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Q08193 (GAS5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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 GAS5

EC=2.4.1.-
Alternative name(s):
Glycolipid-anchored surface protein 5
Gene names
Name:GAS5
Ordered Locus Names:YOL030W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length484 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 cell wall biosynthesis and morphogenesis. Ref.6

Subcellular location

Secretedcell wall. Membrane; Lipid-anchorGPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP). Ref.5

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 72 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 4624431,3-beta-glucanosyltransferase GAS5
PRO_0000010481
Propeptide463 – 48422Removed in mature form Potential
PRO_0000010482

Regions

Region116 – 1249Donor substrate binding By similarity
Compositional bias395 – 4039Asp/Glu-rich (highly acidic)
Compositional bias405 – 46056Ser-rich
Compositional bias405 – 42723Poly-Ser
Compositional bias432 – 4398Poly-Ser

Sites

Active site1601Proton donor By similarity
Active site2621Nucleophile By similarity
Binding site891Donor substrate; via carbonyl oxygen By similarity
Binding site1591Donor substrate By similarity
Binding site1601Acceptor substrate By similarity
Binding site2011Acceptor substrate; via carbonyl oxygen By similarity
Binding site2061Acceptor substrate By similarity
Binding site2951Donor substrate By similarity

Amino acid modifications

Lipidation4621GPI-anchor amidated glycine Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q08193 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: E65B9F4689B8B34C

FASTA48451,870
        10         20         30         40         50         60 
MLLRSLTSAF VLSAGLAQAA SSSNSSTPSI EIKGNAFFNS ESGERFYIRG VDYQPGGSSN 

        70         80         90        100        110        120 
LTDPLADASV CDRDVPVLKD LGINTVRVYT VDNSQDHSHC MKLLQENGIY LILDVNTPTS 

       130        140        150        160        170        180 
AISRYDPACS YNADYLQNVF ATIDTFADYD NVLGFFAGNE VINSVNTTNT ATYVKAVVRD 

       190        200        210        220        230        240 
MKKYIKARKY RQIPVGYSAA DIVANRQLAA EYFNCGDEAD ARIDMFGVND YSWCGESSFV 

       250        260        270        280        290        300 
VSGYSTKMKL YQDYSVPVFL SEFGCNQVKS SRPFTEIEAI YSTQMSSVFS GGLVYEYSNE 

       310        320        330        340        350        360 
TNNYGLVQID GDKVTKLTDF ENLKNEYSKV SNPEGNGGYS TSNNYSTCPD YEKGVWEANN 

       370        380        390        400        410        420 
TLPAMPSAAS AYFTSGAGSP MGTGIATQQS CDAKDDDDEE DDDTSSSSSS SSSSSSSASS 

       430        440        450        460        470        480 
SSESSSSTSK ASSSSPSASE TSLLKSAASA TSSSQSSSKS KGAAGIIEIP LIFRALAELY 


NLVL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74772 Genomic DNA. Translation: CAA99030.1.
AY693093 Genomic DNA. Translation: AAT93112.1.
BK006948 Genomic DNA. Translation: DAA10751.1.
PIRS66713.
RefSeqNP_014612.1. NM_001183284.1.

3D structure databases

ProteinModelPortalQ08193.
SMRQ08193. Positions 23-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34370. 48 interactions.
DIPDIP-4240N.
IntActQ08193. 2 interactions.
MINTMINT-545137.
STRING4932.YOL030W.

Protein family/group databases

CAZyGH72. Glycoside Hydrolase Family 72.

Proteomic databases

MaxQBQ08193.
PaxDbQ08193.
PeptideAtlasQ08193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL030W; YOL030W; YOL030W.
GeneID854127.
KEGGsce:YOL030W.

Organism-specific databases

CYGDYOL030w.
SGDS000005390. GAS5.

Phylogenomic databases

eggNOGNOG73259.
GeneTreeENSGT00390000011003.
HOGENOMHOG000164982.
OMATSGWDQK.
OrthoDBEOG7K3TW7.

Enzyme and pathway databases

BioCycYEAST:G3O-33446-MONOMER.

Gene expression databases

GenevestigatorQ08193.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR004886. Glucanosyltransferase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF03198. Glyco_hydro_72. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

NextBio975840.

Entry information

Entry nameGAS5_YEAST
AccessionPrimary (citable) accession number: Q08193
Secondary accession number(s): D6W235
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries