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Protein

1,3-beta-glucanosyltransferase GAS1

Gene

GAS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • chromatin silencing Source: SGD
  • filamentous growth Source: SGD
  • fungal-type cell wall organization Source: SGD
Complete GO annotation...

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 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR307w.
EuPathDBiFungiDB:YMR307W.
SGDiS000004924. GAS1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • cellular bud scar Source: SGD
  • ER to Golgi transport vesicle Source: SGD
  • extracellular region Source: UniProtKB-KW
  • fungal-type cell wall Source: SGD
  • membrane raft Source: SGD
  • nuclear periphery Source: SGD
  • plasma membrane Source: SGD
  • primary cell septum Source: SGD
Complete GO annotation...

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.

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. 502 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.
InParanoidiP22146.
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

« Hide

        10         20         30         40         50
MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA
60 70 80 90 100
YQADTANETS GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH
110 120 130 140 150
SECMKALNDA DIYVIADLAA PATSINRDDP TWTVDLFNSY KTVVDTFANY
160 170 180 190 200
TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR DVRQYISDKN YRKIPVGYSS
210 220 230 240 250
NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK TSGYADRTAE
260 270 280 290 300
FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET
310 320 330 340 350
NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA
360 370 380 390 400
TGKYWSAATE LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE
410 420 430 440 450
VDCSGISANG TAGKYGAYSF CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS
460 470 480 490 500
ATLQTATTQA SCSSALKEIG SMGTNSASGS VDLGSGTESS TASSNASGSS
510 520 530 540 550
SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV VFTSIISLSI

AAGVGFALV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi35487. 502 interactions.
DIPiDIP-4390N.
IntActiP22146. 8 interactions.
MINTiMINT-564340.
STRINGi4932.YMR307W.

Protein family/group databases

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

2D gel databases

COMPLUYEAST-2DPAGEP22146.

Proteomic databases

MaxQBiP22146.
PaxDbiP22146.
PeptideAtlasiP22146.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYMR307w.
EuPathDBiFungiDB:YMR307W.
SGDiS000004924. GAS1.

Phylogenomic databases

eggNOGiNOG73259.
GeneTreeiENSGT00390000011003.
HOGENOMiHOG000164982.
InParanoidiP22146.
OMAiGGSKSDC.
OrthoDBiEOG7K3TW7.

Enzyme and pathway databases

BioCyciYEAST:G3O-32971-MONOMER.

Miscellaneous databases

NextBioi979115.
PROiP22146.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.