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Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PPT)

 PPP5_MOUSE              Reviewed;         499 AA.
Q60676; G5E819; O35299;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-OCT-2013, sequence version 3.
23-MAY-2018, entry version 170.
RecName: Full=Serine/threonine-protein phosphatase 5;
Short=PP5;
EC=3.1.3.16;
AltName: Full=Protein phosphatase T;
Short=PPT;
Name=Ppp5c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Ollendorff V., Donoghue D.J.;
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-155.
PubMed=7972012; DOI=10.1073/pnas.91.23.11075;
Chinkers M.;
"Targeting of a distinctive protein-serine phosphatase to the protein
kinase-like domain of the atrial natriuretic peptide receptor.";
Proc. Natl. Acad. Sci. U.S.A. 91:11075-11079(1994).
[6]
IDENTIFICATION IN A COMPLEX WITH HSP90AA1 AND NR3C1.
PubMed=9195923; DOI=10.1074/jbc.272.26.16224;
Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K.,
Chinkers M., Pratt W.B.;
"Protein phosphatase 5 is a major component of glucocorticoid
receptor.hsp90 complexes with properties of an FK506-binding
immunophilin.";
J. Biol. Chem. 272:16224-16230(1997).
[7]
INTERACTION WITH CPNE1.
PubMed=12522145; DOI=10.1074/jbc.M212632200;
Tomsig J.L., Snyder S.L., Creutz C.E.;
"Identification of targets for calcium signaling through the copine
family of proteins. Characterization of a coiled-coil copine-binding
motif.";
J. Biol. Chem. 278:10048-10054(2003).
[8]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16790549; DOI=10.1073/pnas.0604138103;
Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.;
"Posttranslational regulation of the mammalian circadian clock by
cryptochrome and protein phosphatase 5.";
Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006).
[9]
FUNCTION IN DNA DAMAGE RESPONSE, AND DISRUPTION PHENOTYPE.
PubMed=17376776; DOI=10.1074/jbc.C700019200;
Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.;
"Mice lacking protein phosphatase 5 are defective in ataxia
telangiectasia mutated (ATM)-mediated cell cycle arrest.";
J. Biol. Chem. 282:14690-14694(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION IN DEPHOSPHORYLATION OF NR3C1 AND PPARG, INTERACTION WITH
NR3C1 AND PPARG, AND SUBCELLULAR LOCATION.
PubMed=21994940; DOI=10.1074/jbc.M111.311662;
Hinds T.D. Jr., Stechschulte L.A., Cash H.A., Whisler D., Banerjee A.,
Yong W., Khuder S.S., Kaw M.K., Shou W., Najjar S.M., Sanchez E.R.;
"Protein phosphatase 5 mediates lipid metabolism through reciprocal
control of glucocorticoid receptor and peroxisome proliferator-
activated receptor-? (PPAR?).";
J. Biol. Chem. 286:42911-42922(2011).
[12]
FUNCTION IN GLUCOSE HOMEOSTASIS, AND DISRUPTION PHENOTYPE.
PubMed=22526606; DOI=10.1007/s00125-012-2541-1;
Grankvist N., Amable L., Honkanen R.E., Sjoeholm A., Ortsaeter H.;
"Serine/threonine protein phosphatase 5 regulates glucose homeostasis
in vivo and apoptosis signalling in mouse pancreatic islets and clonal
MIN6 cells.";
Diabetologia 55:2005-2015(2012).
-!- FUNCTION: Serine/threonine-protein phosphatase that
dephosphorylates a myriad of proteins involved in different
signaling pathways including the kinases CSNK1E, ASK1/MAP3K5,
PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2,
SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular
processes, including apoptosis, differentiation, DNA damage
response, cell survival, regulation of ion channels or circadian
rhythms, in response to steroid and thyroid hormones, calcium,
fatty acids, TGF-beta as well as oxidative and genotoxic stresses.
Participates in the control of DNA damage response mechanisms such
as checkpoint activation and DNA damage repair through, for
instance, the regulation ATM/ATR-signaling and dephosphorylation
of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis
induced by oxidative stress. Plays a positive role in
adipogenesis, mainly through the dephosphorylation and activation
of PPARG transactivation function. Also dephosphorylates and
inhibits the anti-adipogenic effect of NR3C1. Regulates the
circadian rhythms, through the dephosphorylation and activation of
CSNK1E. May modulate TGF-beta signaling pathway by the regulation
of SMAD3 phosphorylation and protein expression levels.
Dephosphorylates and may play a role in the regulation of
TAU/MAPT. Through their dephosphorylation, may play a role in the
regulation of ions channels such as KCNH2.
{ECO:0000269|PubMed:17376776, ECO:0000269|PubMed:21994940,
ECO:0000269|PubMed:22526606}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 Mg(2+) or Mn(2+) cations per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Autoinhibited. In the autoinhibited state, the
TPR domain interacts with the catalytic region and prevents
substrate access to the catalytic pocket. Allosterically activated
by various polyunsaturated fatty acids, free long-chain fatty-
acids and long-chain fatty acyl-CoA esters, arachidonic acid being
the most effective activator. HSP90A and probably RAC1, GNA12 and
GNA13 can also release the autoinhibition by the TPR repeat.
Activation by RAC1, GNA12 and GNA13 is synergistic with the one
produced by fatty acids binding. Inhibited by okadaic acid.
-!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
client protein TSC2 (By similarity). Probably forms a complex
composed of chaperones HSP90 and HSP70, co-chaperones CDC37,
PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1;
this complex does not contain co-chaperones STIP1/HOP and
PTGES3/p23 (By similarity). Part of a complex with HSP90/HSP90AA1
and steroid receptors (PubMed:9195923). Interacts (via TPR
repeats) with HSP90AA1 (via TPR repeat-binding motif) or
HSPA1A/HSPA1B; the interaction is direct and activates the
phosphatase activity (By similarity). Dissociates from
HSPA1A/HSPA1B and HSP90AA1 in response to arachidonic acid (By
similarity). Interacts with CPNE1 (via VWFA domain)
(PubMed:12522145). Interacts with CDC16, CDC27 (By similarity).
Interacts with KLHDC10 (via the 6 Kelch repeats); inhibits the
phosphatase activity on MAP3K5 (By similarity). Interacts with ATM
and ATR; both interactions are induced by DNA damage and enhance
ATM and ATR kinase activity (By similarity). Interacts with RAD17;
reduced by DNA damage (By similarity). Interacts with nuclear
receptors such as NR3C1/GCR and PPARG (activated by agonist);
regulates their transactivation activities (PubMed:9195923,
PubMed:21994940). Interacts (via TPR repeats) with S100 proteins
S100A1, S100A2, S100A6, S100B and S100P; the interactions are
calcium-dependent, strongly activate PPP5C phosphatase activity
and compete with HSP90AA1 and MAP3K5 interactions (By similarity).
Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3
phosphorylation and protein levels (By similarity). Interacts (via
TPR repeats) with CRY1 and CRY2; the interaction with CRY2
downregulates the phosphatase activity on CSNK1E (By similarity).
Interacts (via TPR repeats) with the active form of RAC1, GNA12 or
GNA13; these interactions activate the phosphatase activity and
translocate PPP5C to the cell membrane (By similarity). Interacts
with FLCN (By similarity). {ECO:0000250|UniProtKB:P53041,
ECO:0000269|PubMed:12522145, ECO:0000269|PubMed:21994940,
ECO:0000269|PubMed:9195923}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21994940}.
Cytoplasm {ECO:0000269|PubMed:21994940}. Cell membrane
{ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But
also present in the cytoplasm. Translocates from the cytoplasm to
the plasma membrane in a RAC1-dependent manner.
{ECO:0000250|UniProtKB:P53041}.
-!- TISSUE SPECIFICITY: Exressed in liver (at protein level) and
brain, enriched in suprachiasmatic nuclei.
{ECO:0000269|PubMed:16790549}.
-!- INDUCTION: Does not show circadian oscillation.
{ECO:0000269|PubMed:16790549}.
-!- PTM: Activated by at least two different proteolytic cleavages
producing a 56 kDa and a 50 kDa form. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Animals are fertile with a growth rate
equivalent to that of wild-type. Males weigh less, exhibit reduced
fasting glycaemia and improved glucose tolerance, but retain
normal insulin sensitivity. {ECO:0000269|PubMed:17376776,
ECO:0000269|PubMed:22526606}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF018262; AAB70573.1; -; mRNA.
EMBL; AC148976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466654; EDL42060.1; -; Genomic_DNA.
EMBL; BC003744; AAH03744.1; -; mRNA.
EMBL; U12204; AAB18613.1; -; mRNA.
CCDS; CCDS20859.1; -.
RefSeq; NP_035285.2; NM_011155.2.
UniGene; Mm.3294; -.
UniGene; Mm.475000; -.
ProteinModelPortal; Q60676; -.
SMR; Q60676; -.
BioGrid; 202349; 9.
IntAct; Q60676; 4.
MINT; Q60676; -.
STRING; 10090.ENSMUSP00000003183; -.
iPTMnet; Q60676; -.
PhosphoSitePlus; Q60676; -.
EPD; Q60676; -.
MaxQB; Q60676; -.
PaxDb; Q60676; -.
PeptideAtlas; Q60676; -.
PRIDE; Q60676; -.
Ensembl; ENSMUST00000003183; ENSMUSP00000003183; ENSMUSG00000003099.
GeneID; 19060; -.
KEGG; mmu:19060; -.
UCSC; uc009fiq.2; mouse.
CTD; 5536; -.
MGI; MGI:102666; Ppp5c.
eggNOG; KOG0376; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00530000063173; -.
HOGENOM; HOG000172698; -.
HOVERGEN; HBG000216; -.
InParanoid; Q60676; -.
KO; K04460; -.
OMA; LYPNHFF; -.
OrthoDB; EOG091G0589; -.
TreeFam; TF105562; -.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-8939211; ESR-mediated signaling.
ChiTaRS; Ppp5c; mouse.
PRO; PR:Q60676; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000003099; -.
CleanEx; MM_PPP5C; -.
ExpressionAtlas; Q60676; baseline and differential.
Genevisible; Q60676; MM.
GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:1990635; C:proximal dendrite; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0016791; F:phosphatase activity; ISO:MGI.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:MGI.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0016576; P:histone dephosphorylation; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; IEA:Ensembl.
GO; GO:0051259; P:protein complex oligomerization; IEA:Ensembl.
GO; GO:1904550; P:response to arachidonic acid; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IMP:MGI.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR013235; PPP_dom.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR011236; Ser/Thr_PPase_5.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11668:SF391; PTHR11668:SF391; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF08321; PPP5; 1.
Pfam; PF00515; TPR_1; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Cytoplasm; Hydrolase;
Magnesium; Manganese; Membrane; Metal-binding; Nucleus;
Protein phosphatase; Reference proteome; Repeat; TPR repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P53041}.
CHAIN 2 499 Serine/threonine-protein phosphatase 5.
/FTId=PRO_0000058895.
REPEAT 28 61 TPR 1.
REPEAT 62 95 TPR 2.
REPEAT 96 129 TPR 3.
REGION 184 499 Catalytic.
REGION 303 304 Substrate binding.
{ECO:0000250|UniProtKB:P53041}.
REGION 495 499 Required for autoinhibition.
{ECO:0000250|UniProtKB:P53042}.
ACT_SITE 304 304 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P53041}.
METAL 242 242 Manganese 1.
{ECO:0000250|UniProtKB:P53041}.
METAL 244 244 Manganese 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P53041}.
METAL 271 271 Manganese 1.
{ECO:0000250|UniProtKB:P53041}.
METAL 271 271 Manganese 2.
{ECO:0000250|UniProtKB:P53041}.
METAL 303 303 Manganese 2.
{ECO:0000250|UniProtKB:P53041}.
METAL 352 352 Manganese 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P53041}.
METAL 427 427 Manganese 2; via pros nitrogen.
{ECO:0000250|UniProtKB:P53041}.
BINDING 244 244 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 275 275 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 400 400 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 427 427 Substrate.
{ECO:0000250|UniProtKB:P53041}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P53041}.
CONFLICT 24 24 T -> A (in Ref. 1; AAB70573 and 4;
AAH03744). {ECO:0000305}.
CONFLICT 155 155 D -> G (in Ref. 5; AAB18613).
{ECO:0000305}.
SEQUENCE 499 AA; 56877 MW; 92C5509374FD6721 CRC64;
MAMAEGERTE CAETPRDEPP ADGTLKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPG
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE
TVVKVKPNDK DAKMKYQECS KIVKQKAFER AIAGDEHRRS VVDSLDIESM TIEDEYSGPK
LEDGKVTITF MKDLMQWYKD QKKLHRKCAY QILVQVKEVL CKLSTLVETT LKETEKITVC
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR GVSCQFGPDV TKAFLEENQL
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP
HPNVKPMAYA NTLLQLGMM


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