PP1RA_PIG
ID PP1RA_PIG Reviewed; 925 AA.
AC Q767K9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Protein FB19;
GN Name=PPP1R10; Synonyms=CAT53, FB19;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14673549; DOI=10.1007/s00251-003-0627-0;
RA Shigenari A., Ando A., Renard C., Chardon P., Shiina T., Kulski J.K.,
RA Yasue H., Inoko H.;
RT "Nucleotide sequencing analysis of the swine 433-kb genomic segment located
RT between the non-classical and classical SLA class I gene clusters.";
RL Immunogenetics 55:695-705(2004).
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 (By
CC similarity). {ECO:0000250}.
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 -!- PTM: Phosphorylated on Thr-398 by PKA within the region necessary for
CC interaction with PPP1CA. {ECO:0000250}.
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DR EMBL; AB113357; BAD08440.1; -; Genomic_DNA.
DR RefSeq; NP_001116637.1; NM_001123165.1.
DR RefSeq; XP_005653508.1; XM_005653451.2.
DR RefSeq; XP_005653509.1; XM_005653452.2.
DR RefSeq; XP_013852018.1; XM_013996564.1.
DR AlphaFoldDB; Q767K9; -.
DR BMRB; Q767K9; -.
DR SMR; Q767K9; -.
DR STRING; 9823.ENSSSCP00000030807; -.
DR PaxDb; Q767K9; -.
DR PeptideAtlas; Q767K9; -.
DR PRIDE; Q767K9; -.
DR Ensembl; ENSSSCT00000034462; ENSSSCP00000030807; ENSSSCG00000001347.
DR Ensembl; ENSSSCT00015044433; ENSSSCP00015017555; ENSSSCG00015033554.
DR Ensembl; ENSSSCT00015044482; ENSSSCP00015017576; ENSSSCG00015033554.
DR Ensembl; ENSSSCT00015044662; ENSSSCP00015017662; ENSSSCG00015033554.
DR Ensembl; ENSSSCT00015044827; ENSSSCP00015017739; ENSSSCG00015033554.
DR Ensembl; ENSSSCT00030086221; ENSSSCP00030039756; ENSSSCG00030061672.
DR Ensembl; ENSSSCT00035085784; ENSSSCP00035035710; ENSSSCG00035063785.
DR Ensembl; ENSSSCT00040097159; ENSSSCP00040043298; ENSSSCG00040070742.
DR Ensembl; ENSSSCT00045068536; ENSSSCP00045048772; ENSSSCG00045039371.
DR Ensembl; ENSSSCT00055061061; ENSSSCP00055048952; ENSSSCG00055030634.
DR Ensembl; ENSSSCT00060069516; ENSSSCP00060029940; ENSSSCG00060051078.
DR GeneID; 100144450; -.
DR KEGG; ssc:100144450; -.
DR CTD; 5514; -.
DR VGNC; VGNC:91717; PPP1R10.
DR eggNOG; ENOG502QQ2I; Eukaryota.
DR GeneTree; ENSGT00940000159263; -.
DR HOGENOM; CLU_019410_0_0_1; -.
DR InParanoid; Q767K9; -.
DR OMA; MGKNCKY; -.
DR OrthoDB; 999354at2759; -.
DR TreeFam; TF105541; -.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000001347; Expressed in granulosa cell and 42 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; IBA:GO_Central.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.20.930.10; -; 1.
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 3: Inferred from homology;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome;
KW RNA-binding; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..925
FT /note="Serine/threonine-protein phosphatase 1 regulatory
FT subunit 10"
FT /id="PRO_0000071514"
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT ZN_FING 891..919
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..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..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:0000250"
FT REGION 382..450
FT /note="Essential for PPP1CA inhibition"
FT /evidence="ECO:0000250"
FT REGION 388..417
FT /note="Necessary for interaction with PPP1CA"
FT /evidence="ECO:0000250"
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 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..890
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..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 398
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O55000"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 668
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 696
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96QC0"
FT MOD_RES 741
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"
SQ SEQUENCE 925 AA; 97596 MW; A8A88BD030E48682 CRC64;
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP
EILVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KEEGKSRTTP PERPLTEVKA
ETRAEEAPEK KREKPKSLRT TAPSHAKFRS TGLELETPSL VPVKKNASAV VVSDKYNLKP
IPLKRQSSIA ALGDAAPPAE KKYKPLNTTP NATKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP STAKPSSPEP APPSEAMDTD RPGTPVPPVE
VPELMDTASL EPGALDAKPV ESPGDPSQLT RKGRKRKTVT WPEEGKLREY FYFELDETER
VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVTPGSNS
QERYIQAERE KGILQELFLN KESPHEPDPE PYEPVPPKLI PLDEECSMDE TPYVETLEPG
GAGGSPDGAG GSKLPPVLAN LMGSMGAGKS PQGPGGGGIN VQEILTSIMG SPNSHPSEEL
LKQPDYSDKI KQMLVPHGLL GPGPIANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
PGGPVGPRLL GPPPPPRGGD PFWDGPGDPM RGGPMRGGPG PGPGPYHRGR GGRGGNEPPP
PPPPFRGARG GRSGGGPPNG RGGPGGGMVG GGGHRPHEGP GGGMSSGSGH RPHEGPGGGM
GGGHRPHEGP GGGMGGGHRP HEGPGGGMGG GSGHRPHEGP GGGMGAGGGH RPHEGPGHGG
PHGHRPHDVP GHRGHDHRGP PPHEHRGHDG PGHGGGGHRG HDGGHNHGGD MSKRPVCRHF
MMKGNCRYEN NCAFYHPGVN GPPLP
