ID   PPR3A_MOUSE             Reviewed;        1089 AA.
AC   Q99MR9; Q32MS0; Q8BUJ4; Q8BUL0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3A;
DE   AltName: Full=Protein phosphatase 1 glycogen-associated regulatory subunit;
DE   AltName: Full=Protein phosphatase type-1 glycogen targeting subunit;
DE            Short=RG1;
GN   Name=Ppp1r3a; Synonyms=Pp1g;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=11361130; DOI=10.1006/abbi.2001.2283;
RA   Lanner C., Suzuki Y., Bi C., Zhang H., Cooper L.D., Bowker-Kinley M.M.,
RA   DePaoli-Roach A.A.;
RT   "Gene structure and expression of the targeting subunit, RGL, of the
RT   muscle-specific glycogen-associated type 1 protein phosphatase, PP1G.";
RL   Arch. Biochem. Biophys. 388:135-145(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-626.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic heart;
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   [5]
RP   PROTEIN SEQUENCE OF 259-264, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   FUNCTION.
RC   STRAIN=129/Sv;
RX   PubMed=11283248; DOI=10.1128/mcb.21.8.2683-2694.2001;
RA   Suzuki Y., Lanner C., Kim J.-H., Vilardo P.G., Zhang H., Yang J.,
RA   Cooper L.D., Steele M., Kennedy A., Bock C.B., Scrimgeour A.,
RA   Lawrence J.C. Jr., DePaoli-Roach A.A.;
RT   "Insulin control of glycogen metabolism in knockout mice lacking the
RT   muscle-specific protein phosphatase PP1G/RGL.";
RL   Mol. Cell. Biol. 21:2683-2694(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-51; THR-58 AND
RP   SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Lung;
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: Seems to act as a glycogen-targeting subunit for PP1. PP1 is
CC       essential for cell division, and participates in the regulation of
CC       glycogen metabolism, muscle contractility and protein synthesis. Plays
CC       an important role in glycogen synthesis but is not essential for
CC       insulin activation of glycogen synthase. {ECO:0000269|PubMed:11283248}.
CC   -!- SUBUNIT: Interacts with PPP1CC catalytic subunit of PP1, and associates
CC       with glycogen. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle and heart.
CC       {ECO:0000269|PubMed:11361130}.
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   -!- PTM: Phosphorylation at Ser-48 by ISPK stimulates the dephosphorylation
CC       of glycogen synthase and phosphorylase kinase. {ECO:0000250}.
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DR   EMBL; AF309629; AAK31072.1; -; Genomic_DNA.
DR   EMBL; AF309628; AAK31072.1; JOINED; Genomic_DNA.
DR   EMBL; CH466533; EDL13902.1; -; Genomic_DNA.
DR   EMBL; BC109007; AAI09008.1; -; mRNA.
DR   EMBL; AK084518; BAC39208.2; -; mRNA.
DR   EMBL; AK084719; BAC39262.2; -; mRNA.
DR   CCDS; CCDS19917.1; -.
DR   RefSeq; NP_536712.2; NM_080464.2.
DR   AlphaFoldDB; Q99MR9; -.
DR   SMR; Q99MR9; -.
DR   BioGRID; 228264; 12.
DR   IntAct; Q99MR9; 3.
DR   STRING; 10090.ENSMUSP00000049054; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   GlyGen; Q99MR9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99MR9; -.
DR   PhosphoSitePlus; Q99MR9; -.
DR   MaxQB; Q99MR9; -.
DR   PaxDb; 10090-ENSMUSP00000049054; -.
DR   ProteomicsDB; 291839; -.
DR   Antibodypedia; 45888; 146 antibodies from 23 providers.
DR   DNASU; 140491; -.
DR   Ensembl; ENSMUST00000045096.6; ENSMUSP00000049054.5; ENSMUSG00000042717.6.
DR   GeneID; 140491; -.
DR   KEGG; mmu:140491; -.
DR   UCSC; uc009ayw.1; mouse.
DR   AGR; MGI:2153588; -.
DR   CTD; 5506; -.
DR   MGI; MGI:2153588; Ppp1r3a.
DR   VEuPathDB; HostDB:ENSMUSG00000042717; -.
DR   eggNOG; KOG3986; Eukaryota.
DR   GeneTree; ENSGT00940000157682; -.
DR   HOGENOM; CLU_009399_0_0_1; -.
DR   InParanoid; Q99MR9; -.
DR   OMA; DCWELPS; -.
DR   OrthoDB; 5357390at2759; -.
DR   PhylomeDB; Q99MR9; -.
DR   TreeFam; TF105537; -.
DR   BioGRID-ORCS; 140491; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Ppp1r3a; mouse.
DR   PRO; PR:Q99MR9; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q99MR9; Protein.
DR   Bgee; ENSMUSG00000042717; Expressed in interventricular septum and 34 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; TAS:MGI.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IBA:GO_Central.
DR   CDD; cd22255; PBD_PPP1R3A; 1.
DR   Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR   InterPro; IPR005036; CBM21_dom.
DR   InterPro; IPR038175; CBM21_dom_sf.
DR   PANTHER; PTHR12307; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR12307:SF2; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 3A; 1.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
DR   Genevisible; Q99MR9; MM.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycogen metabolism;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1089
FT                   /note="Protein phosphatase 1 regulatory subunit 3A"
FT                   /id="PRO_0000071501"
FT   TRANSMEM        1047..1067
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          123..231
FT                   /note="CBM21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT   REGION          32..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           64..67
FT                   /note="PP1-binding motif"
FT   COMPBIAS        41..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         40
FT                   /note="Phosphoserine; by GSK3"
FT                   /evidence="ECO:0000250|UniProtKB:Q00756"
FT   MOD_RES         44
FT                   /note="Phosphoserine; by GSK3"
FT                   /evidence="ECO:0000250|UniProtKB:Q00756"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         58
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         67
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q00756"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        959
FT                   /note="G -> S (in Ref. 1; AAK31072)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1089 AA;  121435 MW;  85EC67FD90CC8FD2 CRC64;
     MEPAEEPGQI SKDNFLEVPN LSDSVCEDEE VKATFKPGFS PQPSRRGSGS SEDMYLDTPT
     SASRRVSFAD SLGFSLVSVK EFDCWELPSV STDFDLSGDV FHTDEYVLSP LFDLPSSKEK
     LMEQLQVQKA VLESAEHLPG SSMKGIIRVL NISFEKLVYV RMSLDDWQTH YDILAEYVPN
     SCDGETDQFS FKISLVPPYQ KEGGKVEFCI RYETSAGTFW SNNNGTNYIL VCQKKRKEPE
     PVKPLEEAPS RQIKGCLKVK SRSKEEPLLA PEENKFETLK FTESYIPTII CSHEDKDDLG
     ANHPNVDDIN KKHDEHNGKE LDLMINQRLI TSQDEKNTFA TDTVNFTNKA EGSEKKQAYH
     EINTDLFMGP LSPSLSAESS LKRDFYHSRS SSPGNEYGHP HSEEIISDMG EKGPSLGDTS
     SDELMQLELC SKEDLDDNAN PANGSGRVCS SFDQRMACGL KNNEAGIKKT GIQDYKYSHG
     DSTKLEESNA SSRDDYAKVD NKKEKQTCLG VNENPSKNFQ SVFQTQEGHM GYPKISTEGD
     KANNQDLTSL LSKDITANTW AVTVDPCPST NAKRSWREVG SGSNLEPGTS DLSSPRNFSP
     LTDDHLFQAD RENSDSSNPE NQNMNTRHRK KWNVLETQSE TSETESDIAK HTKEQAEYKD
     MWEKTDNSRN LKATPTEHLF TCRETECYGL SSLADHGITE KAQAVTAYII KTTLESTPES
     ASARGKAIIA KLPQETAGND RPIEVKETAF DPHEGRKDDS HYSLCHGDTA GVIHDNDFER
     ESHLDICNLR VDEMKKEKTT STCFPQKTYD KEKHGIGSVT SIDEPSQVIT GNQKATSKLD
     LHLGVLPTDR AIFQANADLE LLQELSRRTD FNAVPSAFNS DTASASRDSS QVYRHCSKKS
     VPSYGEEKAV TNTTLQSIPT KSEYNWHPES EVLGHAMSKP EDVFKSSEIM KSGSGGERGG
     GPILQQKEGS LENSQGPMFF TNEPLENLDE ASSENEGLMH SGQSQCYLGD KGLVSSASAT
     VSTQELEAQG RESLLSISTN SKIPYFLLFL IFLATVYYYD LMIGLAFYLF SLYWLYWEGG
     RQRESVKKK
//