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Q08193

- GAS5_YEAST

UniProt

Q08193 - GAS5_YEAST

Protein

1,3-beta-glucanosyltransferase GAS5

Gene

GAS5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891Donor substrate; via carbonyl oxygenBy similarity
    Binding sitei159 – 1591Donor substrateBy similarity
    Active sitei160 – 1601Proton donorBy similarity
    Binding sitei160 – 1601Acceptor substrateBy similarity
    Binding sitei201 – 2011Acceptor substrate; via carbonyl oxygenBy similarity
    Binding sitei206 – 2061Acceptor substrateBy similarity
    Active sitei262 – 2621NucleophileBy similarity
    Binding sitei295 – 2951Donor substrateBy similarity

    GO - Molecular functioni

    1. 1,3-beta-glucanosyltransferase activity Source: SGD

    GO - Biological processi

    1. (1->3)-beta-D-glucan metabolic process Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33446-MONOMER.

    Protein family/group databases

    CAZyiGH72. Glycoside Hydrolase Family 72.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,3-beta-glucanosyltransferase GAS5 (EC:2.4.1.-)
    Alternative name(s):
    Glycolipid-anchored surface protein 5
    Gene namesi
    Name:GAS5
    Ordered Locus Names:YOL030W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL030w.
    SGDiS000005390. GAS5.

    Subcellular locationi

    Secretedcell wall 1 Publication. Membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication
    Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP).

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular region Source: UniProtKB-KW
    3. fungal-type cell wall Source: SGD

    Keywords - Cellular componenti

    Cell wall, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 4624431,3-beta-glucanosyltransferase GAS5PRO_0000010481Add
    BLAST
    Propeptidei463 – 48422Removed in mature formSequence AnalysisPRO_0000010482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Lipidationi462 – 4621GPI-anchor amidated glycineSequence Analysis

    Post-translational modificationi

    The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ08193.
    PaxDbiQ08193.
    PeptideAtlasiQ08193.

    Expressioni

    Gene expression databases

    GenevestigatoriQ08193.

    Interactioni

    Protein-protein interaction databases

    BioGridi34370. 48 interactions.
    DIPiDIP-4240N.
    IntActiQ08193. 2 interactions.
    MINTiMINT-545137.
    STRINGi4932.YOL030W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08193.
    SMRiQ08193. Positions 23-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 1249Donor substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi395 – 4039Asp/Glu-rich (highly acidic)
    Compositional biasi405 – 46056Ser-richAdd
    BLAST
    Compositional biasi405 – 42723Poly-SerAdd
    BLAST
    Compositional biasi432 – 4398Poly-Ser

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 72 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73259.
    GeneTreeiENSGT00390000011003.
    HOGENOMiHOG000164982.
    OMAiTSGWDQK.
    OrthoDBiEOG7K3TW7.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR004886. Glucanosyltransferase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF03198. Glyco_hydro_72. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q08193-1 [UniParc]FASTAAdd to Basket

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    MLLRSLTSAF VLSAGLAQAA SSSNSSTPSI EIKGNAFFNS ESGERFYIRG    50
    VDYQPGGSSN LTDPLADASV CDRDVPVLKD LGINTVRVYT VDNSQDHSHC 100
    MKLLQENGIY LILDVNTPTS AISRYDPACS YNADYLQNVF ATIDTFADYD 150
    NVLGFFAGNE VINSVNTTNT ATYVKAVVRD MKKYIKARKY RQIPVGYSAA 200
    DIVANRQLAA EYFNCGDEAD ARIDMFGVND YSWCGESSFV VSGYSTKMKL 250
    YQDYSVPVFL SEFGCNQVKS SRPFTEIEAI YSTQMSSVFS GGLVYEYSNE 300
    TNNYGLVQID GDKVTKLTDF ENLKNEYSKV SNPEGNGGYS TSNNYSTCPD 350
    YEKGVWEANN TLPAMPSAAS AYFTSGAGSP MGTGIATQQS CDAKDDDDEE 400
    DDDTSSSSSS SSSSSSSASS SSESSSSTSK ASSSSPSASE TSLLKSAASA 450
    TSSSQSSSKS KGAAGIIEIP LIFRALAELY NLVL 484
    Length:484
    Mass (Da):51,870
    Last modified:November 1, 1997 - v1
    Checksum:iE65B9F4689B8B34C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74772 Genomic DNA. Translation: CAA99030.1.
    AY693093 Genomic DNA. Translation: AAT93112.1.
    BK006948 Genomic DNA. Translation: DAA10751.1.
    PIRiS66713.
    RefSeqiNP_014612.1. NM_001183284.1.

    Genome annotation databases

    EnsemblFungiiYOL030W; YOL030W; YOL030W.
    GeneIDi854127.
    KEGGisce:YOL030W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74772 Genomic DNA. Translation: CAA99030.1 .
    AY693093 Genomic DNA. Translation: AAT93112.1 .
    BK006948 Genomic DNA. Translation: DAA10751.1 .
    PIRi S66713.
    RefSeqi NP_014612.1. NM_001183284.1.

    3D structure databases

    ProteinModelPortali Q08193.
    SMRi Q08193. Positions 23-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34370. 48 interactions.
    DIPi DIP-4240N.
    IntActi Q08193. 2 interactions.
    MINTi MINT-545137.
    STRINGi 4932.YOL030W.

    Protein family/group databases

    CAZyi GH72. Glycoside Hydrolase Family 72.

    Proteomic databases

    MaxQBi Q08193.
    PaxDbi Q08193.
    PeptideAtlasi Q08193.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL030W ; YOL030W ; YOL030W .
    GeneIDi 854127.
    KEGGi sce:YOL030W.

    Organism-specific databases

    CYGDi YOL030w.
    SGDi S000005390. GAS5.

    Phylogenomic databases

    eggNOGi NOG73259.
    GeneTreei ENSGT00390000011003.
    HOGENOMi HOG000164982.
    OMAi TSGWDQK.
    OrthoDBi EOG7K3TW7.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33446-MONOMER.

    Miscellaneous databases

    NextBioi 975840.

    Gene expression databases

    Genevestigatori Q08193.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR004886. Glucanosyltransferase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF03198. Glyco_hydro_72. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages."
      Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M., de Koster C.G.
      J. Biol. Chem. 280:20894-20901(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GPI-ANCHOR.
    6. "The Gas family of proteins of Saccharomyces cerevisiae: characterization and evolutionary analysis."
      Ragni E., Fontaine T., Gissi C., Latge J.-P., Popolo L.
      Yeast 24:297-308(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiGAS5_YEAST
    AccessioniPrimary (citable) accession number: Q08193
    Secondary accession number(s): D6W235
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 11700 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3