ID   ZGPAT_SALSA             Reviewed;         527 AA.
AC   C0HAV3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Zinc finger CCCH-type with G patch domain-containing protein;
GN   Name=zgpat;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; BT059459; ACN11172.1; -; mRNA.
DR   RefSeq; NP_001167239.1; NM_001173768.1.
DR   AlphaFoldDB; C0HAV3; -.
DR   SMR; C0HAV3; -.
DR   STRING; 8030.ENSSSAP00000040697; -.
DR   GeneID; 100380483; -.
DR   KEGG; sasa:100380483; -.
DR   CTD; 84619; -.
DR   OMA; QYTRGIG; -.
DR   OrthoDB; 1238995at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   Bgee; ENSSSAG00000044761; Expressed in zone of skin and 15 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   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   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..527
FT                   /note="Zinc finger CCCH-type with G patch domain-containing
FT                   protein"
FT                   /id="PRO_0000385194"
FT   DOMAIN          317..363
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   ZN_FING         173..200
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          97..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..124
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57908 MW;  43363B5F7E975593 CRC64;
     MDEGTLEAAI TAYSAQLQQV ESALLAGLDP SQQADLLKLK EDLSQLIELT EASLVSVKKS
     RLLATLEEDD GLQSLATGTP ANGGLDNEFA AFYSEVGEVS GSSSDMRERE DEREEEDDGE
     VEGEVDALSG TKVRAPYRTS WGTLEYHNAM IVGTESCDRN EAQVRVLYVH PTQKSMKPCP
     FFLEDKCRFA DNCRFSHGEV VYVSELREFL ESDLTNLQEG SSCLARQDDG IWYSGKITDI
     DNDFYTVKFD SALLKNVMVE ADGVIPPLRE DDLPSCSDSE DDDNGEGEAA FPRVLTQEED
     WAPSRSSSAF GGWEAHTRGI GSKLMLKMGY EYGKGLGKTS EGRVEPVLAV VLPKGKSLDQ
     CAELTARKTQ RKVAKGKDGQ QVSRNKRTRK ARAHNTGGCH NVFDFLNRKL GNGDANPEAG
     GTCGPPPSHT PSSQGAGVEA YKGGKSTKRN LNVKLFQAAE RVAQTEREIQ RLTESLSRRT
     GRDSSMVTHL EEKLSAARSL LVQQKAQELS AQRENRKADT HKKMTEF