Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q99MR9 (PPR3A_MOUSE)

Last modified April 14, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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=RGL
Gene names
Name: Ppp1r3a
Synonyms: Pp1g
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1089 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.4

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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glycogen metabolism
   Cellular componentMembrane
   DomainTransmembrane
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycogen metabolic process Ref.1

Traceable author statement. Source: MGI

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10891089Protein phosphatase 1 regulatory subunit 3A
PRO_0000071501

Regions

Transmembrane1047 – 106721 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
Modified residue2631Phosphoserine Ref.5
Modified residue3531Phosphoserine Ref.5
Modified residue7361Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99MR9-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 94A86B798D0C8FD2

FASTA1,089121,465
        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 KSGSGGERSG 

       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: 11361130] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129/Sv.
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-626.
Strain: C57BL/6J.
Tissue: Embryonic heart.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 259-264, MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"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: 11283248] [Abstract]
Cited for: FUNCTION.
Strain: 129/Sv.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-353, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF309629, AF309628 Genomic DNA. Translation: AAK31072.1.
AK084518 mRNA. Translation: BAC39208.2.
AK084719 mRNA. Translation: BAC39262.2.
IPIIPI00342163.
RefSeqNP_536712.2.
UniGeneMm.209429

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSiteQ99MR9.

Genome annotation databases

EnsemblENSMUSG00000042717. Mus musculus. [Contig view]
GeneID140491.
KEGGmmu:140491.

Organism-specific databases

MGIMGI:2153588. Ppp1r3a.

Phylogenomic databases

HOGENOMQ99MR9.
HOVERGENQ99MR9.

Gene expression databases

ArrayExpressQ99MR9.
BgeeQ99MR9.
GermOnlineENSMUSG00000042717. Mus musculus.

Family and domain databases

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

Other Resources

NextBio369808.
SOURCESearch...

Entry information

Entry namePPR3A_MOUSE
AccessionPrimary (citable) accession number: Q99MR9
Secondary accession number(s): Q8BUJ4, Q8BUL0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2001
Last modified: April 14, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents