PPR3B_RAT
ID PPR3B_RAT Reviewed; 284 AA.
AC Q6IN01; Q63759;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3B;
DE AltName: Full=33 kDa glycogen-binding protein;
DE AltName: Full=Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 4;
DE Short=PP1 subunit R4;
DE AltName: Full=Protein phosphatase 1 subunit GL;
GN Name=Ppp1r3b; Synonyms=Ppp1r4;
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], PROTEIN SEQUENCE OF 42-56; 61-98; 150-157;
RP 161-169; 181-199; 201-220; 238-259 AND 280-284, FUNCTION, INTERACTION WITH
RP PYGL, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7498521; DOI=10.1016/0014-5793(95)01184-g;
RA Doherty M.J., Moorhead G., Morrice N., Cohen P., Cohen P.T.W.;
RT "Amino acid sequence and expression of the hepatic glycogen-binding (GL)-
RT subunit of protein phosphatase-1.";
RL FEBS Lett. 375:294-298(1995).
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 61-76 AND 150-157, INTERACTION WITH PPP1CC AND PYGL,
RP AND ASSOCIATION WITH GLYCOGEN.
RX PubMed=7720853; DOI=10.1016/0014-5793(95)00197-h;
RA Moorhead G., MacKintosh C., Morrice N., Cohen P.;
RT "Purification of the hepatic glycogen-associated form of protein
RT phosphatase-1 by microcystin-Sepharose affinity chromatography.";
RL FEBS Lett. 362:101-105(1995).
RN [4]
RP INTERACTION WITH GLYCOGEN; PPP1CC AND PYGL.
RX PubMed=9841883; DOI=10.1042/bj3360699;
RA Armstrong C.G., Doherty M.J., Cohen P.T.W.;
RT "Identification of the separate domains in the hepatic glycogen-targeting
RT subunit of protein phosphatase 1 that interact with phosphorylase a,
RT glycogen and protein phosphatase 1.";
RL Biochem. J. 336:699-704(1998).
RN [5]
RP FUNCTION.
RX PubMed=10862764; DOI=10.1074/jbc.m002427200;
RA Gasa R., Jensen P.B., Berman H.K., Brady M.J., DePaoli-Roach A.A.,
RA Newgard C.B.;
RT "Distinctive regulatory and metabolic properties of glycogen-targeting
RT subunits of protein phosphatase-1 (PTG, GL, GM/RGl) expressed in
RT hepatocytes.";
RL J. Biol. Chem. 275:26396-26403(2000).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11872655; DOI=10.2337/diabetes.51.3.591;
RA Munro S., Cuthbertson D.J., Cunningham J., Sales M., Cohen P.T.W.;
RT "Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that
RT is identical to the insulin-sensitive glycogen-targeting subunit G(L) of
RT liver.";
RL Diabetes 51:591-598(2002).
RN [7]
RP FUNCTION.
RX PubMed=17555403; DOI=10.1042/bj20061572;
RA Montori-Grau M., Guitart M., Lerin C., Andreu A.L., Newgard C.B.,
RA Garcia-Martinez C., Gomez-Foix A.M.;
RT "Expression and glycogenic effect of glycogen-targeting protein phosphatase
RT 1 regulatory subunit GL in cultured human muscle.";
RL Biochem. J. 405:107-113(2007).
CC -!- FUNCTION: Acts as a glycogen-targeting subunit for phosphatase PP1.
CC Facilitates interaction of the PP1 with enzymes of the glycogen
CC metabolism and regulates its activity. Suppresses the rate at which PP1
CC dephosphorylates (inactivates) glycogen phosphorylase and enhances the
CC rate at which it activates glycogen synthase and therefore limits
CC glycogen breakdown. Its activity is inhibited by PYGL, resulting in
CC inhibition of the glycogen synthase and glycogen phosphorylase
CC phosphatase activities of PP1. Dramatically increases basal and
CC insulin-stimulated glycogen synthesis upon overexpression in
CC hepatocytes. {ECO:0000269|PubMed:10862764, ECO:0000269|PubMed:17555403,
CC ECO:0000269|PubMed:7498521}.
CC -!- SUBUNIT: Interacts with glycogen, PPP1CC catalytic subunit of PP1 and
CC PYGL. Associates with glycogen particles. Forms complexes with
CC debranching enzyme, glycogen phosphorylase, glycogen synthase and
CC phosphorylase kinase which is necessary for its regulation of PP1
CC activity. {ECO:0000269|PubMed:7498521, ECO:0000269|PubMed:7720853,
CC ECO:0000269|PubMed:9841883}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver. Moderately expressed in
CC kidney, heart, testis, spleen and lung. Weakly expressed in skeletal
CC muscle (at protein level). Expressed predominantly in liver. Expressed
CC moderately in heart. Expressed weakly in lung, kidney, spleen and
CC skeletal muscle. {ECO:0000269|PubMed:11872655,
CC ECO:0000269|PubMed:7498521}.
CC -!- DOMAIN: The PP1-binding domain is located between residues 59 and 94.
CC The glycogen-binding domain is located between residues 94 and 257. The
CC PYGL-binding site lies in the C-terminal 16 amino acids.
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DR EMBL; Y18208; CAA77083.1; -; mRNA.
DR EMBL; BC072514; AAH72514.1; -; mRNA.
DR PIR; S68216; S68216.
DR RefSeq; NP_620267.2; NM_138912.2.
DR RefSeq; XP_006253277.1; XM_006253215.2.
DR RefSeq; XP_006253278.1; XM_006253216.3.
DR AlphaFoldDB; Q6IN01; -.
DR SMR; Q6IN01; -.
DR IntAct; Q6IN01; 1.
DR STRING; 10116.ENSRNOP00000042713; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q6IN01; -.
DR PhosphoSitePlus; Q6IN01; -.
DR PaxDb; Q6IN01; -.
DR DNASU; 192280; -.
DR Ensembl; ENSRNOT00000051720; ENSRNOP00000042713; ENSRNOG00000011474.
DR GeneID; 192280; -.
DR KEGG; rno:192280; -.
DR UCSC; RGD:621600; rat.
DR CTD; 79660; -.
DR RGD; 621600; Ppp1r3b.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000159475; -.
DR HOGENOM; CLU_040215_2_1_1; -.
DR InParanoid; Q6IN01; -.
DR OMA; GIAFDQF; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q6IN01; -.
DR TreeFam; TF105537; -.
DR PRO; PR:Q6IN01; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011474; Expressed in liver and 19 other tissues.
DR Genevisible; Q6IN01; RN.
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; IDA:RGD.
DR GO; GO:0050196; F:[phosphorylase] phosphatase activity; IMP:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:RGD.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
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; IPR030682; PP1_3B.
DR PANTHER; PTHR12307:SF13; PTHR12307:SF13; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PIRSF; PIRSF500814; PP1_GL; 1.
DR PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycogen metabolism;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..284
FT /note="Protein phosphatase 1 regulatory subunit 3B"
FT /id="PRO_0000324545"
FT DOMAIN 124..232
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT MOTIF 61..64
FT /note="PP1-binding motif"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C767"
FT CONFLICT 162
FT /note="R -> S (in Ref. 1; CAA77083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32626 MW; 8E64443CCE0EFE83 CRC64;
MAVDIEYSYS SMAPSLRRER FTFKISPKLN KPLRPCIQLG SKDEAGRMVA PTVQEKKVKK
RVSFADNQGL ALTMVKVFSE FDDPLDIPFN ITELLDNIVS LTTAESESFV LDFPQPSADY
LDFRNRLQTN HVCLENCVLK EKAIAGTVKV QNLAFEKVVK IRMTFDTWKS FTDFPCQYVK
DTYAGSDRDT FSFDISLPEK IQSYERMEFA VCYECNGQSY WDSNKGKNYR ITRAELRSTQ
GMTEPYNGPD FGISFDQFGS PRCSFGLFPE WPSYLGYEKL GPYY
