PP1A_CANLF
ID PP1A_CANLF Reviewed; 330 AA.
AC Q8WMS6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
DE Short=PP-1A;
DE EC=3.1.3.16;
GN Name=PPP1CA;
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., Sabbah H.N., Gupta R.C.;
RT "Cloning of catalytic subunit of protein phosphatase type 1 alpha from dog
RT heart.";
RL Submitted (NOV-2001) 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 Involved in regulation of ionic conductances and long-term synaptic
CC plasticity. May play an important role in dephosphorylating substrates
CC such as the postsynaptic density-associated Ca(2+)/calmodulin dependent
CC protein kinase II. Component of the PTW/PP1 phosphatase complex, which
CC plays a role in the control of chromatin structure and cell cycle
CC progression during the transition from mitosis into interphase.
CC Regulates NEK2 function in terms of kinase activity and centrosome
CC number and splitting, both in the presence and absence of radiation-
CC induced DNA damage. Regulator of neural tube and optic fissure closure,
CC and enteric neural crest cell (ENCCs) migration during development. In
CC balance with CSNK1D and CSNK1E, determines the circadian period length,
CC through the regulation of the speed and rhythmicity of PER1 and PER2
CC phosphorylation. May dephosphorylate CSNK1D and CSNK1E (By similarity).
CC Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139'
CC residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex,
CC thereby inhibiting autophagy (By similarity).
CC {ECO:0000250|UniProtKB:P62136, ECO:0000250|UniProtKB:P62137}.
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=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
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: 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 PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1.
CC Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with
CC PPP1R9A, PPP1R9B and PPP1R7. Interacts with YLPM1. Forms a complex with
CC ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and
CC PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the
CC presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex,
CC composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
CC Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the
CC presence of PPP1R10/PNUTS. Interacts with PPP1R39. transition from
CC mitosis into interphase. Interacts with TRIM28; the interaction
CC dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21
CC promoter site. Interacts with NEK2. Interacts with PHACTR4; which acts
CC as an activator of PP1 activity. Interacts with FER; this promotes
CC phosphorylation at Thr-320. Interacts with BTBD10. Interacts with
CC KCTD20. Interacts with FOXP3. Interacts with CENPA. Interacts with
CC ATG16L1. Found in a complex with PPP1CA, PPP1CC, SHC1 and PEAK1 (By
CC similarity). {ECO:0000250|UniProtKB:P62136,
CC ECO:0000250|UniProtKB:P62137, ECO:0000250|UniProtKB:P62139}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}.
CC Note=Primarily nuclear and largely excluded from the nucleolus. Highly
CC mobile in cells and can be relocalized through interaction with
CC targeting subunits. NOM1 plays a role in targeting this protein to the
CC nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to
CC nuclear speckles (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Dephosphorylated at Thr-320 in the presence of
CC ionizing radiation (By similarity). {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; AY062037; AAL38045.1; -; mRNA.
DR STRING; 9615.ENSCAFP00000017060; -.
DR InParanoid; Q8WMS6; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; 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:0016791; F:phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR037979; PPP1CA.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668:SF377; PTHR11668:SF377; 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; Biological rhythms; Carbohydrate metabolism; Cell cycle;
KW Cell division; Cytoplasm; Glycogen metabolism; Hydrolase; Manganese;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT CHAIN 2..330
FT /note="Serine/threonine-protein phosphatase PP1-alpha
FT catalytic subunit"
FT /id="PRO_0000058773"
FT REGION 306..330
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-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62137"
FT MOD_RES 306
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62137"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62136"
SQ SEQUENCE 330 AA; 37528 MW; DBD86501C5EEB71A CRC64;
MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDXFNXLP IAAIVDEKIF CCHGGLSPDL
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
