ID   ZGPAT_SHEEP             Reviewed;         513 AA.
AC   C5IJB0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN   Name=ZGPAT;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liu G.Y., Ge C.R.;
RT   "ZGPAT zinc finger, CCCH-type with G patch domain.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription repressor that specifically binds the 5'-
CC       GGAG[GA]A[GA]A-3' consensus sequence. Represses transcription by
CC       recruiting the chromatin multiprotein complex NuRD to target promoters.
CC       Negatively regulates expression of EGFR, a gene involved in cell
CC       proliferation, survival and migration. Its ability to repress genes of
CC       the EGFR pathway suggest it may act as a tumor suppressor (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CHD4/Mi-2; the interaction is direct.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; FJ943995; ACR46650.1; -; mRNA.
DR   RefSeq; NP_001155206.1; NM_001161734.1.
DR   AlphaFoldDB; C5IJB0; -.
DR   SMR; C5IJB0; -.
DR   STRING; 9940.ENSOARP00000010858; -.
DR   Ensembl; ENSOART00020018345; ENSOARP00020015177; ENSOARG00020012012.
DR   GeneID; 100302028; -.
DR   KEGG; oas:100302028; -.
DR   CTD; 84619; -.
DR   eggNOG; KOG2185; Eukaryota.
DR   OrthoDB; 1238995at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   CDD; cd04508; TUDOR; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR043560; ZGPAT.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR46297; PTHR46297; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF18044; zf-CCCH_4; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; SSF90229; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..513
FT                   /note="Zinc finger CCCH-type with G patch domain-containing
FT                   protein"
FT                   /id="PRO_0000385192"
FT   DOMAIN          315..361
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   ZN_FING         176..202
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          92..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N5A5"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDM1"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDM1"
SQ   SEQUENCE   513 AA;  55345 MW;  D50F13E8818BD486 CRC64;
     MDEESLQTAL RTYDAQLQQV ELALGAGLDP SELADLRQLQ GDLKELIELT EASLVSIRKS
     KLLAALDGER PVQEDAEPLA FQNAIVETAE VPVAPGAELE TVPSRETGPG PTEPGQEEDD
     GEDEEGGAAL SGRKVNAPYY SAWGTLEYHN AMVVGTEEAD DGSPGVRVLY LYPTHKSLKP
     CPFFLEGKCR FQENCRFSHG QVVSVDELRP FQDPDLSSLQ AGSACLAKRQ DGLWYPARIT
     DVDSGYYTVK FDSLLLKEAV VEGDSILPPL RTDPAGSSDS DGSDADDPSY ARVVEPGAAN
     PGTCSSAFAG WEVHTRGIGS RLLAKMGYEF GKGLGRRADG RVEPVHAVVL PRGKSLDQCA
     EILQKRTRAG QAGVSKPPKC RSRGSGPGGR PPPRSVFDFL NEKLKGGAPG APEVGAAPPG
     RSGKEVYHAS RSTKRALSLR LLQTEEKIEQ TQRAIRGIQE ALARNAGRHS VTTTQLQEKL
     AGAQRQLGQL RAQEAGLQRE QRKADTHKKM TEF