Q99MR9 (PPR3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1089 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from sequence orthology Ref.1. Source: GOC glycogen metabolic process Traceable author statement Ref.1. Source: MGI
Cellular_component	integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	protein serine/threonine phosphatase activity Inferred from sequence orthology Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1089	1089	Protein phosphatase 1 regulatory subunit 3A		PRO_0000071501
Regions
	Transmembrane	1047 – 1067	21	Helical; Potential
	Domain	123 – 231	109	CBM21
	Motif	64 – 67	4	PP1-binding motif
Amino acid modifications
	Modified residue	40	1	Phosphoserine; by GSK3 By similarity
	Modified residue	44	1	Phosphoserine; by GSK3 By similarity
	Modified residue	48	1	Phosphoserine; by PKA and ISPK By similarity
	Modified residue	67	1	Phosphoserine; by PKA By similarity
Experimental info
	Sequence conflict	959	1	G → S in AAK31072. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99MR9 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 85EC67FD90CC8FD2	FASTA	1,089	121,435
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
CCDS	CCDS19917.1.
RefSeq	NP_536712.2. NM_080464.2.
UniGene	Mm.209429.
3D structure databases
ProteinModelPortal	Q99MR9.
SMR	Q99MR9. Positions 124-244.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
IntAct	Q99MR9. 2 interactions.
MINT	MINT-4108485.
Protein family/group databases
CAZy	CBM21. Carbohydrate-Binding Module Family 21.
PTM databases
PhosphoSite	Q99MR9.
Proteomic databases
MaxQB	Q99MR9.
PaxDb	Q99MR9.
PRIDE	Q99MR9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000045096; ENSMUSP00000049054; ENSMUSG00000042717.
GeneID	140491.
KEGG	mmu:140491.
UCSC	uc009ayw.1. mouse.
Organism-specific databases
CTD	5506.
MGI	MGI:2153588. Ppp1r3a.
Phylogenomic databases
eggNOG	NOG288354.
GeneTree	ENSGT00530000062978.
HOGENOM	HOG000115667.
HOVERGEN	HBG053657.
InParanoid	Q32MS0.
KO	K07189.
OMA	AFDPHEG.
OrthoDB	EOG769ZKR.
TreeFam	TF105537.
Gene expression databases
Bgee	Q99MR9.
Genevestigator	Q99MR9.
Family and domain databases
InterPro	IPR005036. CBM_21. [Graphical view]
Pfam	PF03370. CBM_21. 1 hit. [Graphical view]
PROSITE	PS51159. CBM21. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	369808.
PRO	Q99MR9.
SOURCE	Search...

Entry information

Entry name

PPR3A_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program