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Protein phosphatase 1 regulatory subunit 3C (Protein phosphatase 1 regulatory subunit 5) (PP1 subunit R5) (Protein targeting to glycogen) (PTG)

 PPR3C_MOUSE             Reviewed;         317 AA.
Q7TMB3; O08541; Q8BJW8;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
22-NOV-2017, entry version 88.
RecName: Full=Protein phosphatase 1 regulatory subunit 3C;
AltName: Full=Protein phosphatase 1 regulatory subunit 5;
Short=PP1 subunit R5;
AltName: Full=Protein targeting to glycogen;
Short=PTG;
Name=Ppp1r3c {ECO:0000312|MGI:MGI:1858229};
Synonyms=Ppp1r5 {ECO:0000250|UniProtKB:Q9UQK1};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAH52769.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52769.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH54739.1}, and
Olfactory epithelium {ECO:0000312|EMBL:AAH52769.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2] {ECO:0000305, ECO:0000312|EMBL:AAB49689.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 9-317, FUNCTION, ASSOCIATION WITH
GLYCOGEN, AND INTERACTION WITH PPP1CC.
PubMed=9045612; DOI=10.1126/science.275.5305.1475;
Printen J.A., Brady M.J., Saltiel A.R.;
"PTG, a protein phosphatase 1-binding protein with a role in glycogen
metabolism.";
Science 275:1475-1478(1997).
[3] {ECO:0000305, ECO:0000312|EMBL:BAC37313.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-317.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37313.1};
TISSUE=Muellerian duct {ECO:0000312|EMBL:BAC37313.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4] {ECO:0000305}
FUNCTION.
PubMed=9242697; DOI=10.1074/jbc.272.32.20198;
Brady M.J., Printen J.A., Mastick C.C., Saltiel A.R.;
"Role of protein targeting to glycogen (PTG) in the regulation of
protein phosphatase-1 activity.";
J. Biol. Chem. 272:20198-20204(1997).
[5] {ECO:0000305}
FUNCTION.
PubMed=9756875; DOI=10.1074/jbc.273.41.26421;
Berman H.K., O'Doherty R.M., Anderson P., Newgard C.B.;
"Overexpression of protein targeting to glycogen (PTG) in rat
hepatocytes causes profound activation of glycogen synthesis
independent of normal hormone- and substrate-mediated regulatory
mechanisms.";
J. Biol. Chem. 273:26421-26425(1998).
[6] {ECO:0000305}
FUNCTION.
PubMed=10862764; DOI=10.1074/jbc.M002427200;
Gasa R., Jensen P.B., Berman H.K., Brady M.J., DePaoli-Roach A.A.,
Newgard C.B.;
"Distinctive regulatory and metabolic properties of glycogen-targeting
subunits of protein phosphatase-1 (PTG, GL, GM/RGl) expressed in
hepatocytes.";
J. Biol. Chem. 275:26396-26403(2000).
[7] {ECO:0000305}
MUTAGENESIS OF VAL-85; PHE-87; ASP-247 AND GLU-250.
PubMed=10938087; DOI=10.1074/jbc.M005541200;
Fong N.M., Jensen T.C., Shah A.S., Parekh N.N., Saltiel A.R.,
Brady M.J.;
"Identification of binding sites on protein targeting to glycogen for
enzymes of glycogen metabolism.";
J. Biol. Chem. 275:35034-35039(2000).
[8] {ECO:0000305}
FUNCTION.
PubMed=10998419; DOI=10.1074/jbc.M006251200;
Lerin C., Montell E., Berman H.K., Newgard C.B., Gomez-Foix A.M.;
"Overexpression of protein targeting to glycogen in cultured human
muscle cells stimulates glycogen synthesis independent of glycogen and
glucose 6-phosphate levels.";
J. Biol. Chem. 275:39991-39995(2000).
[9] {ECO:0000305}
FUNCTION.
PubMed=10683377; DOI=10.1172/JCI8673;
O'Doherty R.M., Jensen P.B., Anderson P., Jones J.G., Berman H.K.,
Kearney D., Newgard C.B.;
"Activation of direct and indirect pathways of glycogen synthesis by
hepatic overexpression of protein targeting to glycogen.";
J. Clin. Invest. 105:479-488(2000).
[10] {ECO:0000305}
FUNCTION.
PubMed=12805359; DOI=10.1074/jbc.M303846200;
Greenberg C.C., Meredith K.N., Yan L., Brady M.J.;
"Protein targeting to glycogen overexpression results in the specific
enhancement of glycogen storage in 3T3-L1 adipocytes.";
J. Biol. Chem. 278:30835-30842(2003).
[11] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12727934; DOI=10.1172/JCI17975;
Crosson S.M., Khan A., Printen J., Pessin J.E., Saltiel A.R.;
"PTG gene deletion causes impaired glycogen synthesis and
developmental insulin resistance.";
J. Clin. Invest. 111:1423-1432(2003).
[12] {ECO:0000305}
FUNCTION.
PubMed=15322104; DOI=10.1074/jbc.M405660200;
Green A.R., Aiston S., Greenberg C.C., Freeman S., Poucher S.M.,
Brady M.J., Agius L.;
"The glycogenic action of protein targeting to glycogen in hepatocytes
involves multiple mechanisms including phosphorylase inactivation and
glycogen synthase translocation.";
J. Biol. Chem. 279:46474-46482(2004).
[13] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16354703; DOI=10.1128/MCB.26.1.334-342.2006;
Greenberg C.C., Danos A.M., Brady M.J.;
"Central role for protein targeting to glycogen in the maintenance of
cellular glycogen stores in 3T3-L1 adipocytes.";
Mol. Cell. Biol. 26:334-342(2006).
-!- FUNCTION: Acts as a glycogen-targeting subunit for PP1 and
regulates its activity. Activates glycogen synthase, reduces
glycogen phosphorylase activity and limits glycogen breakdown.
Dramatically increases basal and insulin-stimulated glycogen
synthesis upon overexpression in a variety of cell types.
{ECO:0000269|PubMed:10683377, ECO:0000269|PubMed:10862764,
ECO:0000269|PubMed:10998419, ECO:0000269|PubMed:12727934,
ECO:0000269|PubMed:12805359, ECO:0000269|PubMed:15322104,
ECO:0000269|PubMed:16354703, ECO:0000269|PubMed:9045612,
ECO:0000269|PubMed:9242697, ECO:0000269|PubMed:9756875}.
-!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1 and
associates with glycogen. Forms complexes with glycogen
phosphorylase, glycogen synthase and phosphorylase kinase which is
necessary for its regulation of PP1 activity. Also interacts with
EPM2A/laforin. {ECO:0000250|UniProtKB:Q9UQK1,
ECO:0000269|PubMed:9045612}.
-!- DOMAIN: The N-terminal region is required for binding to PP1, the
central region is required for binding to glycogen and the C-
terminal region is required for binding to glycogen phosphorylase,
glycogen synthase and phosphorylase kinase.
{ECO:0000269|PubMed:10938087}.
-!- PTM: Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent
manner. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display embryonic lethality when
homozygous. Heterozygotes display decreased protein levels,
decreased glycogen accumulation and glycogen synthase activity,
reduced insulin-stimulated glycogen synthesis and progressive age-
dependent glucose intolerance. When Ppp1r3c is silenced in adults,
they display decreased PP1 activity and glycogen accumulation,
increased phosphorylation of glycogen phosphorylase, increased
GLUT1 levels, increased glucose uptake and increased glycogen
degradation. {ECO:0000269|PubMed:12727934,
ECO:0000269|PubMed:16354703}.
-!- SEQUENCE CAUTION:
Sequence=AAB49689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; BC052769; AAH52769.1; -; mRNA.
EMBL; BC054739; AAH54739.1; -; mRNA.
EMBL; U89924; AAB49689.1; ALT_INIT; mRNA.
EMBL; AK078506; BAC37313.1; -; mRNA.
CCDS; CCDS37968.1; -.
RefSeq; NP_058550.1; NM_016854.2.
UniGene; Mm.24724; -.
ProteinModelPortal; Q7TMB3; -.
SMR; Q7TMB3; -.
STRING; 10090.ENSMUSP00000084578; -.
CAZy; CBM21; Carbohydrate-Binding Module Family 21.
iPTMnet; Q7TMB3; -.
PhosphoSitePlus; Q7TMB3; -.
MaxQB; Q7TMB3; -.
PaxDb; Q7TMB3; -.
PRIDE; Q7TMB3; -.
Ensembl; ENSMUST00000087321; ENSMUSP00000084578; ENSMUSG00000067279.
GeneID; 53412; -.
KEGG; mmu:53412; -.
UCSC; uc008hhs.1; mouse.
CTD; 5507; -.
MGI; MGI:1858229; Ppp1r3c.
eggNOG; KOG3986; Eukaryota.
eggNOG; ENOG4111FT1; LUCA.
GeneTree; ENSGT00530000062978; -.
HOGENOM; HOG000026799; -.
HOVERGEN; HBG052744; -.
InParanoid; Q7TMB3; -.
KO; K07189; -.
OMA; MRICLAH; -.
OrthoDB; EOG091G0GB5; -.
PhylomeDB; Q7TMB3; -.
TreeFam; TF105537; -.
Reactome; R-MMU-3322077; Glycogen synthesis.
PRO; PR:Q7TMB3; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000067279; -.
Genevisible; Q7TMB3; MM.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
GO; GO:0005977; P:glycogen metabolic process; IDA:MGI.
GO; GO:0006605; P:protein targeting; TAS:MGI.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR005036; CBM21_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR017434; Pase-1_reg-su_3B/C/D_met.
InterPro; IPR030683; PP1_3C.
PANTHER; PTHR12307:SF15; PTHR12307:SF15; 1.
Pfam; PF03370; CBM_21; 1.
PIRSF; PIRSF038207; PP1_GT_animal; 1.
PIRSF; PIRSF500813; PP1_PTG; 1.
PROSITE; PS51159; CBM21; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Glycogen metabolism;
Reference proteome; Ubl conjugation.
CHAIN 1 317 Protein phosphatase 1 regulatory subunit
3C.
/FTId=PRO_0000285928.
DOMAIN 149 257 CBM21. {ECO:0000255|PROSITE-
ProRule:PRU00491}.
REGION 141 263 Interaction with EPM2A.
{ECO:0000250|UniProtKB:Q9UQK1}.
MOTIF 84 87 PP1-binding motif.
MUTAGEN 85 85 V->A: Abolishes binding to PP1 but has no
effect on binding to glycogen synthase,
glycogen phosphorylase or glycogen; when
associated with A-87.
{ECO:0000269|PubMed:10938087}.
MUTAGEN 87 87 F->A: Abolishes binding to PP1 but has no
effect on binding to glycogen synthase,
glycogen phosphorylase or glycogen; when
associated with A-85.
{ECO:0000269|PubMed:10938087}.
MUTAGEN 247 247 D->A: Abolishes binding to glycogen
synthase and glycogen phosphorylase but
has no effect on binding to PP1 or
glycogen; when associated with A-250.
{ECO:0000269|PubMed:10938087}.
MUTAGEN 250 250 E->A: Abolishes binding to glycogen
synthase and glycogen phosphorylase but
has no effect on binding to PP1 or
glycogen; when associated with A-247.
{ECO:0000269|PubMed:10938087}.
CONFLICT 165 165 Q -> E (in Ref. 2; AAB49689).
{ECO:0000305}.
SEQUENCE 317 AA; 36460 MW; 8DC8941B733649D6 CRC64;
MSCTRMIHVL DPRPLTSSVM PVDMAMRICL AHSPPLKSFL GPYNGFQRRN FVNKLKPLKP
CLSVKQEAKS QSEWKSPHNQ AKKRVVFADS KGLSLTAIHV FSDLPEEPAW DLQFDLLDLN
DISSSLKLHE EKNLVFDFPQ PSTDYLSFRD RFQKNFVCLE NCSLQDRTVT GTVKVKNVSF
EKKVQVRITF DTWKTYTDVD CVYMKNVYSS SDSDTFSFAI DLPRVIPTEE KIEFCISYHA
NGRIFWDNNE GQNYRIVHVQ WKPDGVQTQV APKDCAFQQG PPKTEIEPTV FGSPRLASGL
FPEWQSWGRV ENLTSYR


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