PPR3E_MOUSE
ID PPR3E_MOUSE Reviewed; 279 AA.
AC Q8BRJ4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3E;
GN Name=Ppp1r3e;
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], MOTIF, AND FUNCTION.
RX PubMed=15752363; DOI=10.1111/j.1742-4658.2005.04585.x;
RA Munro S., Ceulemans H., Bollen M., Diplexcito J., Cohen P.T.W.;
RT "A novel glycogen-targeting subunit of protein phosphatase 1 that is
RT regulated by insulin and shows differential tissue distribution in humans
RT and rodents.";
RL FEBS J. 272:1478-1489(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-279.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 PP1. PP1 is involved
CC in glycogen metabolism and contributes to the activation of glycogen
CC synthase leading to an increase in glycogen synthesis.
CC {ECO:0000269|PubMed:15752363}.
CC -!- DOMAIN: The CBM21 domain is known to be involved in the localization to
CC glycogen and is characteristic of some regulatory subunit of
CC phosphatase complexes.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31772.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AC116591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK044095; BAC31772.1; ALT_SEQ; mRNA.
DR CCDS; CCDS56958.1; -.
DR AlphaFoldDB; Q8BRJ4; -.
DR SMR; Q8BRJ4; -.
DR STRING; 10090.ENSMUSP00000134894; -.
DR iPTMnet; Q8BRJ4; -.
DR PhosphoSitePlus; Q8BRJ4; -.
DR MaxQB; Q8BRJ4; -.
DR PaxDb; Q8BRJ4; -.
DR PRIDE; Q8BRJ4; -.
DR ProteomicsDB; 291842; -.
DR MGI; MGI:2145790; Ppp1r3e.
DR eggNOG; KOG3986; Eukaryota.
DR InParanoid; Q8BRJ4; -.
DR PRO; PR:Q8BRJ4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BRJ4; protein.
DR GO; GO:0042587; C:glycogen granule; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:0050196; F:[phosphorylase] phosphatase activity; 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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISO: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 Pfam; PF03370; CBM_21; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Protein phosphatase 1 regulatory subunit 3E"
FT /id="PRO_0000338639"
FT DOMAIN 154..259
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 28..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..198
FT /note="Glycogen-binding motif"
FT /evidence="ECO:0000250"
FT REGION 248..256
FT /note="Substrate-binding motif"
FT /evidence="ECO:0000250"
FT MOTIF 87..90
FT /note="PP1-binding motif"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7J1"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7J1"
FT CONFLICT 3
FT /note="P -> H (in Ref. 2; AC116591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30575 MW; 47954E88D6EB2CC0 CRC64;
MSPERPPRTD IPRNLSFIAA LTERAYYRSQ RPSLEEESEE EPGEGGTRPG ARSRAHVPGR
GRRARSAPAG GGGARTARSR SPDTRKRVRF ADALGLELAV VRRFRPGEPP RVPRHVQVQL
QRDALRHFAP CPPRARGLQE ARVALEPALE PGFAARLQAQ RICLERADAG PLGVAGSARV
LDLAYEKRVS VRWSADGWRS LRESPASYAG PAPSPPRADR FAFRLPAPPV GGTLLFALRY
RVTGREFWDN NGGRDYALLG PEHPAGAGAA EPQGWIHFI
