GAC1_YEAST
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 03-AUG-2022, entry version 159.
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 BioGRID; 34573; 52.
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; P28006; -.
DR PRIDE; P28006; -.
DR EnsemblFungi; YOR178C_mRNA; YOR178C; YOR178C.
DR GeneID; 854350; -.
DR KEGG; sce:YOR178C; -.
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; FRNENTI; -.
DR BioCyc; YEAST:G3O-33690-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
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; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
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
