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Q99MR9 (PPR3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1 regulatory subunit 3A
Alternative name(s):
Protein phosphatase 1 glycogen-associated regulatory subunit
Protein phosphatase type-1 glycogen targeting subunit
Short name=RG1
Gene names
Name:Ppp1r3a
Synonyms:Pp1g
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. Ref.6

Subunit structure

Interacts with PPP1CC catalytic subunit of PP1, and associates with glycogen By similarity.

Subcellular location

Membrane; Single-pass membrane protein By similarity.

Tissue specificity

Skeletal muscle and heart. Ref.1

Domain

The CBM21 domain is known to be involved in the localization to glycogen and is characteristic of some regulatory subunit of phosphatase complexes.

Post-translational modification

Phosphorylation at Ser-48 by ISPK stimulates the dephosphorylation of glycogen synthase and phosphorylase kinase By similarity.

Sequence similarities

Contains 1 CBM21 (carbohydrate binding type-21) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10891089Protein phosphatase 1 regulatory subunit 3A
PRO_0000071501

Regions

Transmembrane1047 – 106721Helical; Potential
Domain123 – 231109CBM21
Motif64 – 674PP1-binding motif

Amino acid modifications

Modified residue401Phosphoserine; by GSK3 By similarity
Modified residue441Phosphoserine; by GSK3 By similarity
Modified residue481Phosphoserine; by PKA and ISPK By similarity
Modified residue671Phosphoserine; by PKA By similarity

Experimental info

Sequence conflict9591G → S in AAK31072. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99MR9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 85EC67FD90CC8FD2

FASTA1,089121,435
        10         20         30         40         50         60 
MEPAEEPGQI SKDNFLEVPN LSDSVCEDEE VKATFKPGFS PQPSRRGSGS SEDMYLDTPT 

        70         80         90        100        110        120 
SASRRVSFAD SLGFSLVSVK EFDCWELPSV STDFDLSGDV FHTDEYVLSP LFDLPSSKEK 

       130        140        150        160        170        180 
LMEQLQVQKA VLESAEHLPG SSMKGIIRVL NISFEKLVYV RMSLDDWQTH YDILAEYVPN 

       190        200        210        220        230        240 
SCDGETDQFS FKISLVPPYQ KEGGKVEFCI RYETSAGTFW SNNNGTNYIL VCQKKRKEPE 

       250        260        270        280        290        300 
PVKPLEEAPS RQIKGCLKVK SRSKEEPLLA PEENKFETLK FTESYIPTII CSHEDKDDLG 

       310        320        330        340        350        360 
ANHPNVDDIN KKHDEHNGKE LDLMINQRLI TSQDEKNTFA TDTVNFTNKA EGSEKKQAYH 

       370        380        390        400        410        420 
EINTDLFMGP LSPSLSAESS LKRDFYHSRS SSPGNEYGHP HSEEIISDMG EKGPSLGDTS 

       430        440        450        460        470        480 
SDELMQLELC SKEDLDDNAN PANGSGRVCS SFDQRMACGL KNNEAGIKKT GIQDYKYSHG 

       490        500        510        520        530        540 
DSTKLEESNA SSRDDYAKVD NKKEKQTCLG VNENPSKNFQ SVFQTQEGHM GYPKISTEGD 

       550        560        570        580        590        600 
KANNQDLTSL LSKDITANTW AVTVDPCPST NAKRSWREVG SGSNLEPGTS DLSSPRNFSP 

       610        620        630        640        650        660 
LTDDHLFQAD RENSDSSNPE NQNMNTRHRK KWNVLETQSE TSETESDIAK HTKEQAEYKD 

       670        680        690        700        710        720 
MWEKTDNSRN LKATPTEHLF TCRETECYGL SSLADHGITE KAQAVTAYII KTTLESTPES 

       730        740        750        760        770        780 
ASARGKAIIA KLPQETAGND RPIEVKETAF DPHEGRKDDS HYSLCHGDTA GVIHDNDFER 

       790        800        810        820        830        840 
ESHLDICNLR VDEMKKEKTT STCFPQKTYD KEKHGIGSVT SIDEPSQVIT GNQKATSKLD 

       850        860        870        880        890        900 
LHLGVLPTDR AIFQANADLE LLQELSRRTD FNAVPSAFNS DTASASRDSS QVYRHCSKKS 

       910        920        930        940        950        960 
VPSYGEEKAV TNTTLQSIPT KSEYNWHPES EVLGHAMSKP EDVFKSSEIM KSGSGGERGG 

       970        980        990       1000       1010       1020 
GPILQQKEGS LENSQGPMFF TNEPLENLDE ASSENEGLMH SGQSQCYLGD KGLVSSASAT 

      1030       1040       1050       1060       1070       1080 
VSTQELEAQG RESLLSISTN SKIPYFLLFL IFLATVYYYD LMIGLAFYLF SLYWLYWEGG 


RQRESVKKK 

« Hide

References

« Hide 'large scale' references
[1]"Gene structure and expression of the targeting subunit, RGL, of the muscle-specific glycogen-associated type 1 protein phosphatase, PP1G."
Lanner C., Suzuki Y., Bi C., Zhang H., Cooper L.D., Bowker-Kinley M.M., DePaoli-Roach A.A.
Arch. Biochem. Biophys. 388:135-145(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/Sv.
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-626.
Strain: C57BL/6J.
Tissue: Embryonic heart.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 259-264, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G/RGL."
Suzuki Y., Lanner C., Kim J.-H., Vilardo P.G., Zhang H., Yang J., Cooper L.D., Steele M., Kennedy A., Bock C.B., Scrimgeour A., Lawrence J.C. Jr., DePaoli-Roach A.A.
Mol. Cell. Biol. 21:2683-2694(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: 129/Sv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF309629, AF309628 Genomic DNA. Translation: AAK31072.1.
CH466533 Genomic DNA. Translation: EDL13902.1.
BC109007 mRNA. Translation: AAI09008.1.
AK084518 mRNA. Translation: BAC39208.2.
AK084719 mRNA. Translation: BAC39262.2.
CCDSCCDS19917.1.
RefSeqNP_536712.2. NM_080464.2.
UniGeneMm.209429.

3D structure databases

ProteinModelPortalQ99MR9.
SMRQ99MR9. Positions 124-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99MR9. 2 interactions.
MINTMINT-4108485.

Protein family/group databases

CAZyCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSiteQ99MR9.

Proteomic databases

MaxQBQ99MR9.
PaxDbQ99MR9.
PRIDEQ99MR9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045096; ENSMUSP00000049054; ENSMUSG00000042717.
GeneID140491.
KEGGmmu:140491.
UCSCuc009ayw.1. mouse.

Organism-specific databases

CTD5506.
MGIMGI:2153588. Ppp1r3a.

Phylogenomic databases

eggNOGNOG288354.
GeneTreeENSGT00530000062978.
HOGENOMHOG000115667.
HOVERGENHBG053657.
InParanoidQ32MS0.
KOK07189.
OMAAFDPHEG.
OrthoDBEOG769ZKR.
TreeFamTF105537.

Gene expression databases

BgeeQ99MR9.
GenevestigatorQ99MR9.

Family and domain databases

InterProIPR005036. CBM_21.
[Graphical view]
PfamPF03370. CBM_21. 1 hit.
[Graphical view]
PROSITEPS51159. CBM21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio369808.
PROQ99MR9.
SOURCESearch...

Entry information

Entry namePPR3A_MOUSE
AccessionPrimary (citable) accession number: Q99MR9
Secondary accession number(s): Q32MS0, Q8BUJ4, Q8BUL0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot