PP1G_MOUSE
ID PP1G_MOUSE Reviewed; 323 AA.
AC P63087; O09186; O09189; P37139; Q64679;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit;
DE Short=PP-1G;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 1C catalytic subunit;
GN Name=Ppp1cc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=129, and CD-1; TISSUE=Embryo;
RX PubMed=9339378; DOI=10.1006/geno.1997.4907;
RA Okano K., Heng H., Trevisanato S., Tyers M., Varmuza S.;
RT "Genomic organization and functional analysis of the murine protein
RT phosphatase 1c gamma (Ppp1cc) gene.";
RL Genomics 45:211-215(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Harada Y., Sato E., Izumi F., Imamura Y., Ariga H., Iguchi-Ariga S.;
RT "Tertially complex among Pim-1 kinase, protein phosphatase 1 gamma, and
RT PAP-1.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, and Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 61-74 AND 114-122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=9882500; DOI=10.1006/dbio.1998.9100;
RA Varmuza S., Jurisicova A., Okano K., Hudson J., Boekelheide K., Shipp E.B.;
RT "Spermiogenesis is impaired in mice bearing a targeted mutation in the
RT protein phosphatase 1cgamma gene.";
RL Dev. Biol. 205:98-110(1999).
RN [7]
RP INTERACTION WITH PPP1R15B.
RX PubMed=14638860; DOI=10.1083/jcb.200308075;
RA Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.;
RT "Inhibition of a constitutive translation initiation factor 2alpha
RT phosphatase, CReP, promotes survival of stressed cells.";
RL J. Cell Biol. 163:767-775(2003).
RN [8]
RP INTERACTION WITH SPZ1.
RX PubMed=15226296; DOI=10.1074/jbc.m403710200;
RA Hrabchak C., Varmuza S.;
RT "Identification of the spermatogenic zip protein Spz1 as a putative protein
RT phosphatase-1 (PP1) regulatory protein that specifically binds the
RT PP1cgamma2 splice variant in mouse testis.";
RL J. Biol. Chem. 279:37079-37086(2004).
RN [9]
RP IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
RX PubMed=16835242; DOI=10.1074/jbc.m513556200;
RA Latreille M., Larose L.;
RT "Nck in a complex containing the catalytic subunit of protein phosphatase 1
RT regulates eukaryotic initiation factor 2alpha signaling and cell survival
RT to endoplasmic reticulum stress.";
RL J. Biol. Chem. 281:26633-26644(2006).
RN [10]
RP INTERACTION WITH SH3GLB1.
RC STRAIN=CD-1;
RX PubMed=17381077; DOI=10.1021/bi6025837;
RA Hrabchak C., Henderson H., Varmuza S.;
RT "A testis specific isoform of endophilin B1, endophilin B1t, interacts
RT specifically with protein phosphatase-1c gamma2 in mouse testis and is
RT abnormally expressed in PP1c gamma null mice.";
RL Biochemistry 46:4635-4644(2007).
RN [11]
RP INTERACTION WITH PPP1R42.
RX PubMed=19886865; DOI=10.1042/bc20090091;
RA Wang R., Kaul A., Sperry A.O.;
RT "TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal
RT complex in the testis.";
RL Biol. Cell 102:173-189(2010).
RN [12]
RP INTERACTION WITH IKFZ1.
RX PubMed=19282287; DOI=10.1074/jbc.m900209200;
RA Popescu M., Gurel Z., Ronni T., Song C., Hung K.Y., Payne K.J., Dovat S.;
RT "Ikaros stability and pericentromeric localization are regulated by protein
RT phosphatase 1.";
RL J. Biol. Chem. 284:13869-13880(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21712997; DOI=10.1371/journal.pone.0021325;
RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the
RT mammalian circadian clock.";
RL PLoS ONE 6:E21325-E21325(2011).
RN [15]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21930935; DOI=10.1073/pnas.1107178108;
RA Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
RT "The period of the circadian oscillator is primarily determined by the
RT balance between casein kinase 1 and protein phosphatase 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
RN [16]
RP DISRUPTION PHENOTYPE, AND FUNCTION (ISOFORM 2).
RX PubMed=23082183; DOI=10.1371/journal.pone.0047623;
RA Sinha N., Pilder S., Vijayaraghavan S.;
RT "Significant expression levels of transgenic PPP1CC2 in testis and sperm
RT are required to overcome the male infertility phenotype of Ppp1cc null
RT mice.";
RL PLoS ONE 7:E47623-E47623(2012).
RN [17]
RP INTERACTION (ISOFORM 2) WITH TMEM225.
RX PubMed=25605614; DOI=10.1002/mrd.22453;
RA Matsuura M., Yogo K.;
RT "TMEM225: a possible protein phosphatase 1gamma2 (PP1gamma2) regulator
RT localizes to the equatorial segment in mouse spermatozoa.";
RL Mol. Reprod. Dev. 82:139-148(2015).
CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC proteins to form highly specific holoenzymes which dephosphorylate
CC hundreds of biological targets. Protein phosphatase 1 (PP1) is
CC essential for cell division, and participates in the regulation of
CC glycogen metabolism, muscle contractility and protein synthesis.
CC Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances
CC and long-term synaptic plasticity. May play an important role in
CC dephosphorylating substrates such as the postsynaptic density-
CC associated Ca(2+)/calmodulin dependent protein kinase II. Component of
CC the PTW/PP1 phosphatase complex, which plays a role in the control of
CC chromatin structure and cell cycle progression during the transition
CC from mitosis into interphase. In balance with CSNK1D and CSNK1E,
CC determines the circadian period length, through the regulation of the
CC speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997,
CC ECO:0000269|PubMed:21930935}.
CC -!- FUNCTION: [Isoform 2]: Required for normal male fertility.
CC {ECO:0000269|PubMed:23082183}.
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 -!- ACTIVITY REGULATION: Inactivated by binding to URI1. {ECO:0000250}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then complexed to one or several targeting or
CC regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to
CC myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C,
CC PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts
CC with PPP1R3B, PPP1R7 and CDCA2 (By similarity). Isoform 2 interacts
CC with SPZ1. This interaction can prevent SPZ1 binding to the E-box and
CC inhibits PPP1CC activity. PPP1R15A and PPP1R15B mediate binding to
CC EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2.
CC Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric
CC heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it
CC from degradation. Interacts with NOM1 and PPP1R8. Component of the
CC PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82,
CC and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with
CC NEK2. Interacts with NEK2. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth factor-dependent
CC manner (By similarity). Isoform 2 interacts with PPP1R42; the
CC interaction is direct. Interacts with FOXP3 (By similarity). Isoform 2
CC interacts with TMEM225 (via RVxF motif) (PubMed:25605614). Isoform 2,
CC but not isoform 1, interacts with Sh3glb1 testis-specific isoform 3;
CC this interaction leads to the inhibition of phosphatase activity
CC (PubMed:17381077). Interacts with MKI67 (By similarity). Interacts with
CC RRP1B; this targets PPP1CC to the nucleolus (By similarity). Found in a
CC complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By similarity)
CC (PubMed:14638860, PubMed:15226296, PubMed:16835242, PubMed:17381077,
CC PubMed:19282287, PubMed:19886865, PubMed:25605614). Interacts with
CC DYNLT4 (By similarity). {ECO:0000250|UniProtKB:P36873,
CC ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:15226296,
CC ECO:0000269|PubMed:16835242, ECO:0000269|PubMed:17381077,
CC ECO:0000269|PubMed:19282287, ECO:0000269|PubMed:19886865,
CC ECO:0000269|PubMed:25605614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36873}. Nucleus
CC {ECO:0000250|UniProtKB:P36873}. Cleavage furrow
CC {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P36873}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P36873}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:P36873}. Nucleus speckle
CC {ECO:0000250|UniProtKB:P36873}. Midbody {ECO:0000250|UniProtKB:P36873}.
CC Mitochondrion {ECO:0000250|UniProtKB:P36873}. Cytoplasm, cytoskeleton,
CC microtubule organizing center {ECO:0000250|UniProtKB:P36873}.
CC Note=Colocalizes with SPZ1 in the nucleus (PubMed:15226296).
CC Colocalizes with URI1 at mitochondrion. Rapidly exchanges between the
CC nucleolar, nucleoplasmic and cytoplasmic compartments (By similarity).
CC Highly mobile in cells and can be relocalized through interaction with
CC targeting subunits (By similarity). In the presence of PPP1R8
CC relocalizes from the nucleolus to nuclear speckles (By similarity).
CC Shows a dynamic targeting to specific sites throughout the cell cycle
CC (By similarity). Highly concentrated in nucleoli of interphase cells
CC and localizes at kinetochores early in mitosis (By similarity).
CC Relocalization to chromosome-containing regions occurs at the
CC transition from early to late anaphase (By similarity). Also
CC accumulates at the cleavage furrow and midbody by telophase (By
CC similarity). {ECO:0000250|UniProtKB:P36873,
CC ECO:0000269|PubMed:15226296}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Gamma-1, Pppcc1;
CC IsoId=P63087-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma-2, Pppcc2;
CC IsoId=P63087-2; Sequence=VSP_005095;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed (PubMed:9339378).
CC Isoform 2 is highly enriched in testis, mainly restricted to meiotic
CC and postmeiotic germ cells (PubMed:9339378).
CC {ECO:0000269|PubMed:9339378}.
CC -!- PTM: Phosphorylated by NEK2. {ECO:0000250|UniProtKB:P36873}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit male infertility due to
CC severely impaired spermiogenesis beginning at the round spermatid
CC stage. Females are fertile. {ECO:0000269|PubMed:23082183,
CC ECO:0000269|PubMed:9882500}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; M27071; AAA37526.1; -; mRNA.
DR EMBL; U53456; AAC53383.1; -; mRNA.
DR EMBL; U53276; AAC53384.1; -; Genomic_DNA.
DR EMBL; U53271; AAC53384.1; JOINED; Genomic_DNA.
DR EMBL; U53272; AAC53384.1; JOINED; Genomic_DNA.
DR EMBL; U53273; AAC53384.1; JOINED; Genomic_DNA.
DR EMBL; U53275; AAC53384.1; JOINED; Genomic_DNA.
DR EMBL; U53276; AAC53385.1; -; Genomic_DNA.
DR EMBL; U53271; AAC53385.1; JOINED; Genomic_DNA.
DR EMBL; U53272; AAC53385.1; JOINED; Genomic_DNA.
DR EMBL; U53273; AAC53385.1; JOINED; Genomic_DNA.
DR EMBL; U53275; AAC53385.1; JOINED; Genomic_DNA.
DR EMBL; D85137; BAA19729.1; -; mRNA.
DR EMBL; BC010613; AAH10613.1; -; mRNA.
DR EMBL; BC021646; AAH21646.1; -; mRNA.
DR EMBL; BC085496; AAH85496.1; -; mRNA.
DR CCDS; CCDS19643.1; -. [P63087-1]
DR PIR; C32550; C32550.
DR RefSeq; NP_038664.2; NM_013636.3. [P63087-1]
DR RefSeq; XP_006508478.1; XM_006508415.3.
DR RefSeq; XP_006530263.1; XM_006530200.2. [P63087-2]
DR PDB; 4V0U; X-ray; 7.88 A; D/F/H/J/N=1-323.
DR PDB; 4V0V; X-ray; 1.61 A; A/C=7-300.
DR PDB; 4V0W; X-ray; 1.55 A; A/C=7-300.
DR PDB; 4V0X; X-ray; 1.85 A; A=7-300.
DR PDBsum; 4V0U; -.
DR PDBsum; 4V0V; -.
DR PDBsum; 4V0W; -.
DR PDBsum; 4V0X; -.
DR AlphaFoldDB; P63087; -.
DR SMR; P63087; -.
DR BioGRID; 202337; 48.
DR BioGRID; 241685; 3.
DR IntAct; P63087; 27.
DR MINT; P63087; -.
DR STRING; 10090.ENSMUSP00000099587; -.
DR iPTMnet; P63087; -.
DR PhosphoSitePlus; P63087; -.
DR SwissPalm; P63087; -.
DR EPD; P63087; -.
DR jPOST; P63087; -.
DR MaxQB; P63087; -.
DR PaxDb; P63087; -.
DR PeptideAtlas; P63087; -.
DR PRIDE; P63087; -.
DR ProteomicsDB; 289783; -. [P63087-1]
DR ProteomicsDB; 289784; -. [P63087-2]
DR Antibodypedia; 2879; 448 antibodies from 34 providers.
DR DNASU; 19047; -.
DR Ensembl; ENSMUST00000086294; ENSMUSP00000083474; ENSMUSG00000004455. [P63087-2]
DR Ensembl; ENSMUST00000102528; ENSMUSP00000099587; ENSMUSG00000004455. [P63087-1]
DR GeneID; 19047; -.
DR KEGG; mmu:19047; -.
DR UCSC; uc008zks.1; mouse. [P63087-1]
DR UCSC; uc008zkt.1; mouse. [P63087-2]
DR CTD; 5501; -.
DR MGI; MGI:104872; Ppp1cc.
DR VEuPathDB; HostDB:ENSMUSG00000004455; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000153472; -.
DR InParanoid; P63087; -.
DR OMA; EEHEIRY; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P63087; -.
DR TreeFam; TF354243; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 19047; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Ppp1cc; mouse.
DR PRO; PR:P63087; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P63087; protein.
DR Bgee; ENSMUSG00000004455; Expressed in retinal neural layer and 72 other tissues.
DR ExpressionAtlas; P63087; baseline and differential.
DR Genevisible; P63087; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
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:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030182; P:neuron differentiation; ISS:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
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 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Carbohydrate metabolism; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycogen metabolism;
KW Hydrolase; Kinetochore; Manganese; Metal-binding; Mitochondrion; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT CHAIN 2..323
FT /note="Serine/threonine-protein phosphatase PP1-gamma
FT catalytic subunit"
FT /id="PRO_0000058788"
FT REGION 302..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT MOD_RES 307
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT VAR_SEQ 315..323
FT /note="GMITKQAKK -> VGSGLNPSIQKASNYRNNTVLYE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2544298,
FT ECO:0000303|PubMed:9339378"
FT /id="VSP_005095"
FT CONFLICT 316..317
FT /note="MI -> IV (in Ref. 2; AAC53383/AAC53384 and 3;
FT BAA19729)"
FT /evidence="ECO:0000305"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:4V0W"
FT TURN 18..21
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:4V0W"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:4V0W"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:4V0W"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4V0W"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4V0W"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:4V0W"
SQ SEQUENCE 323 AA; 36984 MW; 4E28412C16898615 CRC64;
MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
KKKPNATRPV TPPRGMITKQ AKK
