FKS2_YEAST
ID FKS2_YEAST Reviewed; 1895 AA.
AC P40989; D6VUG8; Q45U52;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=1,3-beta-glucan synthase component GSC2;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
DE AltName: Full=FK506 sensitivity protein 2;
DE AltName: Full=Glucan synthase of cerevisiae protein 2;
GN Name=GSC2; Synonyms=FKS2, GLS2; OrderedLocusNames=YGR032W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 295-309; 406-424
RP AND 935-948.
RC STRAIN=ATCC 200589 / A451;
RX PubMed=7649185; DOI=10.1111/j.1432-1033.1995.tb20770.x;
RA Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y.,
RA Miyamoto C., Arisawa M., Furuichi Y., Watanabe T.;
RT "Characterization and gene cloning of 1,3-beta-D-glucan synthase from
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 231:845-854(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND TOPOLOGY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7565718; DOI=10.1128/mcb.15.10.5671;
RA Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A.,
RA Nielsen J.B., Foor F.;
RT "Differential expression and function of two homologous subunits of yeast
RT 1,3-beta-D-glucan synthase.";
RL Mol. Cell. Biol. 15:5671-5681(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-1059 AND
RP 1853-LYS-ASP-1854.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP ACTIVATION BY RHO1.
RX PubMed=8662910; DOI=10.1074/jbc.271.24.14604;
RA Mazur P., Baginsky W.;
RT "In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding
RT protein Rho1.";
RL J. Biol. Chem. 271:14604-14609(1996).
RN [8]
RP CASPOFUNGIN RESISTANCE.
RX PubMed=15166135; DOI=10.1534/genetics.167.1.35;
RA Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.;
RT "Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a
RT synthetic interaction network and altered sensitivity to caspofungin.";
RL Genetics 167:35-49(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SMK1, AND ENZYME
RP ACTIVITY.
RX PubMed=16116083; DOI=10.1073/pnas.0502324102;
RA Huang L.S., Doherty H.K., Herskowitz I.;
RT "The Smk1p MAP kinase negatively regulates Gsc2p, a 1,3-beta-glucan
RT synthase, during spore wall morphogenesis in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12431-12436(2005).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [11]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=17158736; DOI=10.1128/ec.00200-06;
RA Ishihara S., Hirata A., Nogami S., Beauvais A., Latge J.-P., Ohya Y.;
RT "Homologous subunits of 1,3-beta-glucan synthase are important for spore
RT wall assembly in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 6:143-156(2007).
CC -!- FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase
CC (GS). Synthesizes 1,3-beta-glucan, a major structural component of the
CC yeast cell wall. Required for spore wall assembly. Negative regulation
CC of activity by SMK1 is important for spore wall deposition. Activity is
CC positively regulated by RHO1. {ECO:0000269|PubMed:17158736,
CC ECO:0000269|PubMed:7565718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000269|PubMed:16116083, ECO:0000269|PubMed:17158736};
CC -!- SUBUNIT: Component of the 1,3-beta-glucan synthase (GS), composed of
CC two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit
CC RHO1. Interacts with SMK1. {ECO:0000269|PubMed:16116083}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7565718}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:7565718}.
CC -!- INDUCTION: Under starvation and during sporulation. Also by pheromones
CC and calcium in a calcineurin-dependent manner.
CC {ECO:0000269|PubMed:7565718}.
CC -!- MISCELLANEOUS: Deletion leads to caspofungin resistance.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; D42127; BAA07707.1; -; Genomic_DNA.
DR EMBL; U16783; AAA85676.1; -; Genomic_DNA.
DR EMBL; DQ115390; AAZ22447.1; -; Genomic_DNA.
DR EMBL; Z72817; CAA97020.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08129.1; -; Genomic_DNA.
DR PIR; S50240; S50240.
DR RefSeq; NP_011546.3; NM_001181161.3.
DR AlphaFoldDB; P40989; -.
DR BioGRID; 33277; 91.
DR ComplexPortal; CPX-1813; 1,3-beta-D-glucan synthase complex, FKS2-RHO1 variant.
DR DIP; DIP-2511N; -.
DR IntAct; P40989; 6.
DR MINT; P40989; -.
DR STRING; 4932.YGR032W; -.
DR BindingDB; P40989; -.
DR ChEMBL; CHEMBL3134; -.
DR DrugBank; DB12471; Ibrexafungerp.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; P40989; -.
DR MaxQB; P40989; -.
DR PaxDb; P40989; -.
DR PRIDE; P40989; -.
DR TopDownProteomics; P40989; -.
DR EnsemblFungi; YGR032W_mRNA; YGR032W; YGR032W.
DR GeneID; 852920; -.
DR KEGG; sce:YGR032W; -.
DR SGD; S000003264; GSC2.
DR VEuPathDB; FungiDB:YGR032W; -.
DR eggNOG; KOG0916; Eukaryota.
DR GeneTree; ENSGT00940000176776; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; P40989; -.
DR OMA; AWTDFFI; -.
DR BioCyc; YEAST:YGR032W-MON; -.
DR BRENDA; 2.4.1.34; 984.
DR PRO; PR:P40989; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P40989; protein.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:SGD.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Cell shape; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Glycosyltransferase; Isopeptide bond; Membrane; Phosphoprotein;
KW Reference proteome; Sporulation; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1895
FT /note="1,3-beta-glucan synthase component GSC2"
FT /id="PRO_0000121726"
FT TOPO_DOM 1..473
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..1579
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1580..1600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1601..1620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1621..1641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1642..1758
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1759..1779
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1780..1821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1822..1842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1843..1895
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 405
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 934
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 1558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT CROSSLNK 1566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P38631"
FT VARIANT 1059
FT /note="N -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 1853..1854
FT /note="TG -> KD (in strain: SK1)"
FT CONFLICT 137
FT /note="A -> T (in Ref. 1; BAA07707)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="K -> E (in Ref. 1; BAA07707)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="K -> R (in Ref. 1; BAA07707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1895 AA; 216990 MW; 9DDE4D8C19BC24DA CRC64;
MSYNDPNLNG QYYSNGDGTG DGNYPTYQVT QDQSAYDEYG QPIYTQNQLD DGYYDPNEQY
VDGTQFPQGQ DPSQDQGPYN NDASYYNQPP NMMNPSSQDG ENFSDFSSYG PPSGTYPNDQ
YTPSQMSYPD QDGSSGASTP YGNGVVNGNG QYYDPNAIEM ALPNDPYPAW TADPQSPLPI
EQIEDIFIDL TNKFGFQRDS MRNMFDHFMT LLDSRSSRMS PEQALLSLHA DYIGGDTANY
KKWYFAAQLD MDDEIGFRNM KLGKLSRKAR KAKKKNKKAM QEASPEDTEE TLNQIEGDNS
LEAADFRWKS KMNQLSPFEM VRQIALFLLC WGEANQVRFT PECLCFIYKC ASDYLDSAQC
QQRPDPLPEG DFLNRVITPL YRFIRSQVYE IVDGRYVKSE KDHNKVIGYD DVNQLFWYPE
GIAKIVMEDG TRLIDLPAEE RYLKLGEIPW DDVFFKTYKE TRSWLHLVTN FNRIWIMHIS
VYWMYCAYNA PTFYTHNYQQ LVDNQPLAAY KWATAALGGT VASLIQVAAT LCEWSFVPRK
WAGAQHLSRR FWFLCVIMGI NLGPVIFVFA YDKDTVYSTA AHVVGAVMFF VAVATLVFFS
VMPLGGLFTS YMKKSTRSYV ASQTFTASFA PLHGLDRWMS YLVWVTVFAA KYAESYFFLI
LSLRDPIRIL STTSMRCTGE YWWGNKICKV QPKIVLGLMI ATDFILFFLD TYLWYIVVNT
VFSVGKSFYL GISILTPWRN IFTRLPKRIY SKILATTDME IKYKPKVLIS QIWNAIIISM
YREHLLAIDH VQKLLYHQVP SEIEGKRTLR APTFFVSQDD NNFETEFFPR DSEAERRISF
FAQSLSTPIP EPLPVDNMPT FTVLTPHYAE RILLSLREII REDDQFSRVT LLEYLKQLHP
VEWDCFVKDT KILAEETAAY ENNEDEPEKE DALKSQIDDL PFYCIGFKSA APEYTLRTRI
WASLRSQTLY RTISGFMNYS RAIKLLYRVE NPEIVQMFGG NADGLERELE KMARRKFKFL
VSMQRLAKFK PHELENAEFL LRAYPDLQIA YLDEEPPLNE GEEPRIYSAL IDGHCEILEN
GRRRPKFRVQ LSGNPILGDG KSDNQNHALI FYRGEYIQLI DANQDNYLEE CLKIRSVLAE
FEELGIEQIH PYTPGLKYED QSTNHPVAIV GAREYIFSEN SGVLGDVAAG KEQTFGTLFA
RTLAQIGGKL HYGHPDFINA TFMTTRGGVS KAQKGLHLNE DIYAGMNAVL RGGRIKHCEY
YQCGKGRDLG FGTILNFTTK IGAGMGEQML SREYYYLGTQ LPIDRFLTFY YAHPGFHLNN
LFIQLSLQMF MLTLVNLHAL AHESILCVYD RDKPITDVLY PIGCYNFHPA IDWVRRYTLS
IFIVFWIAFV PIVVQELIER GLWKATQRFF RHILSLSPMF EVFAGQIYSS ALLSDIAVGG
ARYISTGRGF ATSRIPFSIL YSRFAGSAIY MGSRSMLMLL FGTVAHWQAP LLWFWASLSA
LIFAPFIFNP HQFAWEDFFL DYRDYIRWLS RGNNKYHRNS WIGYVRMSRS RVTGFKRKLV
GDESEKSAGD ASRAHRTNLI MAEIIPCAIY AAGCFIAFTF INAQTGVKTT DEDRVNSTLR
IIICTLAPIV IDIGVLFFCM GLSCCSGPLL GMCCKKTGSV MAGIAHGIAV VVHIVFFIVM
WVLEGFSFVR MLIGVVTCIQ CQRLIFHCMT VLLLTREFKN DHANTAFWTG KWYSTGLGYM
AWTQPTRELT AKVIELSEFA ADFVLGHVIL IFQLPVICIP KIDKFHSIML FWLKPSRQIR
PPIYSLKQAR LRKRMVRRYC SLYFLVLIIF AGCIVGPAVA SAHVPKDLGS GLTGTFHNLV
QPRNVSNNDT GSQMSTYKSH YYTHTPSLKT WSTIK
