PPR3A_MOUSE
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 03-AUG-2022, entry version 126.
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 iPTMnet; Q99MR9; -.
DR PhosphoSitePlus; Q99MR9; -.
DR MaxQB; Q99MR9; -.
DR PaxDb; Q99MR9; -.
DR PRIDE; Q99MR9; -.
DR ProteomicsDB; 291839; -.
DR Antibodypedia; 45888; 133 antibodies from 23 providers.
DR DNASU; 140491; -.
DR Ensembl; ENSMUST00000045096; ENSMUSP00000049054; ENSMUSG00000042717.
DR GeneID; 140491; -.
DR KEGG; mmu:140491; -.
DR UCSC; uc009ayw.1; mouse.
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; TFKPGFS; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q99MR9; -.
DR TreeFam; TF105537; -.
DR BioGRID-ORCS; 140491; 1 hit in 74 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 tissues.
DR Genevisible; Q99MR9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; 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
