PP1RA_RAT
ID PP1RA_RAT Reviewed; 872 AA.
AC O55000; Q6MG09;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
DE AltName: Full=MHC class I region proline-rich protein CAT53;
DE AltName: Full=Phosphatase 1 nuclear targeting subunit;
DE Short=Protein PNUTS;
GN Name=Ppp1r10; Synonyms=Cat53, Pnuts;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PPP1CA INHIBITION, INTERACTION WITH
RP PPP1CA, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=9461602; DOI=10.1074/jbc.273.7.4089;
RA Allen P.B., Kwon Y.G., Nairn A.C., Greengard P.;
RT "Isolation and characterization of PNUTS, a putative protein phosphatase 1
RT nuclear targeting subunit.";
RL J. Biol. Chem. 273:4089-4095(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3]
RP FUNCTION IN PPP1CA INHIBITION, IDENTIFICATION IN A COMPLEX WITH PPP1CA AND
RP RNA HOMOPOLYMERS, PHOSPHORYLATION AT THR-398, MUTAGENESIS OF ARG-396;
RP LYS-397; VAL-399; TRP-401 AND 445-GLU--LEU-450, DNA-BINDING, RNA-BINDING,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12574161; DOI=10.1074/jbc.m209621200;
RA Kim Y.M., Watanabe T., Allen P.B., Kim Y.M., Lee S.J., Greengard P.,
RA Nairn A.C., Kwon Y.G.;
RT "PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit.
RT Characterization of its PP1- and RNA-binding domains and regulation by
RT phosphorylation.";
RL J. Biol. Chem. 278:13819-13828(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-382 AND SER-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1
CC phosphatase complex by providing a binding platform to each component
CC of the complex. The PTW/PP1 phosphatase complex plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. Mediates interaction of WDR82
CC and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has
CC inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA,
CC single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
CC {ECO:0000269|PubMed:12574161, ECO:0000269|PubMed:9461602}.
CC -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts
CC with PPP1CC. Interacts with PPP1CA, WDR82 and TOX4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC Note=Found in discrete nucleoplasmic bodies and within nucleoli.
CC Associates with chromatin during interphase, excluded from condensed
CC chromosomes during early mitosis and is reloaded onto chromosomes at
CC the late telophase (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, brain and intestine (at
CC protein level). Highly expressed in testis.
CC {ECO:0000269|PubMed:12574161, ECO:0000269|PubMed:9461602}.
CC -!- PTM: Phosphorylated on Thr-398 by PKA within the region necessary for
CC interaction with PPP1CA. {ECO:0000269|PubMed:12574161}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE84038.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF040954; AAB96775.1; -; mRNA.
DR EMBL; BX883048; CAE84038.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_075240.1; NM_022951.2.
DR PDB; 4MOY; X-ray; 2.20 A; B=393-433.
DR PDB; 4MP0; X-ray; 2.10 A; B/D=394-433.
DR PDB; 6VTI; NMR; -; A=1-148.
DR PDB; 7LQT; NMR; -; A=1-148.
DR PDBsum; 4MOY; -.
DR PDBsum; 4MP0; -.
DR PDBsum; 6VTI; -.
DR PDBsum; 7LQT; -.
DR AlphaFoldDB; O55000; -.
DR BMRB; O55000; -.
DR SMR; O55000; -.
DR STRING; 10116.ENSRNOP00000001053; -.
DR iPTMnet; O55000; -.
DR PhosphoSitePlus; O55000; -.
DR jPOST; O55000; -.
DR PRIDE; O55000; -.
DR Ensembl; ENSRNOT00000088836; ENSRNOP00000082809; ENSRNOG00000059268.
DR GeneID; 65045; -.
DR KEGG; rno:65045; -.
DR UCSC; RGD:620079; rat.
DR CTD; 5514; -.
DR RGD; 620079; Ppp1r10.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR GeneTree; ENSGT00940000159263; -.
DR InParanoid; O55000; -.
DR OrthoDB; 999354at2759; -.
DR PhylomeDB; O55000; -.
DR PRO; PR:O55000; -.
DR Proteomes; UP000002494; Chromosome 20.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:RGD.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; ISO:RGD.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:RGD.
DR DisProt; DP01202; -.
DR Gene3D; 1.20.930.10; -; 1.
DR IDEAL; IID50266; -.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..872
FT /note="Serine/threonine-protein phosphatase 1 regulatory
FT subunit 10"
FT /id="PRO_0000071515"
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT ZN_FING 838..866
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..348
FT /note="Interaction with TOX4"
FT /evidence="ECO:0000250"
FT REGION 147..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..433
FT /note="Necessary for interaction with PPP1CA"
FT /evidence="ECO:0000269|PubMed:9461602"
FT REGION 382..450
FT /note="Essential for PPP1CA inhibition"
FT REGION 393..408
FT /note="Necessary for interaction with PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 418..619
FT /note="Interaction with WDR82"
FT /evidence="ECO:0000250"
FT REGION 534..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 420..423
FT /note="PP1-binding motif"
FT COMPBIAS 151..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 398
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:12574161"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 665
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 693
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 737
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q80W00"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MUTAGEN 396
FT /note="R->A: Does not abolish interaction with PPP1CA and
FT does not reduce PPP1CA inhibition."
FT /evidence="ECO:0000269|PubMed:12574161"
FT MUTAGEN 397
FT /note="K->A: Does not abolish interaction with PPP1CA and
FT reduces a little PPP1CA inhibition."
FT /evidence="ECO:0000269|PubMed:12574161"
FT MUTAGEN 399
FT /note="V->A: Reduces interaction with PPP1CA and reduces
FT strongly PPP1CA inhibition."
FT /evidence="ECO:0000269|PubMed:12574161"
FT MUTAGEN 401
FT /note="W->A: Abolishes interaction with PPP1CA and PPP1CA
FT inhibition."
FT /evidence="ECO:0000269|PubMed:12574161"
FT MUTAGEN 445..450
FT /note="Missing: Abolishes PPP1CA inhibition."
FT /evidence="ECO:0000269|PubMed:12574161"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6VTI"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:6VTI"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:4MP0"
FT STRAND 407..413
FT /evidence="ECO:0007829|PDB:4MP0"
SQ 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
