PP12_YEAST
ID PP12_YEAST Reviewed; 312 AA.
AC P32598; D3DM39;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-2;
DE EC=3.1.3.16;
GN Name=GLC7; Synonyms=CID1, DIS2; OrderedLocusNames=YER133W;
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=1660885; DOI=10.1016/s0021-9258(18)54353-2;
RA Feng Z.H., Wilson S.E., Peng Z.Y., Schlender K.K., Reimann E.M.,
RA Trumbly R.J.;
RT "The yeast GLC7 gene required for glycogen accumulation encodes a type 1
RT protein phosphatase.";
RL J. Biol. Chem. 266:23796-23801(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544298; DOI=10.1016/0092-8674(89)90338-3;
RA Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.;
RT "The fission yeast dis2+ gene required for chromosome disjoining encodes
RT one of two putative type 1 protein phosphatases.";
RL Cell 57:997-1007(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-73.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9;
RA Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K.,
RA Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M.,
RA Allis C.D.;
RT "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase
RT and Glc7/PP1 phosphatase in budding yeast and nematodes.";
RL Cell 102:279-291(2000).
RN [7]
RP INTERACTION WITH BUD14.
RX PubMed=12477789; DOI=10.1128/ec.1.6.884-894.2002;
RA Cullen P.J., Sprague G.F. Jr.;
RT "The Glc7p-interacting protein Bud14p attenuates polarized growth,
RT pheromone response, and filamentous growth in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:884-894(2002).
RN [8]
RP INTERACTION WITH SCD5.
RX PubMed=12356757; DOI=10.1074/jbc.m208471200;
RA Chang J.S., Henry K., Wolf B.L., Geli M., Lemmon S.K.;
RT "Protein phosphatase-1 binding to scd5p is important for regulation of
RT actin organization and endocytosis in yeast.";
RL J. Biol. Chem. 277:48002-48008(2002).
RN [9]
RP IDENTIFICATION IN THE CPF COMPLEX, COMPOSITION OF THE APT COMPLEX,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA Buratowski S., Moore C.L., Greenblatt J.;
RT "Organization and function of APT, a subcomplex of the yeast cleavage and
RT polyadenylation factor involved in the formation of mRNA and small
RT nucleolar RNA 3'-ends.";
RL J. Biol. Chem. 278:33000-33010(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH YPI1.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [11]
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 [12]
RP INTERACTION WITH BUD14, AND FUNCTION OF THE BUD14-GLC7 COMPLEX.
RX PubMed=16107882; DOI=10.1038/sj.emboj.7600783;
RA Knaus M., Cameroni E., Pedruzzi I., Tatchell K., De Virgilio C., Peter M.;
RT "The Bud14p-Glc7p complex functions as a cortical regulator of dynein in
RT budding yeast.";
RL EMBO J. 24:3000-3011(2005).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-22 AND LYS-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in control of glycogen metabolism, meiosis,
CC translation, chromosome segregation, cell polarity and G2/M cell cycle
CC progression. PP1 may act in opposition to the IPL1 protein kinase in
CC regulating chromosome segregation by dephosphorylating H3S10ph. The
CC BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the
CC cortex and may function as a specific activator of the dynein complex.
CC -!- FUNCTION: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which plays a key role in polyadenylation-dependent pre-mRNA
CC 3'-end formation and cooperates with cleavage factors including the
CC CFIA complex and NAB4/CFIB. Component of the APT complex, which may be
CC involved in polyadenylation-independent transcript 3'-end formation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Probably complexed with regulatory or targeting subunits
CC (PubMed:12819204). Component of the cleavage and polyadenylation factor
CC (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1,
CC REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and
CC PAP1 (PubMed:12819204). Component of the APT complex, which is a
CC subcomplex of CPF, and is composed of PTI1, SYC1, SSU72, GLC7, REF2,
CC PTA1 and SWD2 (PubMed:12819204). Interacts with BUD14 (PubMed:12477789,
CC PubMed:16107882). Interacts with YPI1 (PubMed:14690591). Interacts with
CC SCD5 (via KKVRF motif) (PubMed:12356757). {ECO:0000269|PubMed:12356757,
CC ECO:0000269|PubMed:12477789, ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:16107882}.
CC -!- INTERACTION:
CC P32598; P53858: BNI4; NbExp=4; IntAct=EBI-13715, EBI-3704;
CC P32598; P27637: BUD14; NbExp=7; IntAct=EBI-13715, EBI-20747;
CC P32598; P39732: GIP4; NbExp=4; IntAct=EBI-13715, EBI-20636;
CC P32598; P41818: GLC8; NbExp=5; IntAct=EBI-13715, EBI-7629;
CC P32598; Q12276: HER1; NbExp=4; IntAct=EBI-13715, EBI-35056;
CC P32598; P43638: MHP1; NbExp=5; IntAct=EBI-13715, EBI-10880;
CC P32598; P42073: REF2; NbExp=8; IntAct=EBI-13715, EBI-14915;
CC P32598; Q00816: REG1; NbExp=4; IntAct=EBI-13715, EBI-8270;
CC P32598; P34758: SCD5; NbExp=4; IntAct=EBI-13715, EBI-16685;
CC P32598; P36047: SDS22; NbExp=15; IntAct=EBI-13715, EBI-16783;
CC P32598; Q00416: SEN1; NbExp=8; IntAct=EBI-13715, EBI-16945;
CC P32598; P50278: SOL1; NbExp=3; IntAct=EBI-13715, EBI-17675;
CC P32598; P36104: SWD2; NbExp=5; IntAct=EBI-13715, EBI-26608;
CC P32598; P43587: YPI1; NbExp=11; IntAct=EBI-13715, EBI-22913;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12819204}. Nucleus
CC {ECO:0000269|PubMed:12819204}.
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M77175; AAB59322.1; -; Genomic_DNA.
DR EMBL; M27070; AAA34570.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03231.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07793.1; -; Genomic_DNA.
DR PIR; S32595; S32595.
DR RefSeq; NP_011059.3; NM_001179023.3.
DR AlphaFoldDB; P32598; -.
DR SMR; P32598; -.
DR BioGRID; 36877; 697.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR ComplexPortal; CPX-1230; BNI4-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1231; GAC1-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1249; SDS22-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1260; SDS22-GLC7-YPI1 phosphatase complex.
DR ComplexPortal; CPX-1266; REG1-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1267; REG2-GLC7 phosphatase complex.
DR ComplexPortal; CPX-1705; BUD14-GLC7 phosphatase complex.
DR DIP; DIP-1336N; -.
DR ELM; P32598; -.
DR IntAct; P32598; 183.
DR MINT; P32598; -.
DR STRING; 4932.YER133W; -.
DR iPTMnet; P32598; -.
DR MaxQB; P32598; -.
DR PaxDb; P32598; -.
DR PRIDE; P32598; -.
DR EnsemblFungi; YER133W_mRNA; YER133W; YER133W.
DR GeneID; 856870; -.
DR KEGG; sce:YER133W; -.
DR SGD; S000000935; GLC7.
DR VEuPathDB; FungiDB:YER133W; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000164151; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P32598; -.
DR OMA; EEHEIRY; -.
DR BioCyc; YEAST:YER133W-MON; -.
DR PRO; PR:P32598; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32598; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0001400; C:mating projection base; IDA:SGD.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IC:ComplexPortal.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0051276; P:chromosome organization; IC:ComplexPortal.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
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:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IC:ComplexPortal.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:ComplexPortal.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IGI:SGD.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:ComplexPortal.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR GO; GO:0007116; P:regulation of cell budding; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IGI:SGD.
DR GO; GO:1904547; P:regulation of cellular response to glucose starvation; IC:ComplexPortal.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IC:ComplexPortal.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IMP:SGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:SGD.
DR GO; GO:1901901; P:regulation of protein localization to cell division site involved in cytokinesis; IMP:SGD.
DR GO; GO:0031297; P:replication fork processing; IMP:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037981; PPP1CC.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF204; PTHR11668:SF204; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cell cycle; Cell division; Cytoplasm;
KW Glycogen metabolism; Hydrolase; Isopeptide bond; Manganese; Metal-binding;
KW Mitosis; mRNA processing; Nucleus; Protein phosphatase; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..312
FT /note="Serine/threonine-protein phosphatase PP1-2"
FT /id="PRO_0000058820"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 73
FT /note="R->C: In GLC7-1; decreased glycogen accumulation."
FT /evidence="ECO:0000269|PubMed:8150278"
FT CONFLICT 137
FT /note="D -> H (in Ref. 2; AAA34570)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="G -> V (in Ref. 2; AAA34570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35907 MW; 71B20E3A4ED93235 CRC64;
MDSQPVDVDN IIDRLLEVRG SKPGQQVDLE ENEIRYLCSK ARSIFIKQPI LLELEAPIKI
CGDIHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFIL
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFC MHGGLSPDLN
SMEQIRRVMR PTDIPDVGLL CDLLWSDPDK DIVGWSENDR GVSFTFGPDV VNRFLQKQDM
ELICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAQK
SLPRQAGGRK KK
