ID   GLC8_YEAST              Reviewed;         229 AA.
AC   P41818; D6W0D8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Protein GLC8;
GN   Name=GLC8; OrderedLocusNames=YMR311C; ORFNames=YM9924.03C;
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].
RX   PubMed=8150278; DOI=10.1093/genetics/136.2.485;
RA   Cannon J.F., Pringle J.R., Fiechter A., Khalil M.;
RT   "Characterization of glycogen-deficient glc mutants of Saccharomyces
RT   cerevisiae.";
RL   Genetics 136:485-503(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PHOSPHORYLATION AT THR-118.
RX   PubMed=12407105; DOI=10.1074/jbc.m208058200;
RA   Tan Y.S.H., Morcos P.A., Cannon J.F.;
RT   "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in
RT   vivo.";
RL   J. Biol. Chem. 278:147-153(2003).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, AND IDENTIFICATION BY
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-158 AND SER-184, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-158 AND SER-184, 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).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Modulator of GLC7 type-1 protein phosphatase.
CC   -!- INTERACTION:
CC       P41818; P32598: GLC7; NbExp=5; IntAct=EBI-7629, EBI-13715;
CC   -!- PTM: Phosphorylated by the cyclin-CDKs PCL6-PHO85 and PCL7-PHO85.
CC       Phosphorylation of Thr-118 inactivates GLC8.
CC       {ECO:0000269|PubMed:12407105}.
CC   -!- MISCELLANEOUS: Present with 3440 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L22000; AAA53673.1; -; Genomic_DNA.
DR   EMBL; Z54141; CAA90829.1; -; Genomic_DNA.
DR   EMBL; AY557977; AAS56303.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10212.1; -; Genomic_DNA.
DR   PIR; S47859; S47859.
DR   RefSeq; NP_014042.1; NM_001182822.1.
DR   AlphaFoldDB; P41818; -.
DR   BioGRID; 35491; 130.
DR   DIP; DIP-2349N; -.
DR   ELM; P41818; -.
DR   IntAct; P41818; 4.
DR   MINT; P41818; -.
DR   STRING; 4932.YMR311C; -.
DR   iPTMnet; P41818; -.
DR   MaxQB; P41818; -.
DR   PaxDb; 4932-YMR311C; -.
DR   PeptideAtlas; P41818; -.
DR   EnsemblFungi; YMR311C_mRNA; YMR311C; YMR311C.
DR   GeneID; 855359; -.
DR   KEGG; sce:YMR311C; -.
DR   AGR; SGD:S000004928; -.
DR   SGD; S000004928; GLC8.
DR   VEuPathDB; FungiDB:YMR311C; -.
DR   eggNOG; ENOG502S2VH; Eukaryota.
DR   HOGENOM; CLU_070379_1_0_1; -.
DR   InParanoid; P41818; -.
DR   OMA; LQWNQKN; -.
DR   OrthoDB; 2731313at2759; -.
DR   BioCyc; YEAST:G3O-32975-MONOMER; -.
DR   BioGRID-ORCS; 855359; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P41818; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P41818; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR   GO; GO:0005978; P:glycogen biosynthetic process; TAS:SGD.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   InterPro; IPR007062; PPI-2.
DR   PANTHER; PTHR12398:SF20; PROTEIN PHOSPHATASE 1, REGULATORY (INHIBITOR) SUBUNIT 2; 1.
DR   PANTHER; PTHR12398; PROTEIN PHOSPHATASE INHIBITOR; 1.
DR   Pfam; PF04979; IPP-2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..229
FT                   /note="Protein GLC8"
FT                   /id="PRO_0000071517"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         118
FT                   /note="Phosphothreonine; by PHO85"
FT                   /evidence="ECO:0000269|PubMed:12407105"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   229 AA;  26649 MW;  D4017CA8B3B089C2 CRC64;
     MGGILKNPLA LSPEQLAQQD PETLEEFRRQ VYENTQKNAK LTSHKRNIPG LDNTKEEGEI
     IGTSSTFLPK DTLSLKHEQD MLAKMTPEER VQWNQRNLAE NEITKKQFQD IHIDEPKTPY
     QGAVDPHGEY YRVDDDEDED NSDKKPCQVA NDDIDDLSLG EPEFEIKENK QPDFETNDEN
     DEDSPEARHK KFEEMRKKHY DVRAIFNKKS REALKDEDED EDDSTTKEP
//