Q9P378 (GAS1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1,3-beta-glucanosyltransferase gas1
EC=2.4.1.-

Gene names

Name:	gas1
ORF Names:	SPAC19B12.02c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	542 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 By similarity.
Subcellular location	Secreted › cell wall. Membrane; Lipid-anchor › GPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP). Ref.3
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.
Sequence similarities	Belongs to the glycosyl hydrolase 72 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Membrane Secreted
Domain	Signal
Molecular function	Transferase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	barrier septum assembly Inferred from mutant phenotype. Source: BHF-UCL cell morphogenesis Inferred from mutant phenotype. Source: BHF-UCL cell wall (1->3)-beta-D-glucan metabolic process Inferred from mutant phenotype. Source: BHF-UCL cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW establishment or maintenance of cell polarity Inferred from mutant phenotype. Source: BHF-UCL fungal-type cell wall assembly Inferred from mutant phenotype. Source: BHF-UCL fungal-type cell wall polysaccharide metabolic process Inferred by curator. Source: GeneDB_Spombe
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell septum edging Inferred from direct assay. Source: BHF-UCL external side of plasma membrane Non-traceable author statement. Source: GeneDB_Spombe extracellular region Inferred from electronic annotation. Source: UniProtKB-KW primary cell septum Inferred from direct assay. Source: BHF-UCL site of polarized growth Inferred from direct assay. Source: BHF-UCL
Molecular function	1,3-beta-glucanosyltransferase activity Inferred from direct assay. Source: BHF-UCL cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 516	497	1,3-beta-glucanosyltransferase gas1		PRO_0000010491
	Propeptide	517 – 542	26	Removed in mature form Potential		PRO_0000377426
Regions
	Region	115 – 123	9	Donor substrate binding By similarity
	Compositional bias	434 – 516	83	Ser-rich
Sites
	Active site	157	1	Proton donor By similarity
	Active site	258	1	Nucleophile By similarity
	Binding site	88	1	Donor substrate; via carbonyl oxygen By similarity
	Binding site	156	1	Donor substrate By similarity
	Binding site	157	1	Acceptor substrate By similarity
	Binding site	198	1	Acceptor substrate; via carbonyl oxygen By similarity
	Binding site	203	1	Acceptor substrate By similarity
	Binding site	290	1	Donor substrate By similarity
Amino acid modifications
	Lipidation	516	1	GPI-anchor amidated serine Potential
	Glycosylation	35	1	N-linked (GlcNAc...) Potential
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	249	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Glycosylation	406	1	N-linked (GlcNAc...) Potential
	Glycosylation	484	1	N-linked (GlcNAc...) Potential
	Glycosylation	502	1	N-linked (GlcNAc...) Potential
	Glycosylation	509	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 99		By similarity
	Disulfide bond	230 ↔ 261		By similarity
	Disulfide bond	367 ↔ 419		By similarity
	Disulfide bond	376 ↔ 439		By similarity
	Disulfide bond	395 ↔ 400		By similarity
Experimental info
	Sequence conflict	268 – 278	11	TFSEIVALFSD → HSLSLLPRSET Ref.2
	Sequence conflict	285 – 293	9	SGGIAYQYF → VWWHCLPIW in BAA13864. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9P378 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1D243FDA5AD2EC3A	FASTA	542	58,116
	10 20 30 40 50 60 MKFSILSLAV AGLVGLAKAS VSPVHVDGRY FFYENGTRFF LKGIAYQPNV DDSDTEGTLF 70 80 90 100 110 120 VDPLSDGDAC SRDVPYFQEL SVNAIRVYAV NASLDHSACM QAFQDAGIYV LSDLAQPYEA 130 140 150 160 170 180 ISSSDPTWTV DLFSRYTEVV DSLAPYDNML GFIAGNEVIQ NNTNTNAAAF VKAAVRDVKS 190 200 210 220 230 240 YIKSSGYRQI PVGYSTNDEE VTRDPMAYYF DCGDDDDHVD FYGINIYEWC GDSDFVSSGY 250 260 270 280 290 300 QERTEEFSNM TVPMIFSEFG CIEVRPRTFS EIVALFSDNM TDVWSGGIAY QYFESENEYG 310 320 330 340 350 360 VVTVSGDSVS TLTDFPYLSS RYASVIPSAS YESTMSATLT ATMSCQATNS AWMAATSLPP 370 380 390 400 410 420 TPSEAVCECM DSTRSCVIND DVSSDDYSDL FSYVCNEISC DGITANGTYP GQYGSYSYCD 430 440 450 460 470 480 AKQQLDYVLD AYYSAKGDCD FSGSATLVSA SSATGTCASY LSAAGSSATN AISLTADSNA 490 500 510 520 530 540 VSRNSSASTM STSYTSGSGS SNSSGSSSNS SSKSSSGASS YNLNMVITFL SVVIGGTAVL FI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-542. Strain: PR745.
[3]	"Mass spectrometric identification of covalently bound cell wall proteins from the fission yeast Schizosaccharomyces pombe." de Groot P.W.J., Yin Q.Y., Weig M., Sosinska G.J., Klis F.M., de Koster C.G. Yeast 24:267-278(2007) [PubMed: 17230583] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PROBABLE GPI-ANCHOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAC00550.1. D89203 mRNA. Translation: BAA13864.1.
PIR	T43004.
RefSeq	NP_594765.1. NM_001020192.1.
3D structure databases
ProteinModelPortal	Q9P378.
ModBase	Search...
Protein family/group databases
CAZy	CBM43. Carbohydrate-Binding Module Family 43. GH72. Glycoside Hydrolase Family 72.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC19B12.02c.1; SPAC19B12.02c.1:pep; SPAC19B12.02c.
GeneID	2542584.
GenomeReviews	Gene locus gas1 in contig CU329670_GR.
KEGG	spo:SPAC19B12.02c.
NMPDR	fig|4896.1.peg.4735.
Organism-specific databases
GeneDB_Spombe	SPAC19B12.02c.
Phylogenomic databases
eggNOG	fuNOG06278.
GeneTree	EFGT00050000000135.
HOGENOM	HBG737647.
OMA	YGCNEVT.
OrthoDB	EOG4617C9.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002840-MONOMER.
Gene expression databases
ArrayExpress	Q9P378.
Family and domain databases
InterPro	IPR004886. GAS1. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR012946. X8. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
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...

Entry information

Entry name

GAS1_SCHPO

Accession

Primary (citable) accession number: Q9P378
Secondary accession number(s): P78853

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program