ZC3H8_MOUSE
ID ZC3H8_MOUSE Reviewed; 305 AA.
AC Q9JJ48; Q80X92;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger CCCH domain-containing protein 8;
DE AltName: Full=Fetal liver zinc finger protein 1;
GN Name=Zc3h8; Synonyms=Fliz1, Zc3hdc8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Fetal liver;
RX PubMed=11318609; DOI=10.1006/geno.2000.6480;
RA Dahm K., Nielsen P.J., Mueller A.M.;
RT "Transcripts of Fliz1, a nuclear zinc finger protein, are expressed in
RT discrete foci of the murine fetal liver.";
RL Genomics 73:194-202(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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).
RN [3]
RP DNA-BINDING.
RX PubMed=12077251; DOI=10.4049/jimmunol.169.1.248;
RA Hwang E.S., Choi A., Ho I.-C.;
RT "Transcriptional regulation of GATA-3 by an intronic regulatory region and
RT fetal liver zinc finger protein 1.";
RL J. Immunol. 169:248-253(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-91, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the little elongation complex (LEC), a complex
CC required to regulate small nuclear RNA (snRNA) gene transcription by
CC RNA polymerase II and III. Acts as a transcriptional repressor of the
CC GATA3 promoter. Induces thymocyte apoptosis when overexpressed, which
CC may indicate a role in regulation of thymocyte homeostasis (By
CC similarity). Sequence-specific DNA-binding factor that binds to the 5'-
CC AGGTCTC-3' sequence within the negative cis-acting element intronic
CC regulatory region (IRR) of the GATA3 gene. {ECO:0000250}.
CC -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC with ICE1 (via C-terminus domain) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11318609}.
CC Note=Colocalizes with coilin in subnuclear cajal and histone locus
CC bodies. Translocates in the LEC complex to cajal and histone locus
CC bodies at snRNA genes in a ICE1-dependent manner. Associates to
CC transcriptionally active chromatin at snRNA genes (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, muscle, testis, kidney,
CC brain, liver, lung and spleen. {ECO:0000269|PubMed:11318609}.
CC -!- DOMAIN: The N-terminal region and all three C3H1-type zinc fingers are
CC necessary to induce transcriptional repression. {ECO:0000250}.
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DR EMBL; AF061961; AAF74513.1; -; mRNA.
DR EMBL; BC048687; AAH48687.1; -; mRNA.
DR CCDS; CCDS16718.1; -.
DR RefSeq; NP_065619.2; NM_020594.2.
DR AlphaFoldDB; Q9JJ48; -.
DR SMR; Q9JJ48; -.
DR STRING; 10090.ENSMUSP00000028866; -.
DR iPTMnet; Q9JJ48; -.
DR PhosphoSitePlus; Q9JJ48; -.
DR EPD; Q9JJ48; -.
DR MaxQB; Q9JJ48; -.
DR PaxDb; Q9JJ48; -.
DR PRIDE; Q9JJ48; -.
DR ProteomicsDB; 275269; -.
DR Antibodypedia; 47908; 257 antibodies from 30 providers.
DR DNASU; 57432; -.
DR Ensembl; ENSMUST00000028866; ENSMUSP00000028866; ENSMUSG00000027387.
DR GeneID; 57432; -.
DR KEGG; mmu:57432; -.
DR UCSC; uc033hqb.1; mouse.
DR CTD; 84524; -.
DR MGI; MGI:1930128; Zc3h8.
DR VEuPathDB; HostDB:ENSMUSG00000027387; -.
DR eggNOG; KOG1040; Eukaryota.
DR GeneTree; ENSGT00940000161918; -.
DR HOGENOM; CLU_059008_0_0_1; -.
DR InParanoid; Q9JJ48; -.
DR OMA; KWPGTGN; -.
DR OrthoDB; 145192at2759; -.
DR PhylomeDB; Q9JJ48; -.
DR TreeFam; TF318143; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 57432; 15 hits in 74 CRISPR screens.
DR PRO; PR:Q9JJ48; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JJ48; protein.
DR Bgee; ENSMUSG00000027387; Expressed in animal zygote and 189 other tissues.
DR Genevisible; Q9JJ48; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0035363; C:histone locus body; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0033085; P:negative regulation of T cell differentiation in thymus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119; PTHR13119; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; SSF90229; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein level;
KW Apoptosis; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..305
FT /note="Zinc finger CCCH domain-containing protein 8"
FT /id="PRO_0000213904"
FT ZN_FING 205..232
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 234..261
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 262..285
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5P1"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5P1"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N5P1"
FT CONFLICT 124
FT /note="S -> P (in Ref. 1; AAF74513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 34913 MW; BD9473758E576F30 CRC64;
MDFENLFSKP PNPALGKKPA ADPEERIDEI DGTEVEETQT EKVKWKVKRD REQIPKKFKH
LGNAATSPKS LLRKKSRSKD YDPYSDGETC SQGSEDNFDK ELQQYIQAKE MANAAQPSLL
PEESVKKAGA EGTQQTAKQK NKKSKAGHKK VKQKKMKRKW PGTGDKGSRA LLKNSGSREQ
TDEPEEKQPR VRMSQGFINQ HTVERKGKQV CKYFLERKCI KGDQCKFDHD AEIEKKKEMC
KYYVQGYCTK GENCLYLHSE YPCKFYHTGT KCYQGDHCNF SHAPLTAETQ ELLAKVLDTD
KKSCK
