1,3-beta-glucan synthase component GSC2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40989 (FKS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1,3-beta-glucan synthase component GSC2
EC=2.4.1.34

Alternative name(s):
1,3-beta-D-glucan-UDP glucosyltransferase
FK506 sensitivity protein 2
Glucan synthase of cerevisiae protein 2

Gene names

Name:	GSC2
Synonyms:	FKS2, GLS2
Ordered Locus Names:	YGR032W

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1895 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Required for spore wall assembly. Negative regulation of activity by SMK1 is important for spore wall deposition. Activity is positively regulated by RHO1. Ref.2 Ref.12
Catalytic activity	UDP-glucose + ((1->3)-beta-D-glucosyl)(n) = UDP + ((1->3)-beta-D-glucosyl)(n+1). Ref.10 Ref.12
Subunit structure	Component of the 1,3-beta-glucan synthase (GS), composed of two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit RHO1. Interacts with SMK1. Ref.10
Subcellular location	Membrane; Multi-pass membrane protein Ref.2.
Induction	Under starvation and during sporulation. Also by pheromones and calcium in a calcineurin-dependent manner. Ref.2
Miscellaneous	Deletion leads to caspofungin resistance.
Sequence similarities	Belongs to the glycosyltransferase 48 family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation Sporulation
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	(1->3)-beta-D-glucan biosynthetic process Inferred from direct assay Ref.2. Source: SGD ascospore wall assembly Inferred from mutant phenotype Ref.10. Source: SGD regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	1,3-beta-D-glucan synthase complex Inferred from direct assay PubMed 7983071. Source: SGD actin cap Traceable author statement PubMed 10652251. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD prospore membrane Inferred from direct assay PubMed 15755916. Source: SGD
Molecular_function	1,3-beta-D-glucan synthase activity Inferred from direct assay Ref.2 Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1895

1895

1,3-beta-glucan synthase component GSC2

PRO_0000121726

Regions

Topological domain

1 – 473

473

Extracellular Potential

Transmembrane

474 – 494

Helical; Potential

Topological domain

495 – 511

Cytoplasmic Potential

Transmembrane

512 – 532

Helical; Potential

Topological domain

533 – 550

Extracellular Potential

Transmembrane

551 – 571

Helical; Potential

Topological domain

572 – 582

Cytoplasmic Potential

Transmembrane

583 – 603

Helical; Potential

Topological domain

604 – 1579

976

Extracellular Potential

Transmembrane

1580 – 1600

Helical; Potential

Topological domain

1601 – 1620

Cytoplasmic Potential

Transmembrane

1621 – 1641

Helical; Potential

Topological domain

1642 – 1758

117

Extracellular Potential

Transmembrane

1759 – 1779

Helical; Potential

Topological domain

1780 – 1821

Cytoplasmic Potential

Transmembrane

1822 – 1842

Helical; Potential

Topological domain

1843 – 1895

Extracellular Potential

Amino acid modifications

Modified residue

974

Phosphoserine Ref.13

Cross-link

806

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Natural variations

Natural variant

1059

N → S in strain: SK1. Ref.3

Natural variant

1853 – 1854

TG → KD in strain: SK1.

Experimental info

Sequence conflict

137

A → T in BAA07707. Ref.1

Sequence conflict

261

K → E in BAA07707. Ref.1

Sequence conflict

275

K → R in BAA07707. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P40989 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 9DDE4D8C19BC24DA
Show »

FASTA

1,895

216,990

        10         20         30         40         50         60 
MSYNDPNLNG QYYSNGDGTG DGNYPTYQVT QDQSAYDEYG QPIYTQNQLD DGYYDPNEQY 

        70         80         90        100        110        120 
VDGTQFPQGQ DPSQDQGPYN NDASYYNQPP NMMNPSSQDG ENFSDFSSYG PPSGTYPNDQ 

       130        140        150        160        170        180 
YTPSQMSYPD QDGSSGASTP YGNGVVNGNG QYYDPNAIEM ALPNDPYPAW TADPQSPLPI 

       190        200        210        220        230        240 
EQIEDIFIDL TNKFGFQRDS MRNMFDHFMT LLDSRSSRMS PEQALLSLHA DYIGGDTANY 

       250        260        270        280        290        300 
KKWYFAAQLD MDDEIGFRNM KLGKLSRKAR KAKKKNKKAM QEASPEDTEE TLNQIEGDNS 

       310        320        330        340        350        360 
LEAADFRWKS KMNQLSPFEM VRQIALFLLC WGEANQVRFT PECLCFIYKC ASDYLDSAQC 

       370        380        390        400        410        420 
QQRPDPLPEG DFLNRVITPL YRFIRSQVYE IVDGRYVKSE KDHNKVIGYD DVNQLFWYPE 

       430        440        450        460        470        480 
GIAKIVMEDG TRLIDLPAEE RYLKLGEIPW DDVFFKTYKE TRSWLHLVTN FNRIWIMHIS 

       490        500        510        520        530        540 
VYWMYCAYNA PTFYTHNYQQ LVDNQPLAAY KWATAALGGT VASLIQVAAT LCEWSFVPRK 

       550        560        570        580        590        600 
WAGAQHLSRR FWFLCVIMGI NLGPVIFVFA YDKDTVYSTA AHVVGAVMFF VAVATLVFFS 

       610        620        630        640        650        660 
VMPLGGLFTS YMKKSTRSYV ASQTFTASFA PLHGLDRWMS YLVWVTVFAA KYAESYFFLI 

       670        680        690        700        710        720 
LSLRDPIRIL STTSMRCTGE YWWGNKICKV QPKIVLGLMI ATDFILFFLD TYLWYIVVNT 

       730        740        750        760        770        780 
VFSVGKSFYL GISILTPWRN IFTRLPKRIY SKILATTDME IKYKPKVLIS QIWNAIIISM 

       790        800        810        820        830        840 
YREHLLAIDH VQKLLYHQVP SEIEGKRTLR APTFFVSQDD NNFETEFFPR DSEAERRISF 

       850        860        870        880        890        900 
FAQSLSTPIP EPLPVDNMPT FTVLTPHYAE RILLSLREII REDDQFSRVT LLEYLKQLHP 

       910        920        930        940        950        960 
VEWDCFVKDT KILAEETAAY ENNEDEPEKE DALKSQIDDL PFYCIGFKSA APEYTLRTRI 

       970        980        990       1000       1010       1020 
WASLRSQTLY RTISGFMNYS RAIKLLYRVE NPEIVQMFGG NADGLERELE KMARRKFKFL 

      1030       1040       1050       1060       1070       1080 
VSMQRLAKFK PHELENAEFL LRAYPDLQIA YLDEEPPLNE GEEPRIYSAL IDGHCEILEN 

      1090       1100       1110       1120       1130       1140 
GRRRPKFRVQ LSGNPILGDG KSDNQNHALI FYRGEYIQLI DANQDNYLEE CLKIRSVLAE 

      1150       1160       1170       1180       1190       1200 
FEELGIEQIH PYTPGLKYED QSTNHPVAIV GAREYIFSEN SGVLGDVAAG KEQTFGTLFA 

      1210       1220       1230       1240       1250       1260 
RTLAQIGGKL HYGHPDFINA TFMTTRGGVS KAQKGLHLNE DIYAGMNAVL RGGRIKHCEY 

      1270       1280       1290       1300       1310       1320 
YQCGKGRDLG FGTILNFTTK IGAGMGEQML SREYYYLGTQ LPIDRFLTFY YAHPGFHLNN 

      1330       1340       1350       1360       1370       1380 
LFIQLSLQMF MLTLVNLHAL AHESILCVYD RDKPITDVLY PIGCYNFHPA IDWVRRYTLS 

      1390       1400       1410       1420       1430       1440 
IFIVFWIAFV PIVVQELIER GLWKATQRFF RHILSLSPMF EVFAGQIYSS ALLSDIAVGG 

      1450       1460       1470       1480       1490       1500 
ARYISTGRGF ATSRIPFSIL YSRFAGSAIY MGSRSMLMLL FGTVAHWQAP LLWFWASLSA 

      1510       1520       1530       1540       1550       1560 
LIFAPFIFNP HQFAWEDFFL DYRDYIRWLS RGNNKYHRNS WIGYVRMSRS RVTGFKRKLV 

      1570       1580       1590       1600       1610       1620 
GDESEKSAGD ASRAHRTNLI MAEIIPCAIY AAGCFIAFTF INAQTGVKTT DEDRVNSTLR 

      1630       1640       1650       1660       1670       1680 
IIICTLAPIV IDIGVLFFCM GLSCCSGPLL GMCCKKTGSV MAGIAHGIAV VVHIVFFIVM 

      1690       1700       1710       1720       1730       1740 
WVLEGFSFVR MLIGVVTCIQ CQRLIFHCMT VLLLTREFKN DHANTAFWTG KWYSTGLGYM 

      1750       1760       1770       1780       1790       1800 
AWTQPTRELT AKVIELSEFA ADFVLGHVIL IFQLPVICIP KIDKFHSIML FWLKPSRQIR 

      1810       1820       1830       1840       1850       1860 
PPIYSLKQAR LRKRMVRRYC SLYFLVLIIF AGCIVGPAVA SAHVPKDLGS GLTGTFHNLV 

      1870       1880       1890 
QPRNVSNNDT GSQMSTYKSH YYTHTPSLKT WSTIK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae." Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y., Miyamoto C., Arisawa M., Furuichi Y., Watanabe T. Eur. J. Biochem. 231:845-854(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 295-309; 406-424 AND 935-948. Strain: ATCC 200589 / A451.
[2]	"Differential expression and function of two homologous subunits of yeast 1,3-beta-D-glucan synthase." Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A., Nielsen J.B., Foor F. Mol. Cell. Biol. 15:5671-5681(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TOPOLOGY. Strain: ATCC 204508 / S288c.
[3]	"Quantitative trait loci mapped to single-nucleotide resolution in yeast." Deutschbauer A.M., Davis R.W. Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-1059 AND 1853-LYS-ASP-1854. Strain: SK1.
[4]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding protein Rho1." Mazur P., Baginsky W. J. Biol. Chem. 271:14604-14609(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ACTIVATION BY RHO1.
[8]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-806, MASS SPECTROMETRY. Strain: SUB592.
[9]	"Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin." Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H. Genetics 167:35-49(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CASPOFUNGIN RESISTANCE.
[10]	"The Smk1p MAP kinase negatively regulates Gsc2p, a 1,3-beta-glucan synthase, during spore wall morphogenesis in Saccharomyces cerevisiae." Huang L.S., Doherty H.K., Herskowitz I. Proc. Natl. Acad. Sci. U.S.A. 102:12431-12436(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SMK1, ENZYME ACTIVITY.
[11]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[12]	"Homologous subunits of 1,3-beta-glucan synthase are important for spore wall assembly in Saccharomyces cerevisiae." Ishihara S., Hirata A., Nogami S., Beauvais A., Latge J.-P., Ohya Y. Eukaryot. Cell 6:143-156(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[13]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D42127 Genomic DNA. Translation: BAA07707.1. U16783 Genomic DNA. Translation: AAA85676.1. DQ115390 Genomic DNA. Translation: AAZ22447.1. Z72817 Genomic DNA. Translation: CAA97020.1. BK006941 Genomic DNA. Translation: DAA08129.1.
PIR	S50240.
RefSeq	NP_011546.3. NM_001181161.3.
3D structure databases
ProteinModelPortal	P40989.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2511N.
IntAct	P40989. 5 interactions.
MINT	MINT-1326074.
STRING	4932.YGR032W.
Protein family/group databases
CAZy	GT48. Glycosyltransferase Family 48.
Proteomic databases
PaxDb	P40989.
PeptideAtlas	P40989.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR032W; YGR032W; YGR032W.
GeneID	852920.
KEGG	sce:YGR032W. sce:YGR036C.
Organism-specific databases
CYGD	YGR032w.
SGD	S000003264. GSC2.
Phylogenomic databases
eggNOG	NOG307043.
GeneTree	ENSGT00390000004828.
HOGENOM	HOG000216604.
KO	K00706. K07252.
OMA	REPYPAW.
OrthoDB	EOG49PF6H.
Gene expression databases
Genevestigator	P40989.
GermOnline	YGR032W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR026899. FKS1-like_dom1. IPR003440. Glyco_trans_48. [Graphical view]
Pfam	PF14288. FKS1_dom1. 1 hit. PF02364. Glucan_synthase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P40989.
ChEMBL	CHEMBL3134.
NextBio	972628.

Entry information

Entry name

FKS2_YEAST

Accession

Primary (citable) accession number: P40989
Secondary accession number(s): D6VUG8, Q45U52

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents