PP14C_MOUSE
ID PP14C_MOUSE Reviewed; 164 AA.
AC Q8R4S0;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; 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 STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Inhibitor of the PP1 regulatory subunit PPP1CA.
CC {ECO:0000269|PubMed:11812771}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:11812771}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11812771}.
CC -!- TISSUE SPECIFICITY: Detected in heart, muscle, spinal cord,
CC hippocampus, hypothalamus, thalamus, midbrain, brain stem, cerebellum,
CC brain cortex and olfactory bulb. {ECO:0000269|PubMed:11812771}.
CC -!- INDUCTION: Up-regulated by morphine. {ECO:0000269|PubMed:11812771}.
CC -!- PTM: The main inhibitory site appears to be Thr-72 (By similarity). Has
CC over 600-fold higher inhibitory activity when phosphorylated, creating
CC a molecular switch for regulating the phosphorylation status of PPP1CA
CC substrates and smooth muscle contraction. {ECO:0000250,
CC ECO:0000269|PubMed:11812771}.
CC -!- SIMILARITY: Belongs to the PP1 inhibitor family. {ECO:0000305}.
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DR EMBL; AF407167; AAL83508.1; -; mRNA.
DR EMBL; AK085997; BAC39589.1; -; mRNA.
DR EMBL; BC055717; AAH55717.1; -; mRNA.
DR CCDS; CCDS56669.1; -.
DR RefSeq; NP_597844.1; NM_133485.2.
DR AlphaFoldDB; Q8R4S0; -.
DR STRING; 10090.ENSMUSP00000045110; -.
DR iPTMnet; Q8R4S0; -.
DR PhosphoSitePlus; Q8R4S0; -.
DR MaxQB; Q8R4S0; -.
DR PaxDb; Q8R4S0; -.
DR PeptideAtlas; Q8R4S0; -.
DR PRIDE; Q8R4S0; -.
DR ProteomicsDB; 289782; -.
DR Antibodypedia; 54632; 103 antibodies from 22 providers.
DR Ensembl; ENSMUST00000043374; ENSMUSP00000045110; ENSMUSG00000040653.
DR GeneID; 76142; -.
DR KEGG; mmu:76142; -.
DR UCSC; uc007ehq.1; mouse.
DR CTD; 81706; -.
DR MGI; MGI:1923392; Ppp1r14c.
DR VEuPathDB; HostDB:ENSMUSG00000040653; -.
DR eggNOG; ENOG502RYQF; Eukaryota.
DR GeneTree; ENSGT00950000182985; -.
DR HOGENOM; CLU_114155_1_0_1; -.
DR InParanoid; Q8R4S0; -.
DR OMA; KPSHPAM; -.
DR OrthoDB; 1492626at2759; -.
DR PhylomeDB; Q8R4S0; -.
DR TreeFam; TF105546; -.
DR BioGRID-ORCS; 76142; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r14c; mouse.
DR PRO; PR:Q8R4S0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R4S0; protein.
DR Bgee; ENSMUSG00000040653; Expressed in interventricular septum and 60 other tissues.
DR ExpressionAtlas; Q8R4S0; baseline and differential.
DR Genevisible; Q8R4S0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:MGI.
DR GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
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; Membrane; Methylation; Phosphoprotein;
KW 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_0000071495"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..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:0000250|UniProtKB:Q8TAE6"
FT MOD_RES 27
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
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; 17754 MW; 0919DEE0344B691B CRC64;
MSVVTGGGEA AGGGGGGGAR VFFQSPRGGT GGSPGSSSSS GSSREDSAPV TTVAAAGQVQ
QQQRRHQQGK VTVKYDRKEL RKRLVLEEWI VEQLGQLYGC EEEEMPDVEI DIDDLLDANS
EEERASKLQE ALVDCYKPTE EFIRELLSRI RGMRKLSPPQ KKSV
