ZGPAT_BOVIN
ID ZGPAT_BOVIN Reviewed; 513 AA.
AC Q17QX2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN Name=ZGPAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) 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; BC118131; AAI18132.1; -; mRNA.
DR RefSeq; NP_001019685.2; NM_001024514.2.
DR RefSeq; XP_010809737.1; XM_010811435.1.
DR AlphaFoldDB; Q17QX2; -.
DR SMR; Q17QX2; -.
DR STRING; 9913.ENSBTAP00000042610; -.
DR PaxDb; Q17QX2; -.
DR PRIDE; Q17QX2; -.
DR Ensembl; ENSBTAT00000009860; ENSBTAP00000009860; ENSBTAG00000007498.
DR Ensembl; ENSBTAT00000045200; ENSBTAP00000042610; ENSBTAG00000007498.
DR GeneID; 510866; -.
DR KEGG; bta:510866; -.
DR CTD; 84619; -.
DR VEuPathDB; HostDB:ENSBTAG00000007498; -.
DR VGNC; VGNC:57036; ZGPAT.
DR eggNOG; KOG2185; Eukaryota.
DR GeneTree; ENSGT00390000000732; -.
DR HOGENOM; CLU_040504_1_0_1; -.
DR InParanoid; Q17QX2; -.
DR OMA; QYTRGIG; -.
DR OrthoDB; 1238995at2759; -.
DR TreeFam; TF105970; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000007498; Expressed in ileocecal valve and 104 other tissues.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
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 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR043560; ZGPAT.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR46297; PTHR46297; 1.
DR Pfam; PF01585; G-patch; 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_0000385190"
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 90..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..296
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 492..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; 55285 MW; A27A89B3A6AD4594 CRC64;
MDEESLQTAL RTYDAQLQQV ELALGAGLDP SELADLRQLQ GDLKELIELT EASLVSVRKS
KLLAALDGER PAQEDAEPLA LQNAIAETAE VPVAPGAELE TVPSRETGPG PTERGQEEDD
GEDEEGGAAL SGRKVNAPYY SAWGTLEYHN AMIVGTEEAD DGSPGVRVLY LYPTHKSLKP
CSFFLEGKCR FQENCRFSHG QVVSVDELRP FQDPDLSSLQ AGSACLAKRQ DGLWYPARIT
DVDSGYYTVK FDSLLLKETV VEGDSILPPL RTEPAGSSDS DGSDADDPSY ARVVEPGAAN
PGTCSSAFAG WEVHTRGIGS RLLAKMGYEF GKGLGRHAEG RVEPVHAVVL PRGKSLDQCA
EILQKRTRAG QAGVSKPPKC RSRGSGPGGR PPPRSVFDFL NEKLKGGAPG APEVGAAPPG
RSGKEVYHAS RSTKRALSLR LLQTEEKIEQ TQRAIRGIQE ALARNAGRHS VTTAQLQEKL
AGAQQQLGQL RAQEAGLQRE QRKADTHKKM TEF
