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Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (Phosphatase 1 nuclear targeting subunit) (Protein PNUTS)

 PP1RA_RAT               Reviewed;         872 AA.
O55000; Q6MG09;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 130.
RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
AltName: Full=MHC class I region proline-rich protein CAT53;
AltName: Full=Phosphatase 1 nuclear targeting subunit;
Short=Protein PNUTS;
Name=Ppp1r10; Synonyms=Cat53, Pnuts;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PPP1CA INHIBITION, INTERACTION
WITH PPP1CA, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
PubMed=9461602; DOI=10.1074/jbc.273.7.4089;
Allen P.B., Kwon Y.G., Nairn A.C., Greengard P.;
"Isolation and characterization of PNUTS, a putative protein
phosphatase 1 nuclear targeting subunit.";
J. Biol. Chem. 273:4089-4095(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15060004; DOI=10.1101/gr.1987704;
Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T.,
Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
"The genomic sequence and comparative analysis of the rat major
histocompatibility complex.";
Genome Res. 14:631-639(2004).
[3]
FUNCTION IN PPP1CA INHIBITION, IDENTIFICATION IN A COMPLEX WITH PPP1CA
AND RNA HOMOPOLYMERS, PHOSPHORYLATION AT THR-398, MUTAGENESIS OF
ARG-396; LYS-397; VAL-399; TRP-401 AND 445-GLU--LEU-450, DNA-BINDING,
RNA-BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12574161; DOI=10.1074/jbc.M209621200;
Kim Y.M., Watanabe T., Allen P.B., Kim Y.M., Lee S.J., Greengard P.,
Nairn A.C., Kwon Y.G.;
"PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit.
Characterization of its PP1- and RNA-binding domains and regulation by
phosphorylation.";
J. Biol. Chem. 278:13819-13828(2003).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-382 AND
SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Scaffold protein which mediates the formation of the
PTW/PP1 phosphatase complex by providing a binding platform to
each component of the complex. The PTW/PP1 phosphatase complex
plays a role in the control of chromatin structure and cell cycle
progression during the transition from mitosis into interphase.
Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and
PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA
only when phosphorylated. Binds to mRNA, single-stranded DNA
(ssDNA), poly(A) and poly(G) homopolymers.
{ECO:0000269|PubMed:12574161, ECO:0000269|PubMed:9461602}.
-!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
Interacts with PPP1CC. Interacts with PPP1CA, WDR82 and TOX4 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and
within nucleoli. Associates with chromatin during interphase,
excluded from condensed chromosomes during early mitosis and is
reloaded onto chromosomes at the late telophase (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in testis, brain and intestine (at
protein level). Highly expressed in testis.
{ECO:0000269|PubMed:12574161, ECO:0000269|PubMed:9461602}.
-!- PTM: Phosphorylated on Thr-398 by PKA within the region necessary
for interaction with PPP1CA. {ECO:0000269|PubMed:12574161}.
-!- SEQUENCE CAUTION:
Sequence=CAE84038.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF040954; AAB96775.1; -; mRNA.
EMBL; BX883048; CAE84038.1; ALT_SEQ; Genomic_DNA.
RefSeq; NP_075240.1; NM_022951.2.
UniGene; Rn.37758; -.
PDB; 4MOY; X-ray; 2.20 A; B=393-433.
PDB; 4MP0; X-ray; 2.10 A; B/D=394-433.
PDBsum; 4MOY; -.
PDBsum; 4MP0; -.
ProteinModelPortal; O55000; -.
SMR; O55000; -.
iPTMnet; O55000; -.
PhosphoSitePlus; O55000; -.
PRIDE; O55000; -.
GeneID; 65045; -.
KEGG; rno:65045; -.
UCSC; RGD:620079; rat.
CTD; 5514; -.
RGD; 620079; Ppp1r10.
HOGENOM; HOG000049285; -.
HOVERGEN; HBG053646; -.
InParanoid; O55000; -.
KO; K17552; -.
PhylomeDB; O55000; -.
PRO; PR:O55000; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0000785; C:chromatin; ISO:RGD.
GO; GO:0000790; C:nuclear chromatin; IDA:RGD.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
Gene3D; 1.20.930.10; -; 1.
Gene3D; 4.10.1000.10; -; 1.
InterPro; IPR003617; TFIIS/CRSP70_N_sub.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR017923; TFIIS_N.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF08711; Med26; 1.
Pfam; PF00642; zf-CCCH; 1.
SMART; SM00509; TFS2N; 1.
SMART; SM00356; ZnF_C3H1; 1.
SUPFAM; SSF47676; SSF47676; 1.
SUPFAM; SSF90229; SSF90229; 1.
PROSITE; PS51319; TFIIS_N; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Nucleus; Phosphoprotein;
Protein phosphatase inhibitor; Reference proteome; RNA-binding;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 872 Serine/threonine-protein phosphatase 1
regulatory subunit 10.
/FTId=PRO_0000071515.
DOMAIN 73 147 TFIIS N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00649}.
ZN_FING 838 866 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 348 Interaction with TOX4. {ECO:0000250}.
REGION 357 433 Necessary for interaction with PPP1CA.
{ECO:0000269|PubMed:9461602}.
REGION 382 450 Essential for PPP1CA inhibition.
REGION 393 408 Necessary for interaction with PPP1CC.
{ECO:0000250}.
REGION 418 619 Interaction with WDR82. {ECO:0000250}.
MOTIF 420 423 PP1-binding motif.
COMPBIAS 304 310 Poly-Lys.
COMPBIAS 540 836 Gly-rich.
MOD_RES 313 313 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 398 398 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:12574161}.
MOD_RES 545 545 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 665 665 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 693 693 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96QC0}.
MOD_RES 737 737 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q80W00}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96QC0}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96QC0}.
MUTAGEN 396 396 R->A: Does not abolish interaction with
PPP1CA and does not reduce PPP1CA
inhibition.
{ECO:0000269|PubMed:12574161}.
MUTAGEN 397 397 K->A: Does not abolish interaction with
PPP1CA and reduces a little PPP1CA
inhibition.
{ECO:0000269|PubMed:12574161}.
MUTAGEN 399 399 V->A: Reduces interaction with PPP1CA and
reduces strongly PPP1CA inhibition.
{ECO:0000269|PubMed:12574161}.
MUTAGEN 401 401 W->A: Abolishes interaction with PPP1CA
and PPP1CA inhibition.
{ECO:0000269|PubMed:12574161}.
MUTAGEN 445 450 Missing: Abolishes PPP1CA inhibition.
{ECO:0000269|PubMed:12574161}.
HELIX 404 406 {ECO:0000244|PDB:4MP0}.
STRAND 407 413 {ECO:0000244|PDB:4MP0}.
SEQUENCE 872 AA; 92828 MW; 23CC61B4B296E948 CRC64;
MGSGPIDPKE LLKGLDSFLT RDGEVKSVDG IAKIFSLMKE ARKMVSRCTY LNIILQTRAP
EVLVKFIDVG GYKLLNSWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KEEGKSRTTL PERPLTEVKA
ETRAEEAPEK KKEKPKSLRT TAPSHAKFRS TGLELDTPSL VPVKKNSSTV VVSDKYNLKP
IPLKRQSATA APGDAAPPAE KKYKPLNTTP NTTKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP AAPAEPMDTD RPGTPVPAVE
VPELMDAASS EPGALDAKPV ESPGDPNQLT RKGRKRKTVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVIPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECAMDE TPYVETLEPG
GSGGSPDGAG GSKLPPVLAN LMGSMGAGKS PQGPGGGGIN VQEILTSIMG SPNNHPSEEL
LKQPDYSDKL KQMLVPHGLL GPGPVANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PVGPRLLGPP PPSRGGDPFW DGPGDPMRGG PMRGGPGPGP GPYHRGRGGR GGNEPPPPPP
FRGARGGRSG GGPPNGRGGP GGGGMVGGGG HRPHEGPGGS MGSGHRSHEG PGGSMGSGHR
SHEGPGHGGP HGHRPHDVPS HRGHDHRGPP PHEHRGHDGH GGGGHRGHDG GHSHGGDMSN
RPVCRHFMMK GNCRYENNCA FYHPGVNGPP LP


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