ID   PP14C_RAT               Reviewed;         164 AA.
AC   Q8R4R9;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 14C;
DE   AltName: Full=Kinase-enhanced PP1 inhibitor;
DE   AltName: Full=PKC-potentiated PP1 inhibitory protein;
GN   Name=Ppp1r14c; Synonyms=Kepi;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=11812771; DOI=10.1074/jbc.m107558200;
RA   Liu Q.-R., Zhang P.-W., Zhen Q., Walther D., Wang X.-B., Uhl G.;
RT   "KEPI, a PKC-dependent protein phosphatase 1 inhibitor regulated by
RT   morphine.";
RL   J. Biol. Chem. 277:13312-13320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 35-44, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Inhibitor of the PP1 regulatory subunit PPP1CA.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Has over 600-fold higher inhibitory activity when phosphorylated,
CC       creating a molecular switch for regulating the phosphorylation status
CC       of PPP1CA substrates and smooth muscle contraction. The main inhibitory
CC       site appears to be Thr-72 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
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DR   EMBL; AF407168; AAL83509.1; -; mRNA.
DR   EMBL; BC086978; AAH86978.1; -; mRNA.
DR   RefSeq; NP_596916.1; NM_133425.3.
DR   AlphaFoldDB; Q8R4R9; -.
DR   STRING; 10116.ENSRNOP00000022046; -.
DR   iPTMnet; Q8R4R9; -.
DR   PhosphoSitePlus; Q8R4R9; -.
DR   jPOST; Q8R4R9; -.
DR   PaxDb; Q8R4R9; -.
DR   PRIDE; Q8R4R9; -.
DR   Ensembl; ENSRNOT00000022046; ENSRNOP00000022046; ENSRNOG00000016368.
DR   GeneID; 171010; -.
DR   KEGG; rno:171010; -.
DR   UCSC; RGD:620538; rat.
DR   CTD; 81706; -.
DR   RGD; 620538; Ppp1r14c.
DR   eggNOG; ENOG502RYQF; Eukaryota.
DR   GeneTree; ENSGT00950000182985; -.
DR   HOGENOM; CLU_114155_1_0_1; -.
DR   InParanoid; Q8R4R9; -.
DR   OMA; KPSHPAM; -.
DR   OrthoDB; 1492626at2759; -.
DR   PhylomeDB; Q8R4R9; -.
DR   TreeFam; TF105546; -.
DR   PRO; PR:Q8R4R9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000016368; Expressed in heart and 16 other tissues.
DR   Genevisible; Q8R4R9; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:RGD.
DR   GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR   Gene3D; 1.10.150.220; -; 1.
DR   InterPro; IPR008025; CPI-17.
DR   InterPro; IPR036658; CPI-17_sf.
DR   PANTHER; PTHR16188; PTHR16188; 1.
DR   Pfam; PF05361; PP1_inhibitor; 1.
DR   SUPFAM; SSF81790; SSF81790; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Methylation;
KW   Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAE6"
FT   CHAIN           2..164
FT                   /note="Protein phosphatase 1 regulatory subunit 14C"
FT                   /id="PRO_0000071496"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAE6"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         27
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R4S0"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAE6"
FT   MOD_RES         72
FT                   /note="Phosphothreonine; by ILK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TAE6"
SQ   SEQUENCE   164 AA;  17980 MW;  2E48BCB85446A4DE CRC64;
     MSVVTGGGEA AGGTSGGGAR VFFQSPRGGT GGSRESSSHS GSSREDSAPV ATVAAAGQVQ
     QQQRRHQQGK VTVKYDRKEL RKRLVLEEWI VEQLGQLYGC EEEEMPDVEI DIDDLLDADS
     EEERASKLQE ALVDCYKPTE EFIRELLSRI RGMRKLSPPQ KKSV