LOCUS       NP_114074                330 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein phosphatase PP1-alpha catalytic subunit
            [Mus musculus].
ACCESSION   NP_114074
VERSION     NP_114074.1
DBSOURCE    REFSEQ: accession NM_031868.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Zhang,L., Jiao,G., You,Y., Li,X., Liu,J., Sun,Z., Li,Q., Dai,Z.,
            Ma,J., Zhou,H., Li,G., Meng,C. and Chen,Y.
  TITLE     Arginine methylation of PPP1CA by CARM1 regulates glucose
            metabolism and affects osteogenic differentiation and osteoclastic
            differentiation
  JOURNAL   Clin Transl Med 13 (9), e1369 (2023)
   PUBMED   37649137
  REMARK    GeneRIF: Arginine methylation of PPP1CA by CARM1 regulates glucose
            metabolism and affects osteogenic differentiation and osteoclastic
            differentiation.
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Park,E.J., Kim,H.S., Lee,D.H., Kim,S.M., Yoon,J.S., Lee,J.M.,
            Im,S.J., Lee,H., Lee,M.W. and Lee,C.W.
  TITLE     Ssu72 phosphatase is essential for thermogenic adaptation by
            regulating cytosolic translation
  JOURNAL   Nat Commun 14 (1), 1097 (2023)
   PUBMED   36841836
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Wang,N., Langfelder,P., Stricos,M., Ramanathan,L., Richman,J.B.,
            Vaca,R., Plascencia,M., Gu,X., Zhang,S., Tamai,T.K., Zhang,L.,
            Gao,F., Ouk,K., Lu,X., Ivanov,L.V., Vogt,T.F., Lu,Q.R.,
            Morton,A.J., Colwell,C.S., Aaronson,J.S., Rosinski,J., Horvath,S.
            and Yang,X.W.
  TITLE     Mapping brain gene coexpression in daytime transcriptomes unveils
            diurnal molecular networks and deciphers perturbation gene
            signatures
  JOURNAL   Neuron 110 (20), 3318-3338 (2022)
   PUBMED   36265442
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Chen,Y., Che,M., Li,C., Li,Y., Zhang,T., Li,X. and Sun,C.
  TITLE     PP1A prevents ROS-induced pyroptosis by inhibiting MAPK/caspase-3
            in mouse adipose tissue
  JOURNAL   FEBS J 289 (13), 3839-3853 (2022)
   PUBMED   35080339
  REMARK    GeneRIF: PP1A prevents ROS-induced pyroptosis by inhibiting
            MAPK/caspase-3 in mouse adipose tissue.
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Smith,G.D., Sadhu,A., Mathies,S. and Wolf,D.P.
  TITLE     Characterization of protein phosphatases in mouse oocytes
  JOURNAL   Dev Biol 204 (2), 537-549 (1998)
   PUBMED   9882488
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Fernandes,M., Lespinasse,F., Rotomondo,F., Poirier,C., Guenet,J.L.,
            Gaudray,P. and Carle,G.F.
  TITLE     Comparative mapping of two adjacent regions of MMU19 with their
            human counterpart on HSA11q13
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 237-246 (1998)
   PUBMED   9730611
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Saadat,M., Mizuno,Y., Kikuchi,K. and Yoshida,M.C.
  TITLE     Comparative mapping of the gene encoding the catalytic subunit of
            protein phosphatase type 1 alpha (PPP1CA) to human, rat, and mouse
            chromosomes
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 55-57 (1995)
   PUBMED   7736790
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Saadat,M., Kakinoki,Y., Mizuno,Y., Kikuchi,K. and Yoshida,M.C.
  TITLE     Chromosomal localization of human, rat, and mouse protein
            phosphatase type 1 beta catalytic subunit genes (PPP1CB) by
            fluorescence in situ hybridization
  JOURNAL   Jpn J Genet 69 (6), 697-700 (1994)
   PUBMED   7857673
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Becker,W., Kentrup,H., Klumpp,S., Schultz,J.E. and Joost,H.G.
  TITLE     Molecular cloning of a protein serine/threonine phosphatase
            containing a putative regulatory tetratricopeptide repeat domain
  JOURNAL   J Biol Chem 269 (36), 22586-22592 (1994)
   PUBMED   8077208
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AC140073.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK167244.1, AK167981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="19"
                     /map="19 3.89 cM"
     Protein         1..330
                     /product="serine/threonine-protein phosphatase PP1-alpha
                     catalytic subunit"
                     /EC_number="3.1.3.16"
                     /note="PP-1A"
                     /calculated_mol_wt=37409
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Region          8..298
                     /region_name="MPP_PP1_PPKL"
                     /note="PP1, PPKL (PP1 and kelch-like) enzymes, and related
                     proteins, metallophosphatase domain; cd07414"
                     /db_xref="CDD:277359"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Site            order(64,66,92,96,124..125,129..130,134,173,195..197,206,
                     220..222,248,272..276)
                     /site_type="active"
                     /db_xref="CDD:277359"
     Site            order(64,66,92,124,173,248)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277359"
     Site            order(96,129..130,134,195..197,206,220..222,272..276)
                     /site_type="other"
                     /note="natural toxin binding site [chemical binding]"
                     /db_xref="CDD:277359"
     Site            order(179,181,198,203,216,225,233..234,236..238,240..242,
                     257,261,288..289,291,293,295)
                     /site_type="other"
                     /note="MYPT1 binding site [polypeptide binding]"
                     /db_xref="CDD:277359"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Region          306..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62137.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62136; propagated from
                     UniProtKB/Swiss-Prot (P62137.1)"
     CDS             1..330
                     /gene="Ppp1ca"
                     /gene_synonym="dism2; Ppp1c"
                     /coded_by="NM_031868.2:44..1036"
                     /db_xref="CCDS:CCDS29421.1"
                     /db_xref="GeneID:19045"
                     /db_xref="MGI:MGI:103016"
ORIGIN      
        1 msdseklnld siigrllevq gsrpgknvql teneirglcl ksreiflsqp illeleaplk
       61 icgdihgqyy dllrlfeygg fppesnylfl gdyvdrgkqs leticlllay kirypenffl
      121 lrgnhecasi nriygfydec krryniklwk tftdcfnclp iaaivdekif cchgglspdl
      181 qsmeqirrim rptdvpdqgl lcdllwsdpd kdvqgwgend rgvsftfgae vvakflhkhd
      241 ldlicrahqv vedgyeffak rqlvtlfsap nycgefdnag ammsvdetlm csfqilkpad
      301 knkgkygqfs glnpggrpit pprnsakakk
//
