ID   PP1G_CANLF              Reviewed;         323 AA.
AC   Q8MJ46;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 121.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Mishra S., Tiwari N., Rastogi S., Sabbah H.N., Gupta R.C.;
RT   "Cloning and sequencing of catalytic subunit of protein phosphatase 1 gamma
RT   isoform from dog heart.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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. PPP1R15A
CC       and PPP1R15B mediate binding to EIF2S1. Part of a complex containing
CC       PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R3B, PPP1R7 and CDCA2.
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 PPP1R42; the interaction is direct. Interacts with
CC       URI1; the interaction is phosphorylation-dependent and occurs in a
CC       growth factor-dependent manner. Interacts with FOXP3. Interacts with
CC       TMEM225 (via RVxF motif). Interacts with MKI67. Interacts with RRP1B;
CC       this targets PPP1CC to the nucleolus (By similarity). Interacts with
CC       DYNLT4 (By similarity). Interacts (via RVxF motif) with FIRRM;
CC       regulates PLK1 kinase activity (By similarity).
CC       {ECO:0000250|UniProtKB:P36873, ECO:0000250|UniProtKB:P63087}.
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. Colocalizes with URI1 at
CC       mitochondrion. Rapidly exchanges between the nucleolar, nucleoplasmic
CC       and cytoplasmic compartments. Highly mobile in cells and can be
CC       relocalized through interaction with targeting subunits. In the
CC       presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles.
CC       Shows a dynamic targeting to specific sites throughout the cell cycle.
CC       Highly concentrated in nucleoli of interphase cells and localizes at
CC       kinetochores early in mitosis. Relocalization to chromosome-containing
CC       regions occurs at the transition from early to late anaphase. Also
CC       accumulates at the cleavage furrow and midbody by telophase.
CC       {ECO:0000250|UniProtKB:P36873, ECO:0000250|UniProtKB:P63087}.
CC   -!- PTM: Phosphorylated by NEK2. {ECO:0000250}.
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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF525130; AAM88379.1; -; mRNA.
DR   RefSeq; NP_001003033.1; NM_001003033.1.
DR   AlphaFoldDB; Q8MJ46; -.
DR   SMR; Q8MJ46; -.
DR   STRING; 9615.ENSCAFP00000030520; -.
DR   PaxDb; 9612-ENSCAFP00000030520; -.
DR   GeneID; 403557; -.
DR   KEGG; cfa:403557; -.
DR   CTD; 5501; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   InParanoid; Q8MJ46; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF204; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Carbohydrate metabolism; Cell cycle; Cell division;
KW   Centromere; Chromosome; Cytoplasm; Cytoskeleton; 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_0000058786"
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"
SQ   SEQUENCE   323 AA;  37015 MW;  8DD287FA615B2E41 CRC64;
     MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK
     ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
     LRGNHECVSI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
     QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGETD RGVSFTFGAE VVAKFLHKHD
     LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
     KKKPNATRPV TPLRGMITKQ AKK
//