P22146 (GAS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,3-beta-glucanosyltransferase GAS1
EC=2.4.1.-

Alternative name(s):
Glycolipid-anchored surface protein 1
Glycoprotein GP115

Gene names

Name:	GAS1
Synonyms:	GGP1
Ordered Locus Names:	YMR307W
ORF Names:	YM9952.09

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.9 Ref.10
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Secreted › cell 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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.14
Post-translational modification	Extensively N- and O-glycosylated. Ref.14 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 11000 wall-bound molecules/cell in log phase YPD medium. Ref.12
Sequence similarities	Belongs to the glycosyl hydrolase 72 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell membrane Cell wall Membrane Secreted
Domain	Signal
Molecular function	Transferase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro chromatin silencing Inferred from mutant phenotype PubMed 19541632. Source: SGD filamentous growth Inferred from mutant phenotype PubMed 15645503. Source: SGD fungal-type cell wall organization Inferred from mutant phenotype PubMed 9515908. Source: SGD
Cellular_component	ER to Golgi transport vesicle Inferred from direct assay PubMed 18462190. Source: SGD anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cellular bud scar Inferred from direct assay PubMed 19793924. Source: SGD extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD membrane raft Inferred from direct assay PubMed 10716729. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nuclear periphery Inferred from direct assay PubMed 19541632. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836Ref.1PubMed 19793924. Source: SGD primary cell septum Inferred from direct assay PubMed 19793924. Source: SGD
Molecular_function	1,3-beta-glucanosyltransferase activity Inferred from direct assay Ref.9Ref.10PubMed 17397106. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGP1	P25376	1	EBI-7327,EBI-2357
GAP1	P19145	1	EBI-7327,EBI-7314
PMP2	P40975	1	EBI-7327,EBI-2043041
PMP3	P87284	1	EBI-7327,EBI-13555
PMT7	Q06644	1	EBI-7327,EBI-13600
SPF1	P39986	1	EBI-7327,EBI-3128

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.1
	Chain	23 – 528	506	1,3-beta-glucanosyltransferase GAS1		PRO_0000010473
	Propeptide	529 – 559	31	Removed in mature form		PRO_0000010474
Regions
	Region	119 – 127	9	Donor substrate binding By similarity
	Compositional bias	438 – 525	88	Ser-rich
Sites
	Active site	161	1	Proton donor
	Active site	262	1	Nucleophile
	Binding site	92	1	Donor substrate; via carbonyl oxygen By similarity
	Binding site	160	1	Donor substrate By similarity
	Binding site	161	1	Acceptor substrate By similarity
	Binding site	202	1	Acceptor substrate; via carbonyl oxygen By similarity
	Binding site	207	1	Acceptor substrate By similarity
	Binding site	294	1	Donor substrate By similarity
Amino acid modifications
	Lipidation	528	1	GPI-anchor amidated asparagine Ref.1 Ref.5 Ref.7 Ref.11
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	149	1	N-linked (GlcNAc...) Potential
	Glycosylation	165	1	N-linked (GlcNAc...) Potential
	Glycosylation	253	1	N-linked (GlcNAc...) Potential
	Glycosylation	283	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Glycosylation	495	1	N-linked (GlcNAc...) Potential
	Disulfide bond	74 ↔ 103		By similarity
	Disulfide bond	216 ↔ 348		By similarity
	Disulfide bond	234 ↔ 265		By similarity
	Disulfide bond	370 ↔ 421		By similarity
	Disulfide bond	372 ↔ 462		By similarity
	Disulfide bond	379 ↔ 445		By similarity
	Disulfide bond	398 ↔ 403		By similarity
Experimental info
	Mutagenesis	74	1	C → S: Impairs the folding and stability of the protein. Ref.10
	Mutagenesis	103	1	C → S: Partially impairs the folding and stability of the protein. Ref.10
	Mutagenesis	161	1	E → Q: Loss of function. Ref.10
	Mutagenesis	262	1	E → Q: Loss of function. Ref.10
	Mutagenesis	265	1	C → S: Partially impairs the folding and stability of the protein. Ref.10
	Mutagenesis	348	1	C → S: Impairs the folding and stability of the protein. Ref.13
	Sequence conflict	211	1	T → A in CAA37512. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P22146 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: D6E39568DCB4C5AE	FASTA	559	59,582
	10 20 30 40 50 60 MLFKSLSKLA TAAAFFAGVA TADDVPAIEV VGNKFFYSNN GSQFYIRGVA YQADTANETS 70 80 90 100 110 120 GSTVNDPLAN YESCSRDIPY LKKLNTNVIR VYAINTTLDH SECMKALNDA DIYVIADLAA 130 140 150 160 170 180 PATSINRDDP TWTVDLFNSY KTVVDTFANY TNVLGFFAGN EVTNNYTNTD ASAFVKAAIR 190 200 210 220 230 240 DVRQYISDKN YRKIPVGYSS NDDEDTRVKM TDYFACGDDD VKADFYGINM YEWCGKSDFK 250 260 270 280 290 300 TSGYADRTAE FKNLSIPVFF SEYGCNEVTP RLFTEVEALY GSNMTDVWSG GIVYMYFEET 310 320 330 340 350 360 NKYGLVSIDG NDVKTLDDFN NYSSEINKIS PTSANTKSYS ATTSDVACPA TGKYWSAATE 370 380 390 400 410 420 LPPTPNGGLC SCMNAANSCV VSDDVDSDDY ETLFNWICNE VDCSGISANG TAGKYGAYSF 430 440 450 460 470 480 CTPKEQLSFV MNLYYEKSGG SKSDCSFSGS ATLQTATTQA SCSSALKEIG SMGTNSASGS 490 500 510 520 530 540 VDLGSGTESS TASSNASGSS SKSNSGSSGS SSSSSSSSAS SSSSSKKNAA TNVKANLAQV 550 VFTSIISLSI AAGVGFALV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. , Skelton J., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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, PROBABLE 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, 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53424 Genomic DNA. Translation: CAA37512.1. X56399 Genomic DNA. Translation: CAA39809.1. Z49212 Genomic DNA. Translation: CAA89140.1. BK006946 Genomic DNA. Translation: DAA10208.1.
PIR	RWBYS1. S53977.
RefSeq	NP_014038.1. NM_001182818.1.
3D structure databases
ProteinModelPortal	P22146.
SMR	P22146. Positions 23-475.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4390N.
IntAct	P22146. 6 interactions.
MINT	MINT-564340.
STRING	4932.YMR307W.
Protein family/group databases
CAZy	CBM43. Carbohydrate-Binding Module Family 43. GH72. Glycoside Hydrolase Family 72.
2D gel databases
COMPLUYEAST-2DPAGE	P22146.
Proteomic databases
PaxDb	P22146.
PeptideAtlas	P22146.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR307W; YMR307W; YMR307W.
GeneID	855355.
KEGG	sce:YMR307W.
Organism-specific databases
CYGD	YMR307w.
SGD	S000004924. GAS1.
Phylogenomic databases
eggNOG	NOG73259.
GeneTree	ENSGT00390000011003.
HOGENOM	HOG000164982.
OMA	YGCNEVT.
OrthoDB	EOG4617C9.
Gene expression databases
Genevestigator	P22146.
GermOnline	YMR307W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR004886. Glucanosyltransferase. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. IPR012946. X8. [Graphical view]
Pfam	PF03198. Glyco_hydro_72. 1 hit. PF07983. X8. 1 hit. [Graphical view]
SMART	SM00768. X8. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	979115.

Entry information

Entry name

GAS1_YEAST

Accession

Primary (citable) accession number: P22146
Secondary accession number(s): D6W0D4, P23151

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program