GYS1_YEAST
ID GYS1_YEAST Reviewed; 708 AA.
AC P23337; D6VTP6;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Glycogen [starch] synthase isoform 1;
DE EC=2.4.1.11 {ECO:0000269|PubMed:2123485};
GN Name=GSY1; OrderedLocusNames=YFR015C;
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], PARTIAL PROTEIN SEQUENCE OF 2-17; 52-62;
RP 86-105; 377-391; 593-600; 602-608 AND 660-669, CLEAVAGE OF INITIATOR
RP METHIONINE, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=YPH52;
RX PubMed=2123485; DOI=10.1016/s0021-9258(17)45298-7;
RA Farkas I., Hardy T.A., Depaoli-Roach A.A., Roach P.J.;
RT "Isolation of the GSY1 gene encoding yeast glycogen synthase and evidence
RT for the existence of a second gene.";
RL J. Biol. Chem. 265:20879-20886(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
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 [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis
CC of glycogen. {ECO:0000269|PubMed:2123485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC Evidence={ECO:0000269|PubMed:2123485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC Evidence={ECO:0000269|PubMed:2123485};
CC -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate, and
CC phosphorylation by a cAMP-dependent kinase.
CC {ECO:0000305|PubMed:2123485}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000305|PubMed:2123485}.
CC -!- INTERACTION:
CC P23337; P27472: GSY2; NbExp=3; IntAct=EBI-8031, EBI-8036;
CC -!- DEVELOPMENTAL STAGE: Activity increases just before cells entry in the
CC stationary phase. {ECO:0000305|PubMed:2123485}.
CC -!- INDUCTION: Synthesized in response to growth limitation.
CC {ECO:0000305|PubMed:2123485}.
CC -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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DR EMBL; M60919; AAA88715.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09254.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12456.1; -; Genomic_DNA.
DR PIR; A38326; A38326.
DR RefSeq; NP_116670.1; NM_001179980.1.
DR AlphaFoldDB; P23337; -.
DR SMR; P23337; -.
DR BioGRID; 31167; 83.
DR DIP; DIP-5354N; -.
DR IntAct; P23337; 13.
DR MINT; P23337; -.
DR STRING; 4932.YFR015C; -.
DR CAZy; GT3; Glycosyltransferase Family 3.
DR iPTMnet; P23337; -.
DR MaxQB; P23337; -.
DR PaxDb; P23337; -.
DR PRIDE; P23337; -.
DR DNASU; 850569; -.
DR EnsemblFungi; YFR015C_mRNA; YFR015C; YFR015C.
DR GeneID; 850569; -.
DR KEGG; sce:YFR015C; -.
DR SGD; S000001911; GSY1.
DR VEuPathDB; FungiDB:YFR015C; -.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR HOGENOM; CLU_015910_1_0_1; -.
DR InParanoid; P23337; -.
DR OMA; YFFTSGR; -.
DR BioCyc; YEAST:YFR015C-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR PRO; PR:P23337; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P23337; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:SGD.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:SGD.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176; PTHR10176; 1.
DR Pfam; PF05693; Glycogen_syn; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Direct protein sequencing; Glycogen biosynthesis;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2123485"
FT CHAIN 2..708
FT /note="Glycogen [starch] synthase isoform 1"
FT /id="PRO_0000194773"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 660
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 662
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 708 AA; 80510 MW; 9EF2D3858529E68A CRC64;
MARDLQNHLL FEVATEVTNR VGGIYSVLKS KAPVTVAQYG DNYTLLGPLN KATYESEVEK
LDWEDESIFP EELLPIQKTL MSMREKGVNF VYGNWLIEGA PRVILFELDS VRHFLNEWKA
DLWSLVGIPS PEHDHETNDA ILLGYVVVWF LGEVSKLDSS HAIIGHFHEW LAGVALPLCR
KKRIDVVTIF TTHATLLGRY LCAAGDVDFY NNLQYFDVDQ EAGKRGIYHR YCIERAAAHT
ADVFTTVSQI TALEAEHLLK RKPDGILPNG LNVVKFQAVH EFQNLHALKK DKINDFVRGH
FHGCFDFDLD NTVYFFIAGR YEYKNKGADM FIESLARLNY RLKVSGSKKT VVAFLIMPAK
TNSFTVEALK SQAIVKSLEN TVNEVTASIG KRIFEHTMRY PHNGLESELP TNLDELLKSS
EKVLLKKRVL ALRRPYGELP PVVTHNMCDD ANDPILNQIR HVRLFNDSSD RVKVIFHPEF
LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL
IETDQAKDYG IYIVDRRFKS PDESVEQLAD YMEEFVNKTR RQRINQRNRT ERLSDLLDWK
RMGLEYVKAR QLGLRRAYPE QFKQLVGETI SDANMNTLAG GKKFKIARPL SVPGSPKVRS
NSTVYMTPGD LGTLQDANNA DDYFNLSTNG AIDNDDDDND TSAYYEDN
