ID   PPR3E_RAT               Reviewed;         279 AA.
AC   P0C7L8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3E;
GN   Name=Ppp1r3e;
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], MOTIF, FUNCTION, AND TISSUE SPECIFICITY.
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=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
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   -!- TISSUE SPECIFICITY: Expressed in liver and heart, with low levels in
CC       skeletal muscle. {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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03095589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C7L8; -.
DR   SMR; P0C7L8; -.
DR   STRING; 10116.ENSRNOP00000019992; -.
DR   PaxDb; P0C7L8; -.
DR   UCSC; RGD:1583926; rat.
DR   RGD; 1583926; Ppp1r3e.
DR   eggNOG; KOG3986; Eukaryota.
DR   InParanoid; P0C7L8; -.
DR   PhylomeDB; P0C7L8; -.
DR   PRO; PR:P0C7L8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0042587; C:glycogen granule; 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:2001069; F:glycogen binding; IBA:GO_Central.
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; IMP: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   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript 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_0000338640"
FT   DOMAIN          154..259
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          28..89
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:0000250|UniProtKB:Q9H7J1"
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        91
FT                   /note="P -> A (in Ref. 2; AABR03095589)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  30624 MW;  BC3E26DB85C6EE85 CRC64;
     MSHERPPRND IPRNLSFIAA LTERAYYRSQ RPSLEEESEE EPGEGGTRPG ARSRAHVPGR
     GRRARSAPAG GGGARTARSR SPDTRKRVRF PDALGLELAV VRRFRPGEPP RVPRHVQVQL
     QRDALRHFAP CPPRTRGLQD ARIALEPALE PGFAARLQAQ RICLERADAG PLGVAGSARV
     LDLAYEKRVS VRWSADGWRS LRESPASYAG PAPAPPRADR FAFRLPAPPV GGALLFALRY
     RVTGREFWDN NGGRDYALLG PEHPGGAGAA EPQGWIHFI