ID A0A433SWR0_ELYCH Unreviewed; 978 AA.
AC A0A433SWR0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=EGW08_018501 {ECO:0000313|EMBL:RUS73740.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS73740.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS73740.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS73740.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS73740.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS73740.1}.
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DR EMBL; RQTK01000905; RUS73740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433SWR0; -.
DR STRING; 188477.A0A433SWR0; -.
DR Proteomes; UP000271974; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
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:UP000271974};
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 71..145
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51319"
FT DOMAIN 951..978
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 951..978
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 148..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 106547 MW; 409AFB164E6B8C42 CRC64;
MPPIDPQQLL RALGPLLTDQ GGIKGAQAAL QIASLMKDAS KLVSKCVYLN ILRVTESEEA
FTKFVEVGGW DTLNAWLDVA RTENNSPLLG ELLEVYLRIP VTVALLKQNS AAKTIKKMQG
KTDNDKLKKL STELVDVWMK TIRGQNVGTD ADLDDKKKKK KHKDKDSEKE KDKDYEKDRD
KNHRDSKKGK EEKENNDRHR SRDKDSKERD TQDSNRDRKD RDRHKDKDRS HRDKSKDSSS
KSSSSSSSSS SSQNKHKETI SNSSKKSAAE DSKATSAEKS KSASTEEESH RRLKTVKAIG
SRIRSTGLFD DDEEEMDIVK KPVDKTAAKR ISNLESKGEE SSEKKPRLHL NMPAMSSSGL
TSSTTTPPEI MHGRIKIIPP KKPPAHEIQE SNVFMAALQQ SSSYASFGLK KKKKAASPSV
TTPPVLLRGG SLTTATSPPQ GVQGSVTVSE PGPTSPPLLS PTTAMAQKLP SVPSFYRDTL
EETPDSDKKD AKQEDGRDSP PTLDLMAPLD CQAEPRKEQD MDTSKTDEPL LDFGNAEDFQ
EANVEEPPKS TKPKKRVSWA RESQMEQIFY FEMDENEREN VNRPKSFSDL KREEMMLDRR
AIESGKRFTN DTMVEVLQWK LPKLIDNAIV VVDSGCNSVE RQIQMEREQS VLCALFFNKV
PDTPNEPDPE IPSEEEDIKV IPLEDENGSC TEYEHTYNFN DPSSLPYDPE FGALPLQGQN
PQHGAAGGHL ANGHAGGAGM GGPPPGLHGN LAGQGSGSMG HMMSSLPPGI SHILHVLKQQ
AQETRDPIMQ NLQGMLSNVL QTTNPQDSGM LVDRILNALE PFMNQIPGLS NLINSVKGNG
GMDFPVGGAA GAGAGGPGGR FLGHPAGPGG PMSGGNPRHG LLGSAPPGFN MEAAASGNMR
PPLGMSAGPM SMMNNGGSNF GMGMGGPPPG HWRGGGGGGG RSRPFKRGHH RGNTVCTFFV
KTRNCKYGES CQFLHPNS
//
