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Q06135 (GAS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1,3-beta-glucanosyltransferase GAS2
EC=2.4.1.-
Alternative name(s):
Glycolipid-anchored surface protein 2
Gene names
Name:GAS2
Ordered Locus Names:YLR343W
ORF Names:L8300.5
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 spore wall assembly. Ref.3 Ref.4

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor By similarity.

Developmental stage

Expressed exclusively during sporulation (at protein level). Ref.3

Post-translational modification

N-glycosylated.

Sequence similarities

Belongs to the glycosyl hydrolase 72 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 5315071,3-beta-glucanosyltransferase GAS2
PRO_0000010475
Propeptide532 – 55524Removed in mature form Potential
PRO_0000010476

Regions

Region134 – 1429Donor substrate binding

Sites

Active site1761Proton donor
Active site2751Nucleophile
Binding site1071Donor substrate; via carbonyl oxygen
Binding site1751Donor substrate
Binding site1761Acceptor substrate
Binding site2171Acceptor substrate; via carbonyl oxygen
Binding site2221Acceptor substrate
Binding site3071Donor substrate

Amino acid modifications

Lipidation5311GPI-anchor amidated aspartate Potential
Glycosylation4981N-linked (GlcNAc...) Potential
Disulfide bond89 ↔ 118 Ref.5
Disulfide bond231 ↔ 367 Ref.5
Disulfide bond247 ↔ 278 Ref.5
Disulfide bond390 ↔ 442 Ref.5
Disulfide bond392 ↔ 489 Ref.5
Disulfide bond399 ↔ 466 Ref.5
Disulfide bond419 ↔ 424 Ref.5

Experimental info

Mutagenesis621Q → A: Slightly reduces catalytic activity. Ref.6
Mutagenesis1071Y → F or Q: Slightly reduces catalytic activity. Ref.6
Mutagenesis1321D → N: Slightly reduces catalytic activity. Ref.6
Mutagenesis1751N → A: Abolishes catalytic activity. Ref.6
Mutagenesis1761E → Q: Abolishes catalytic activity. Ref.6
Mutagenesis2441Y → F or Q: Moderately reduces hydrolysis, and causes a 10-fold reduction in transglycosylation activity. Ref.6
Mutagenesis2751E → Q: Abolishes catalytic activity. Ref.6
Mutagenesis3071Y → Q: Moderately reduces catalytic activity. Ref.6
Mutagenesis4041F → A: Slightly reduces catalytic activity. Ref.6
Mutagenesis4741Y → A: No effect. Ref.6

Secondary structure

1 ....................................................... 555
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06135 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 15395E4F137DAC7F

FASTA55562,362
        10         20         30         40         50         60 
MNKKQNFYAA IIVAIFLCLQ LSHGSSGVSF EKTPAIKIVG NKFFDSESGE QFFIKGIAYQ 

        70         80         90        100        110        120 
LQRSEEELSN ANGAFETSYI DALADPKICL RDIPFLKMLG VNTLRVYAID PTKSHDICME 

       130        140        150        160        170        180 
ALSAEGMYVL LDLSEPDISI NRENPSWDVH IFERYKSVID AMSSFPNLLG YFAGNEVTND 

       190        200        210        220        230        240 
HTNTFASPFV KAAIRDAKEY ISHSNHRKIP VGYSTNDDAM TRDNLARYFV CGDVKADFYG 

       250        260        270        280        290        300 
INMYEWCGYS TYGTSGYRER TKEFEGYPIP VFFSEFGCNL VRPRPFTEVS ALYGNKMSSV 

       310        320        330        340        350        360 
WSGGLAYMYF EEENEYGVVK INDNDGVDIL PDFKNLKKEF AKADPKGITE EEYLTAKEPT 

       370        380        390        400        410        420 
EVESVECPHI AVGVWEANEK LPETPDRSKC ACLDEILPCE IVPFGAESGK YEEYFSYLCS 

       430        440        450        460        470        480 
KVDCSDILAN GKTGEYGEFS DCSVEQKLSL QLSKLYCKIG ANDRHCPLND KNVYFNLESL 

       490        500        510        520        530        540 
QPLTSESICK NVFDSIRNIT YNHGDYSKSN PSRSKESLNV KYPSSEEREN DGTIAFKTSG 

       550 
FVILLISMIA AGILL

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"GAS2 and GAS4, a pair of developmentally regulated genes required for spore wall assembly in Saccharomyces cerevisiae."
Ragni E., Coluccio A., Rolli E., Rodriguez-Pena J.M., Colasante G., Arroyo J., Neiman A.M., Popolo L.
Eukaryot. Cell 6:302-316(2007) [PubMed: 17189486] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[4]"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: 17397106] [Abstract]
Cited for: FUNCTION.
[5]"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: 18468997] [Abstract]
Cited for: DISULFIDE BONDS.
[6]"Molecular mechanisms of yeast cell wall glucan remodeling."
Hurtado-Guerrero R., Schuettelkopf A.W., Mouyna I., Ibrahim A.F.M., Shepherd S., Fontaine T., Latge J.-P., van Aalten D.M.F.
J. Biol. Chem. 284:8461-8469(2009) [PubMed: 19097997] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF WILD-TYPE AND MUTANT GLN-176 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF GLN-62; TYR-107; ASP-132; ASN-175; GLU-176; TYR-244; GLU-275; TYR-307; PHE-404 AND TYR-474.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U19028 Genomic DNA. Translation: AAB67255.1.
BK006945 Genomic DNA. Translation: DAA09648.1.
PIRS51346.
RefSeqNP_013447.1. NM_001182232.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W61X-ray1.62A1-555[»]
2W62X-ray1.85A1-555[»]
2W63X-ray1.90A1-555[»]
ProteinModelPortalQ06135.
SMRQ06135. Positions 27-506.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4669N.
MINTMINT-526782.
STRINGQ06135.

Protein family/group databases

CAZyCBM43. Carbohydrate-Binding Module Family 43.
GH72. Glycoside Hydrolase Family 72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR343W; YLR343W; YLR343W.
GeneID851056.
KEGGsce:YLR343W.
NMPDRfig|4932.3.peg.4468.

Organism-specific databases

CYGDYLR343w.
SGDS000004335. GAS2.

Phylogenomic databases

eggNOGfuNOG04022.
GeneTreeEFGT00050000000135.
HOGENOMHBG737647.
OMAEWCGYST.
OrthoDBEOG45MRDT.

Gene expression databases

ArrayExpressQ06135.
GenevestigatorQ06135.
GermOnlineYLR343W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004886. GAS1.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF03198. Glyco_hydro_72. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Other

NextBio967676.

Entry information

Entry nameGAS2_YEAST
AccessionPrimary (citable) accession number: Q06135
Secondary accession number(s): D6VYY2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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