LOCUS       NP_071943                323 aa            linear   ROD 09-FEB-2025
DEFINITION  serine/threonine-protein phosphatase PP1-gamma catalytic subunit
            isoform 1 [Rattus norvegicus].
ACCESSION   NP_071943 XP_346436
VERSION     NP_071943.1
DBSOURCE    REFSEQ: accession NM_022498.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Liu,X., Huang,S., Liu,C., Liu,X., Shen,Y. and Cui,Z.
  TITLE     PPP1CC is associated with astrocyte and microglia proliferation
            after traumatic spinal cord injury in rats
  JOURNAL   Pathol Res Pract 213 (11), 1355-1364 (2017)
   PUBMED   29033188
  REMARK    GeneRIF: that PPP1CC promoted astrocyte and microglia proliferation
            after inflammation
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Buren,S., Gomes,A.L., Teijeiro,A., Fawal,M.A., Yilmaz,M.,
            Tummala,K.S., Perez,M., Rodriguez-Justo,M., Campos-Olivas,R.,
            Megias,D. and Djouder,N.
  TITLE     Regulation of OGT by URI in Response to Glucose Confers
            c-MYC-Dependent Survival Mechanisms
  JOURNAL   Cancer Cell 30 (2), 290-307 (2016)
   PUBMED   27505673
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Hafver,T.L., Hodne,K., Wanichawan,P., Aronsen,J.M., Dalhus,B.,
            Lunde,P.K., Lunde,M., Martinsen,M., Enger,U.H., Fuller,W.,
            Sjaastad,I., Louch,W.E., Sejersted,O.M. and Carlson,C.R.
  TITLE     Protein Phosphatase 1c Associated with the Cardiac Sodium Calcium
            Exchanger 1 Regulates Its Activity by Dephosphorylating Serine
            68-phosphorylated Phospholemman
  JOURNAL   J Biol Chem 291 (9), 4561-4579 (2016)
   PUBMED   26668322
  REMARK    GeneRIF: Data suggest that Ncx1 (sodium-calcium exchanger 1) is
            substrate-specifying Pp1c regulator protein, regulating Ncx1
            activity via Ser-68-phospholemman (Plm) dephosphorylation in
            cardiomyocytes; Plm/Ncx1/Pp1c complex is up-regulated in heart
            failure.
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Santos,M., Rebelo,S., Van Kleeff,P.J., Kim,C.E., Dauer,W.T.,
            Fardilha,M., da Cruz E Silva,O.A. and da Cruz E Silva,E.F.
  TITLE     The nuclear envelope protein, LAP1B, is a novel protein phosphatase
            1 substrate
  JOURNAL   PLoS One 8 (10), e76788 (2013)
   PUBMED   24116158
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Allen,P.B., Ouimet,C.C. and Greengard,P.
  TITLE     Spinophilin, a novel protein phosphatase 1 binding protein
            localized to dendritic spines
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9956-9961 (1997)
   PUBMED   9275233
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Ouimet,C.C., da Cruz e Silva,E.F. and Greengard,P.
  TITLE     The alpha and gamma 1 isoforms of protein phosphatase 1 are highly
            and specifically concentrated in dendritic spines
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3396-3400 (1995)
   PUBMED   7724573
REFERENCE   8  (residues 1 to 323)
  AUTHORS   .
  TITLE     Identification of members of the protein phosphatase 1 gene family
            in the rat and enhanced expression of protein phosphatase 1 alpha
            gene in rat hepatocellular carcinomas
  JOURNAL   Jpn J Cancer Res 82 (7), 873 (1991)
   PUBMED   1653777
  REMARK    Correction to:[Jpn J Cancer Res. 1990 Dec;81(12):1272-80. doi:
            10.1111/j.1349-7006.1990.tb02690.x.. PMID: 2177460]
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Wadzinski,B.E., Heasley,L.E. and Johnson,G.L.
  TITLE     Multiplicity of protein serine-threonine phosphatases in PC12
            pheochromocytoma and FTO-2B hepatoma cells
  JOURNAL   J Biol Chem 265 (35), 21504-21508 (1990)
   PUBMED   2174876
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Sasaki,K., Shima,H., Kitagawa,Y., Irino,S., Sugimura,T. and
            Nagao,M.
  TITLE     Identification of members of the protein phosphatase 1 gene family
            in the rat and enhanced expression of protein phosphatase 1 alpha
            gene in rat hepatocellular carcinomas
  JOURNAL   Jpn J Cancer Res 81 (12), 1272-1280 (1990)
   PUBMED   2177460
  REMARK    Erratum:[Jpn J Cancer Res. 1991 Jul;82(7):873.. PMID: 1653777]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CB740494.1, FN803249.1, FM122849.1, FM102812.1 and DV727747.1.
            
            On May 3, 2006 this sequence version replaced XP_346436.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the shorter protein (isoform 1).
            
            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##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760389 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="12"
                     /map="12q16"
     Protein         1..323
                     /product="serine/threonine-protein phosphatase PP1-gamma
                     catalytic subunit isoform 1"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase PP1-gamma
                     catalytic subunit; protein serine-threonine phosphatase
                     catalytic subunit PP-1b; protein phosphatase 1C catalytic
                     subunit; protein phosphatase 1, catalytic subunit, gamma
                     isozyme"
                     /calculated_mol_wt=36853
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P36873; propagated from
                     UniProtKB/Swiss-Prot (P63088.1)"
     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            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"
     Region          302..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63088.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P36873; propagated from
                     UniProtKB/Swiss-Prot (P63088.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P36873; propagated from
                     UniProtKB/Swiss-Prot (P63088.1)"
     CDS             1..323
                     /gene="Ppp1cc"
                     /gene_synonym="PP-1G; Ppp1cc1"
                     /coded_by="NM_022498.2:254..1225"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24669"
                     /db_xref="RGD:3377"
ORIGIN      
        1 madidklnid siiqrllevr gskpgknvql qeneirglcl ksreiflsqp illeleaplk
       61 icgdihgqyy dllrlfeygg fppesnylfl gdyvdrgkqs leticlllay kikypenffl
      121 lrgnhecasi nriygfydec krryniklwk tftdcfnclp iaaivdekif cchgglspdl
      181 qsmeqirrim rptdvpdqgl lcdllwsdpd kdvlgwgend rgvsftfgae vvakflhkhd
      241 ldlicrahqv vedgyeffak rqlvtlfsap nycgefdnag ammsvdetlm csfqilkpae
      301 kkkpnatrpv tpprgmitkq akk
//
