U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    GAS4 1,3-beta-glucanosyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853988, updated on 2-Nov-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    GAS4
    Official Full Name
    1,3-beta-glucanosyltransferase
    Primary source
    SGD:S000005492
    Locus tag
    YOL132W
    See related
    AllianceGenome:SGD:S000005492; FungiDB:YOL132W; VEuPathDB:YOL132W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables 1,3-beta-glucanosyltransferase activity. Involved in ascospore wall assembly. Located in fungal-type cell wall. [provided by Alliance of Genome Resources, Nov 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See GAS4 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (71300..72715)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene mediator complex subunit MED7 Neighboring gene SCF ubiquitin ligase complex subunit HRT1 Neighboring gene uncharacterized protein Neighboring gene Mg(2+) transporter ALR1

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. GAS2 and GAS4, a pair of developmentally regulated genes required for spore wall assembly in Saccharomyces cerevisiae. Ragni E, et al. Eukaryot Cell, 2007 Feb. PMID 17189486, Free PMC Article
    2. Expression, stability, and replacement of glucan-remodeling enzymes during developmental transitions in Saccharomyces cerevisiae. Rolli E, et al. Mol Biol Cell, 2011 May. PMID 21389112, Free PMC Article
    3. Identification of the catalytic residues of the first family of beta(1-3)glucanosyltransferases identified in fungi. Mouyna I, et al. Biochem J, 2000 May 1. PMID 10769178, Free PMC Article
    4. Catalytic properties of the Gas family β-(1,3)-glucanosyltransferases active in fungal cell-wall biogenesis as determined by a novel fluorescent assay. Mazáň M, et al. Biochem J, 2011 Sep 1. PMID 21651500
    5. The Gas family of proteins of Saccharomyces cerevisiae: characterization and evolutionary analysis. Ragni E, et al. Yeast, 2007 Apr. PMID 17397106

    See all (26) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables 1,3-beta-glucanosyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 1,3-beta-glucanosyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables 1,3-beta-glucanosyltransferase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in ascospore wall assembly IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in ascospore wall assembly IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cell wall organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in fungal-type cell wall organization IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    is_active_in fungal-type cell wall IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in fungal-type cell wall IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in fungal-type vacuole HDA PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in side of membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    1,3-beta-glucanosyltransferase
    NP_014509.1
    • 1,3-beta-glucanosyltransferase; involved with Gas2p in spore wall assembly; has similarity to Gas1p; localizes to the cell wall

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001147.6 Reference assembly

      Range
      71300..72715
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183386.1 → NP_014509.1  TPA: 1,3-beta-glucanosyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014509.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W1T6, Q08271
      UniProtKB/TrEMBL
      A6ZN79, B3LIT4, B5VRC7, C7GV08, C8ZHI4, G2WMA5, N1P3A1
      Conserved Domains (1) summary
      pfam03198
      Location:15 → 335
      Glyco_hydro_72; Glucanosyltransferase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q08271.1

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools