PP1G_CANLF
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 03-AUG-2022, entry version 114.
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). {ECO:0000250|UniProtKB:P36873,
CC 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";
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DR EMBL; AF525130; AAM88379.1; -; mRNA.
DR RefSeq; NP_001003033.1; NM_001003033.1.
DR AlphaFoldDB; Q8MJ46; -.
DR SMR; Q8MJ46; -.
DR STRING; 9612.ENSCAFP00000030520; -.
DR PaxDb; Q8MJ46; -.
DR GeneID; 403557; -.
DR KEGG; cfa:403557; -.
DR CTD; 5501; -.
DR eggNOG; KOG0374; Eukaryota.
DR InParanoid; Q8MJ46; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
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:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
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 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 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
