ID   PPR3C_RAT               Reviewed;         317 AA.
AC   Q5U2R5;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3C;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 5;
DE            Short=PP1 subunit R5;
DE   AltName: Full=Protein targeting to glycogen;
DE            Short=PTG;
GN   Name=Ppp1r3c {ECO:0000312|EMBL:AAH85894.1};
GN   Synonyms=Ppp1r5 {ECO:0000250|UniProtKB:Q7TMB3};
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] {ECO:0000312|EMBL:AAH85894.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart {ECO:0000312|EMBL:AAH85894.1};
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).
CC   -!- FUNCTION: Acts as a glycogen-targeting subunit for PP1 and regulates
CC       its activity. Activates glycogen synthase, reduces glycogen
CC       phosphorylase activity and limits glycogen breakdown. Dramatically
CC       increases basal and insulin-stimulated glycogen synthesis upon
CC       overexpression in a variety of cell types (By similarity).
CC       {ECO:0000250|UniProtKB:Q7TMB3}.
CC   -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1 and associates
CC       with glycogen. Forms complexes with glycogen phosphorylase, glycogen
CC       synthase and phosphorylase kinase which is necessary for its regulation
CC       of PP1 activity. Also interacts with EPM2A/laforin (By similarity).
CC       {ECO:0000250|UniProtKB:Q7TMB3, ECO:0000250|UniProtKB:Q9UQK1}.
CC   -!- DOMAIN: The N-terminal region is required for binding to PP1, the
CC       central region is required for binding to glycogen and the C-terminal
CC       region is required for binding to glycogen phosphorylase, glycogen
CC       synthase and phosphorylase kinase. {ECO:0000250|UniProtKB:Q7TMB3}.
CC   -!- PTM: Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent manner.
CC       {ECO:0000250}.
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DR   EMBL; BC085894; AAH85894.1; -; mRNA.
DR   RefSeq; NP_001012072.1; NM_001012072.1.
DR   AlphaFoldDB; Q5U2R5; -.
DR   SMR; Q5U2R5; -.
DR   STRING; 10116.ENSRNOP00000024941; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   iPTMnet; Q5U2R5; -.
DR   PhosphoSitePlus; Q5U2R5; -.
DR   PaxDb; Q5U2R5; -.
DR   GeneID; 309513; -.
DR   KEGG; rno:309513; -.
DR   UCSC; RGD:1309132; rat.
DR   CTD; 5507; -.
DR   RGD; 1309132; Ppp1r3c.
DR   eggNOG; KOG3986; Eukaryota.
DR   InParanoid; Q5U2R5; -.
DR   OrthoDB; 1232750at2759; -.
DR   PhylomeDB; Q5U2R5; -.
DR   Reactome; R-RNO-3322077; Glycogen synthesis.
DR   PRO; PR:Q5U2R5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0042587; C:glycogen granule; IDA:RGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR   GO; GO:0050196; F:[phosphorylase] phosphatase activity; IMP:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IMP:RGD.
DR   GO; GO:2001069; F:glycogen binding; ISO:RGD.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0005977; P:glycogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IDA:RGD.
DR   GO; GO:0005981; P:regulation of glycogen catabolic process; IDA:RGD.
DR   Gene3D; 2.60.40.2440; -; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   InterPro; IPR017434; Pase-1_reg-su_3B/C/D_met.
DR   InterPro; IPR030683; PP1_3C.
DR   PANTHER; PTHR12307:SF15; PTHR12307:SF15; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR   PIRSF; PIRSF500813; PP1_PTG; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycogen metabolism; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..317
FT                   /note="Protein phosphatase 1 regulatory subunit 3C"
FT                   /id="PRO_0000285929"
FT   DOMAIN          149..257
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          141..263
FT                   /note="Interaction with EPM2A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQK1"
FT   MOTIF           84..87
FT                   /note="PP1-binding motif"
SQ   SEQUENCE   317 AA;  36413 MW;  6B73930ED3537F5F CRC64;
     MSCTRMIHVL DPRPLTSSVM PVDMAMRICL AHSPPLKSFL GPYNGLQRRH FVNKPKPLKP
     CLSVKQEAKS QKEWKSPHSQ AKKRVVFADS KGLSLTAIHV FSDLPEEPAW DLQFDLLDLN
     DISSSLKLHE EKNLVFDFPQ PSSDYLSFRD RFQKNFVCLE NCSLQDRTVT GTVKVKNVSF
     EKKVQVRITF DTWKTYTDVD CVYLKNVYGS SDSDTFSFAI DLPRVIPTEE KIEFCISYHA
     NGRVFWDNNE AQNYRIVHVQ WKPDGVQTQV APKDCAFQQV PLKTELEPTV FGSPRLASGL
     FPEWQSWGRV ENLASYR