ID   GAC1_YEAST              Reviewed;         793 AA.
AC   P28006; D6W2N4; Q08551;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit GAC1;
GN   Name=GAC1; OrderedLocusNames=YOR178C;
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=1310938; DOI=10.1002/j.1460-2075.1992.tb05031.x;
RA   Francois J.M., Thompson-Jaeger S., Skroch J., Zellenka U., Spevak W.,
RA   Tatchell K.;
RT   "GAC1 may encode a regulatory subunit for protein phosphatase type 1 in
RT   Saccharomyces cerevisiae.";
RL   EMBO J. 11:87-96(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-424, 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   [5]
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: Regulates the activity of glycogen synthase. It is most
CC       probably a regulatory subunit for protein phosphatase type 1.
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DR   EMBL; X63941; CAA45371.1; -; Genomic_DNA.
DR   EMBL; Z75086; CAA99387.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10950.1; -; Genomic_DNA.
DR   PIR; S67070; S67070.
DR   RefSeq; NP_014821.3; NM_001183597.3.
DR   AlphaFoldDB; P28006; -.
DR   SMR; P28006; -.
DR   BioGRID; 34573; 62.
DR   ComplexPortal; CPX-1231; GAC1-GLC7 phosphatase complex.
DR   DIP; DIP-2375N; -.
DR   ELM; P28006; -.
DR   IntAct; P28006; 13.
DR   MINT; P28006; -.
DR   STRING; 4932.YOR178C; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   iPTMnet; P28006; -.
DR   PaxDb; 4932-YOR178C; -.
DR   PeptideAtlas; P28006; -.
DR   EnsemblFungi; YOR178C_mRNA; YOR178C; YOR178C.
DR   GeneID; 854350; -.
DR   KEGG; sce:YOR178C; -.
DR   AGR; SGD:S000005704; -.
DR   SGD; S000005704; GAC1.
DR   VEuPathDB; FungiDB:YOR178C; -.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000176558; -.
DR   HOGENOM; CLU_014598_0_0_1; -.
DR   InParanoid; P28006; -.
DR   OMA; DEHINSQ; -.
DR   OrthoDB; 2039299at2759; -.
DR   BioCyc; YEAST:G3O-33690-MONOMER; -.
DR   Reactome; R-SCE-3322077; Glycogen synthesis.
DR   BioGRID-ORCS; 854350; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P28006; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P28006; Protein.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:SGD.
DR   GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR   GO; GO:0031072; F:heat shock protein binding; IDA:SGD.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IPI:SGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IPI:SGD.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:SGD.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IMP:SGD.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   PANTHER; PTHR12307; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR12307:SF51; SERINE_THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT GAC1-RELATED; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   1: Evidence at protein level;
KW   Glycogen biosynthesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..793
FT                   /note="Serine/threonine-protein phosphatase 1 regulatory
FT                   subunit GAC1"
FT                   /id="PRO_0000071518"
FT   DOMAIN          235..360
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        228
FT                   /note="S -> SS (in Ref. 1; CAA45371)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   793 AA;  88533 MW;  1880E966A6480D80 CRC64;
     MVIQTATTLS PAKARPSFPH NDLIKSMSDS LISRPTHPPI RKLKSSLKIS HPEPISRSKS
     EIFCTSPEKN VRFAIELTTV KRFDKNAEPS SISNENSPTL SPVDSNTAAD DVQLFNNEDC
     WFNDSSLVTN LLKNEKKFRY MNSLNNMFKL DLYDSEDEDD IDEHINSQAE YGYTYNSLST
     RGKTSENKSA TSSLATQATN ICDWKLHCTD LVPFKIAPPL FTKTLSASDL QGQLTKYLNG
     QNVKLHSLTQ LGDDSSKITG LVYVKNLSFE KYLEIKFTFN SWRDIHYVTA NFNRTINSNV
     DEFKFTIDLN SLKYILLIKR IITMEKNTSS CPLNIELCCR YDVNNETYYD NNNGKNYHLF
     MTTFKKGGET KEKIPVVVEP ASQTDAAMSP KEMKARFVSS NPTLSRFLPQ SRKFSEDTDY
     YNTSPLKHLY HNDTTSWVKP KRLNVVLDKL ENATPPPPSS ALANDTARTG KITKDKNNVL
     APPTASNSID LPILGSQHQS LYSGSSSYSS SSSSISSSLS FASSNNSSTN SSSASCSFPL
     TELDNFDYAN LYEPNDTFTT ANLFNHSLNS LMPEISTPSF FGGFRNENTI NNNDSKNLVT
     SLEDSYEDKQ SVITDTTMDE NNKTSTINNS TDTLIKPSKE NGTVKENKSS ANSTSAPSSS
     QNRASTILND HSNGKSDLKY VNYQSLLDSH CFYNHPSSPN LQSTSFSSAA PFSGISQASD
     IFDYENEDSD SNQIAGEIDN NSFPPHFYLD EDDKSACLSD DALIDHHRNT NPFINTFSSS
     PPILSQEVDR WRL
//