ID A0A452DTZ3_CAPHI Unreviewed; 920 AA.
AC A0A452DTZ3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10 {ECO:0000256|ARBA:ARBA00022330};
DE AltName: Full=MHC class I region proline-rich protein CAT53 {ECO:0000256|ARBA:ARBA00032334};
GN Name=PPP1R10 {ECO:0000313|Ensembl:ENSCHIP00000003175.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000003175.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000003175.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000003175.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00025627}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00649}.
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DR EMBL; LWLT01000028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452DTZ3; -.
DR STRING; 9925.ENSCHIP00000003175; -.
DR Ensembl; ENSCHIT00000009600.1; ENSCHIP00000003175.1; ENSCHIG00000007066.1.
DR GeneTree; ENSGT00940000159263; -.
DR OMA; NGPPQIW; -.
DR Proteomes; UP000291000; Chromosome 23.
DR Bgee; ENSCHIG00000007066; Expressed in fallopian tube and 17 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; 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; IEA:Ensembl.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IEA:Ensembl.
DR CDD; cd00183; TFIIS_I; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 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 PANTHER; PTHR46557; SERINE/THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10-RELATED; 1.
DR PANTHER; PTHR46557:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 10; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00649};
KW Protein phosphatase inhibitor {ECO:0000256|ARBA:ARBA00023272};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 73..147
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 886..914
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 886..914
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 147..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 335..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 97193 MW; 4B5E95C7AF70CFF0 CRC64;
MGSGPIDPKE LLKGLDSFLN RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNILLQTRSP
EVLIKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
SKSSDDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KEEGKSRTTP PERPVTEVKA
ETRAEEAPEK KREKPKSLRT TAPSHAKFRS TGLELETPSL VPVKKNASAV VVSDKYNLKP
IPLKRQSSAA APGDAAPPAE KKYKPLNTTP NATKEIKVKI IPPQPMEGLG FLDALNSAPV
PGIKIKKKKK VLSPTAAKPS PFEGKTSTEP SVAKPSSPEP APPEAMDTER PGTPVPPVEV
PELMDTASLE PGALDVKPVE SPSDPSQLTR KGRKRKTVTW PEEGKLREYF YFELDETERV
NVNKIKDFGE AAKREILSDR HAFETARRLS HDNMEEKVPW VCPRPLVLPS PLVTPGSNSQ
ERYIQAEREK GILQELFLNK ESPHEPDPEP YEPIPPKLIP LDEECSMDET PYVETLEPGG
AGGSPDGAGG SKLPPVLANL MGSMGAGKSP QGPGGGGINV QEILTSIMGS PNSHPSEELL
KQADYSDKIK QMLVPHGLLG PGPIANGFPP GGPGAPKGMQ HFPPGPGGPM PGPGGPGGPV
GPRLLGPPPP PRGGDPFWDG PGDPMRGGPM RGGPGPGPGP YHRGRGGRGG NEPPPPPPPF
RGARGGRSGG GPPNGRGGPG GGMVGGGGHR PHEGPGGGMN SGSGHRPHEG PGSGMGGGHR
PHEGPGGSMG GGHRPHEGPG GGMGGGSGHR PHEGPGGGMG AGGGHRPHEG PGHGGPHGHR
PHDVPGHRGH DHRGPPPHEH RGHDGPGHGG GGHRGHDGGH SHGGDMSNRP VCRHFMMKGN
CRYENNCAFY HPGVNGPPLP
//
