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P22146

- GAS1_YEAST

UniProt

P22146 - GAS1_YEAST

Protein

1,3-beta-glucanosyltransferase GAS1

Gene

GAS1

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 136 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921Donor substrate; via carbonyl oxygenBy similarity
    Binding sitei160 – 1601Donor substrateBy similarity
    Active sitei161 – 1611Proton donor
    Binding sitei161 – 1611Acceptor substrateBy similarity
    Binding sitei202 – 2021Acceptor substrate; via carbonyl oxygenBy similarity
    Binding sitei207 – 2071Acceptor substrateBy similarity
    Active sitei262 – 2621Nucleophile
    Binding sitei294 – 2941Donor substrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. chromatin silencing Source: SGD
    3. filamentous growth Source: SGD
    4. fungal-type cell wall organization Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Cell wall biogenesis/degradation

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32971-MONOMER.

    Protein family/group databases

    CAZyiCBM43. Carbohydrate-Binding Module Family 43.
    GH72. Glycoside Hydrolase Family 72.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,3-beta-glucanosyltransferase GAS1 (EC:2.4.1.-)
    Alternative name(s):
    Glycolipid-anchored surface protein 1
    Glycoprotein GP115
    Gene namesi
    Name:GAS1
    Synonyms:GGP1
    Ordered Locus Names:YMR307W
    ORF Names:YM9952.09
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR307w.
    SGDiS000004924. GAS1.

    Subcellular locationi

    Cell membrane; Lipid-anchorGPI-anchor. Secretedcell wall
    Note: Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cellular bud scar Source: SGD
    3. ER to Golgi transport vesicle Source: SGD
    4. extracellular region Source: UniProtKB-KW
    5. fungal-type cell wall Source: SGD
    6. membrane raft Source: SGD
    7. nuclear periphery Source: SGD
    8. plasma membrane Source: SGD
    9. primary cell septum Source: SGD

    Keywords - Cellular componenti

    Cell membrane, Cell wall, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741C → S: Impairs the folding and stability of the protein. 1 Publication
    Mutagenesisi103 – 1031C → S: Partially impairs the folding and stability of the protein. 1 Publication
    Mutagenesisi161 – 1611E → Q: Loss of function. 1 Publication
    Mutagenesisi262 – 2621E → Q: Loss of function. 1 Publication
    Mutagenesisi265 – 2651C → S: Partially impairs the folding and stability of the protein. 1 Publication
    Mutagenesisi348 – 3481C → S: Impairs the folding and stability of the protein. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 5285061,3-beta-glucanosyltransferase GAS1PRO_0000010473Add
    BLAST
    Propeptidei529 – 55931Removed in mature formPRO_0000010474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi74 ↔ 103By similarity
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 348By similarity
    Disulfide bondi234 ↔ 265By similarity
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi370 ↔ 421By similarity
    Disulfide bondi372 ↔ 462By similarity
    Disulfide bondi379 ↔ 445By similarity
    Disulfide bondi398 ↔ 403By similarity
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi495 – 4951N-linked (GlcNAc...)Sequence Analysis
    Lipidationi528 – 5281GPI-anchor amidated asparagine1 Publication

    Post-translational modificationi

    Extensively N- and O-glycosylated.1 Publication
    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

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP22146.
    PaxDbiP22146.
    PeptideAtlasiP22146.

    2D gel databases

    COMPLUYEAST-2DPAGEP22146.

    Expressioni

    Gene expression databases

    GenevestigatoriP22146.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGP1P253761EBI-7327,EBI-2357
    GAP1P191451EBI-7327,EBI-7314
    PMP2P409751EBI-7327,EBI-2043041
    PMP3P872841EBI-7327,EBI-13555
    PMT7Q066441EBI-7327,EBI-13600
    SPF1P399861EBI-7327,EBI-3128

    Protein-protein interaction databases

    BioGridi35487. 498 interactions.
    DIPiDIP-4390N.
    IntActiP22146. 8 interactions.
    MINTiMINT-564340.
    STRINGi4932.YMR307W.

    Structurei

    3D structure databases

    ProteinModelPortaliP22146.
    SMRiP22146. Positions 23-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1279Donor substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi438 – 52588Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 72 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73259.
    GeneTreeiENSGT00390000011003.
    HOGENOMiHOG000164982.
    OMAiGGSKSDC.
    OrthoDBiEOG7K3TW7.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR004886. Glucanosyltransferase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012946. X8.
    [Graphical view]
    PfamiPF03198. Glyco_hydro_72. 1 hit.
    PF07983. X8. 1 hit.
    [Graphical view]
    SMARTiSM00768. X8. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P22146-1 [UniParc]FASTAAdd to Basket

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    MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA    50
    YQADTANETS GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH 100
    SECMKALNDA DIYVIADLAA PATSINRDDP TWTVDLFNSY KTVVDTFANY 150
    TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR DVRQYISDKN YRKIPVGYSS 200
    NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK TSGYADRTAE 250
    FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET 300
    NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA 350
    TGKYWSAATE LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE 400
    VDCSGISANG TAGKYGAYSF CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS 450
    ATLQTATTQA SCSSALKEIG SMGTNSASGS VDLGSGTESS TASSNASGSS 500
    SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV VFTSIISLSI 550
    AAGVGFALV 559
    Length:559
    Mass (Da):59,582
    Last modified:February 1, 1996 - v2
    Checksum:iD6E39568DCB4C5AE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2111T → A in CAA37512. (PubMed:1824714)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53424 Genomic DNA. Translation: CAA37512.1.
    X56399 Genomic DNA. Translation: CAA39809.1.
    Z49212 Genomic DNA. Translation: CAA89140.1.
    BK006946 Genomic DNA. Translation: DAA10208.1.
    PIRiS53977. RWBYS1.
    RefSeqiNP_014038.1. NM_001182818.1.

    Genome annotation databases

    EnsemblFungiiYMR307W; YMR307W; YMR307W.
    GeneIDi855355.
    KEGGisce:YMR307W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53424 Genomic DNA. Translation: CAA37512.1 .
    X56399 Genomic DNA. Translation: CAA39809.1 .
    Z49212 Genomic DNA. Translation: CAA89140.1 .
    BK006946 Genomic DNA. Translation: DAA10208.1 .
    PIRi S53977. RWBYS1.
    RefSeqi NP_014038.1. NM_001182818.1.

    3D structure databases

    ProteinModelPortali P22146.
    SMRi P22146. Positions 23-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35487. 498 interactions.
    DIPi DIP-4390N.
    IntActi P22146. 8 interactions.
    MINTi MINT-564340.
    STRINGi 4932.YMR307W.

    Protein family/group databases

    CAZyi CBM43. Carbohydrate-Binding Module Family 43.
    GH72. Glycoside Hydrolase Family 72.

    2D gel databases

    COMPLUYEAST-2DPAGE P22146.

    Proteomic databases

    MaxQBi P22146.
    PaxDbi P22146.
    PeptideAtlasi P22146.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR307W ; YMR307W ; YMR307W .
    GeneIDi 855355.
    KEGGi sce:YMR307W.

    Organism-specific databases

    CYGDi YMR307w.
    SGDi S000004924. GAS1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32971-MONOMER.

    Miscellaneous databases

    NextBioi 979115.

    Gene expression databases

    Genevestigatori P22146.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR004886. Glucanosyltransferase.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR012946. X8.
    [Graphical view ]
    Pfami PF03198. Glyco_hydro_72. 1 hit.
    PF07983. X8. 1 hit.
    [Graphical view ]
    SMARTi SM00768. X8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane."
      Nuoffer C., Jenoe P., Conzelmann A., Riezman H.
      Mol. Cell. Biol. 11:27-37(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-39; 237-240; 435-437 AND 527-528, SUBCELLULAR LOCATION, GPI-ANCHOR AT ASN-528.
    2. "Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region."
      Vai M., Gatti E., Lacana E., Popolo L., Alberghina L.
      J. Biol. Chem. 266:12242-12248(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DBY939.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "A major 125-kd membrane glycoprotein of Saccharomyces cerevisiae is attached to the lipid bilayer through an inositol-containing phospholipid."
      Conzelmann A., Riezman H., Desponds C., Bron C.
      EMBO J. 7:2233-2240(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, GPI-ANCHOR.
    6. "Immunochemical characterization of gp115, a yeast glycoprotein modulated by the cell cycle."
      Popolo L., Grandori R., Vai M., Lacana E., Alberghina L.
      Eur. J. Cell Biol. 47:173-180(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "The cell cycle modulated glycoprotein GP115 is one of the major yeast proteins containing glycosylphosphatidylinositol."
      Vai M., Popolo L., Grandori R., Lacana E., Alberghina L.
      Biochim. Biophys. Acta 1038:277-285(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR.
    8. "A constitutive role for GPI anchors in Saccharomyces cerevisiae: cell wall targeting."
      De Sampaio G., Bourdineaud J.-P., Lauquin G.J.-M.
      Mol. Microbiol. 34:247-256(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Glycosylphosphatidylinositol-anchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall."
      Mouyna I., Fontaine T., Vai M., Monod M., Fonzi W.A., Diaquin M., Popolo L., Hartland R.P., Latge J.-P.
      J. Biol. Chem. 275:14882-14889(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Characterization of recombinant forms of the yeast Gas1 protein and identification of residues essential for glucanosyltransferase activity and folding."
      Carotti C., Ragni E., Palomares O., Fontaine T., Tedeschi G., Rodriguez R., Latge J.-P., Vai M., Popolo L.
      Eur. J. Biochem. 271:3635-3645(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-74; CYS-103; GLU-161; GLU-262 AND CYS-265.
    11. "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.
    12. "Mass spectrometric quantitation of covalently bound cell wall proteins in Saccharomyces cerevisiae."
      Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.
      FEMS Yeast Res. 7:887-896(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: LEVEL OF PROTEIN EXPRESSION, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Disulfide bond structure and domain organization of yeast beta(1,3)-glucanosyltransferases involved in cell wall biogenesis."
      Popolo L., Ragni E., Carotti C., Palomares O., Aardema R., Back J.W., Dekker H.L., de Koning L.J., de Jong L., de Koster C.G.
      J. Biol. Chem. 283:18553-18565(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-348.
    14. "An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies."
      Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H., Montefiori D., Smith D.F., Doms R.W., Geng Y.
      J. Virol. 82:6447-6457(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiGAS1_YEAST
    AccessioniPrimary (citable) accession number: P22146
    Secondary accession number(s): D6W0D4, P23151
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 11000 wall-bound molecules/cell in log phase YPD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3