ref. 2) Curated1
    Sequence conflicti193F → S in CAA21969 (Ref. 2) Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X56556 Genomic DNA Translation: CAA39908.1
    AL033497 Genomic DNA Translation: CAA21969.1
    CP017623 Genomic DNA Translation: AOW25980.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A47702
    T52149

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_721488.2, XM_716395.2

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    3636837

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    cal:CAALFM_C102990CA

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X56556 Genomic DNA Translation: CAA39908.1
    AL033497 Genomic DNA Translation: CAA21969.1
    CP017623 Genomic DNA Translation: AOW25980.1
    PIRiA47702
    T52149
    RefSeqiXP_721488.2, XM_716395.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1CZ1X-ray1.85A45-438[»]
    1EQCX-ray1.85A45-438[»]
    1EQPX-ray1.90A45-438[»]
    2PB1X-ray1.90A39-438[»]
    2PBOX-ray1.85A39-438[»]
    2PC8X-ray1.80A39-438[»]
    2PF0X-ray1.90A39-438[»]
    3N9KX-ray1.70A40-438[»]
    3O6AX-ray2.00A40-438[»]
    4M80X-ray1.86A40-438[»]
    4M81X-ray1.86A40-438[»]
    4M82X-ray1.59A40-438[»]
    ProteinModelPortaliP29717
    SMRiP29717
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    DrugBankiDB01816 Castanospermine

    Protein family/group databases

    CAZyiGH5 Glycoside Hydrolase Family 5
    mycoCLAPiEXG5A_CANAL

    Proteomic databases

    PRIDEiP29717

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi3636837
    KEGGical:CAALFM_C102990CA

    Organism-specific databases

    CGDiCAL0000190583 XOG1

    Phylogenomic databases

    HOGENOMiHOG000114462
    InParanoidiP29717
    KOiK01210
    OMAiAPEWHFQ
    OrthoDBiEOG092C22A6

    Enzyme and pathway databases

    BRENDAi3.2.1.58 1096
    SABIO-RKiP29717

    Miscellaneous databases

    EvolutionaryTraceiP29717
    PMAP-CutDBiP29717

    Protein Ontology

    More...
    PROi
    PR:P29717

    Family and domain databases

    InterProiView protein in InterPro
    IPR001547 Glyco_hydro_5
    IPR018087 Glyco_hydro_5_CS
    IPR017853 Glycoside_hydrolase_SF
    PfamiView protein in Pfam
    PF00150 Cellulase, 1 hit
    SUPFAMiSSF51445 SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS00659 GLYCOSYL_HYDROL_F5, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEXG1_CANAL
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29717
    Secondary accession number(s): A0A1D8PCW5
    , Q5AI63, Q5AIZ3, Q9URL8
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: March 15, 2017
    Last modified: December 5, 2018
    This is version 135 of the entry and version 5 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    4. Candida albicans
      Candida albicans: entries and gene names
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again