ZGPAT_RAT
ID ZGPAT_RAT Reviewed; 507 AA.
AC Q5PPF5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN Name=Zgpat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC087720; AAH87720.1; -; mRNA.
DR RefSeq; NP_001009656.1; NM_001009656.1.
DR RefSeq; XP_006235811.1; XM_006235749.1.
DR RefSeq; XP_006235812.1; XM_006235750.2.
DR RefSeq; XP_006235813.1; XM_006235751.2.
DR RefSeq; XP_006235814.1; XM_006235752.3.
DR AlphaFoldDB; Q5PPF5; -.
DR SMR; Q5PPF5; -.
DR STRING; 10116.ENSRNOP00000019084; -.
DR jPOST; Q5PPF5; -.
DR PaxDb; Q5PPF5; -.
DR Ensembl; ENSRNOT00000019084; ENSRNOP00000019084; ENSRNOG00000014235.
DR GeneID; 296478; -.
DR KEGG; rno:296478; -.
DR UCSC; RGD:1310801; rat.
DR CTD; 84619; -.
DR RGD; 1310801; Zgpat.
DR eggNOG; KOG2185; Eukaryota.
DR GeneTree; ENSGT00390000000732; -.
DR HOGENOM; CLU_040504_1_0_1; -.
DR InParanoid; Q5PPF5; -.
DR OMA; QYTRGIG; -.
DR OrthoDB; 1238995at2759; -.
DR PhylomeDB; Q5PPF5; -.
DR PRO; PR:Q5PPF5; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014235; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q5PPF5; RN.
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; ISO:RGD.
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; ISO:RGD.
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:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; 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..507
FT /note="Zinc finger CCCH-type with G patch domain-containing
FT protein"
FT /id="PRO_0000385191"
FT DOMAIN 309..355
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 170..196
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 88..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..507
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 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM1"
FT MOD_RES 276
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM1"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM1"
SQ SEQUENCE 507 AA; 56172 MW; 4E46CB80553378B0 CRC64;
MDEDNLETAL QTYRAQLQQV ELALGAGLDA SEQADLRQLQ GDLKELIELT EASLLSVRKS
KLLSTVDQEH QEDAEYLAFQ KAIAEEAPVD PGNDSKTVPG SEVQPTPTSS ALEEEEEDPD
LEDLSGAKVN APYYSAWGTL EYHNAMVVGA EEAEDGSACV RVLYLYPTHK SLKPCPFFLE
GKCRFKENCR FSHGQLVSVD ELRPFQDPDL SLLQTGSACL AKHQDGLWHP ARITDVDNGY
YTVKFDSLLL KEAVVEGDSI LPPLRTEATD SSDSDTGDAS DSSYARVVEA NTVDTGTCSS
AFAGWEVHTR GIGSKLLVKM GYEFGKGLGR HAEGRVEPIH AVVLPRGKSL DQCAEILQKK
TKQGQTGASR PPRCRRRSSR PEGRPPPRNV FDFLNEKLQS QVPGTPDAGV DTPERRNKDM
YHASKSAKQA LSLQLFQTEE KIERTQRDIR GIQEALTRNT GRHGMATAHL QEKLEGAQRQ
LGQLRAQEAD LQRKQRKADT HRKMTEF
