PPR3B_MOUSE
ID PPR3B_MOUSE Reviewed; 284 AA.
AC Q8C767; Q6PAJ7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3B;
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;
DE Short=PTG;
GN Name=Ppp1r3b; Synonyms=Ppp1r4;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [2]
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 [3]
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 [4]
RP INDUCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16949035; DOI=10.1016/j.bbrc.2006.08.091;
RA Niimi T., Kurotani R., Kimura S., Kitagawa Y.;
RT "Identification and expression of alternative splice variants of the mouse
RT Ppp1r3b gene in lung epithelial cells.";
RL Biochem. Biophys. Res. Commun. 349:588-596(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver (at protein level).
CC Expressed predominantly in liver. Expressed moderately in heart.
CC Expressed weakly in prostate, stomach, thyroid, lung, kidney, spleen
CC and skeletal muscle. {ECO:0000269|PubMed:11872655,
CC ECO:0000269|PubMed:16949035}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lung at 12.5 and 16.5 dpc and
CC declines thereafter. Expressed in epithelial cells of the bronchus and
CC smooth muscle of the pulmonary artery at 13.5 and 16.5 dpc.
CC {ECO:0000269|PubMed:16949035}.
CC -!- INDUCTION: Up-regulated by TITF1. {ECO:0000269|PubMed:16949035}.
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 PYGL. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK052438; BAC34990.1; -; mRNA.
DR EMBL; BC060261; AAH60261.1; ALT_INIT; mRNA.
DR EMBL; BC079666; AAH79666.1; -; mRNA.
DR CCDS; CCDS22243.1; -.
DR RefSeq; NP_808409.1; NM_177741.3.
DR RefSeq; XP_006509181.1; XM_006509118.3.
DR RefSeq; XP_017168286.1; XM_017312797.1.
DR RefSeq; XP_017168287.1; XM_017312798.1.
DR AlphaFoldDB; Q8C767; -.
DR SMR; Q8C767; -.
DR BioGRID; 232645; 9.
DR IntAct; Q8C767; 10.
DR STRING; 10090.ENSMUSP00000065679; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q8C767; -.
DR PhosphoSitePlus; Q8C767; -.
DR MaxQB; Q8C767; -.
DR PaxDb; Q8C767; -.
DR PRIDE; Q8C767; -.
DR ProteomicsDB; 291840; -.
DR Antibodypedia; 22075; 136 antibodies from 21 providers.
DR DNASU; 244416; -.
DR Ensembl; ENSMUST00000070481; ENSMUSP00000065679; ENSMUSG00000046794.
DR Ensembl; ENSMUST00000210337; ENSMUSP00000147736; ENSMUSG00000046794.
DR Ensembl; ENSMUST00000211648; ENSMUSP00000147633; ENSMUSG00000046794.
DR GeneID; 244416; -.
DR KEGG; mmu:244416; -.
DR UCSC; uc009lkw.1; mouse.
DR CTD; 79660; -.
DR MGI; MGI:2177268; Ppp1r3b.
DR VEuPathDB; HostDB:ENSMUSG00000046794; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00940000159475; -.
DR HOGENOM; CLU_040215_2_1_1; -.
DR InParanoid; Q8C767; -.
DR OMA; GIAFDQF; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q8C767; -.
DR TreeFam; TF105537; -.
DR BioGRID-ORCS; 244416; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ppp1r3b; mouse.
DR PRO; PR:Q8C767; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C767; protein.
DR Bgee; ENSMUSG00000046794; Expressed in left lung lobe and 178 other tissues.
DR Genevisible; Q8C767; MM.
DR GO; GO:0042587; C:glycogen granule; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:MGI.
DR GO; GO:0050196; F:[phosphorylase] phosphatase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:2001069; F:glycogen binding; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; TAS:MGI.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; ISO:MGI.
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; Glycogen metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Protein phosphatase 1 regulatory subunit 3B"
FT /id="PRO_0000324544"
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:0007744|PubMed:21183079"
SQ SEQUENCE 284 AA; 32433 MW; 193C1BAC1286D344 CRC64;
MAVDIQYSYS SMAPSLRRER FTFKISPKLS KPLRPCIQLG SKDEASGMVA PAVQEKKVKK
RVSFADNQGL ALTMVKVFSE FDDPLDIPFN ITELLDNIVS LTTAESESFV LDFPQPSADY
LDFRNRLQTN HVCLENCVLK DKAIAGTVKV QNLAFEKVVK IRMTFDTWKS FTDFPCQYVK
DTYAGSDRDT FSFDISLPEK IQSYERMEFA VCYECNGQAY WDSNKGKNYR ITRAELRSSP
GKIEPYNGPD FGISFDQFGS PRCSFGLFPE WPSYLGYEKL GPYY
