ELF4_MOUSE
ID ELF4_MOUSE Reviewed; 655 AA.
AC Q9Z2U4; B1AY67;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=ETS-related transcription factor Elf-4;
DE AltName: Full=E74-like factor 4;
DE AltName: Full=Myeloid Elf-1-like factor;
GN Name=Elf4 {ECO:0000312|MGI:MGI:1928377};
GN Synonyms=Mef {ECO:0000312|EMBL:AAD01601.1};
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] {ECO:0000312|EMBL:AAD01601.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miyazaki Y., De Blasio T., Nimer S.D.;
RT "Murine MEF (myeloid elf-1-like factor) cDNA clone.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=12387738; DOI=10.1016/s1074-7613(02)00422-3;
RA Lacorazza H.D., Miyazaki Y., Di Cristofano A., Deblasio A., Hedvat C.,
RA Zhang J., Cordon-Cardo C., Mao S., Pandolfi P.P., Nimer S.D.;
RT "The ETS protein MEF plays a critical role in perforin gene expression and
RT the development of natural killer and NK-T cells.";
RL Immunity 17:437-449(2002).
RN [4]
RP FUNCTION.
RX PubMed=19380490; DOI=10.1128/mcb.01551-08;
RA Sashida G., Liu Y., Elf S., Miyata Y., Ohyashiki K., Izumi M., Menendez S.,
RA Nimer S.D.;
RT "ELF4/MEF activates MDM2 expression and blocks oncogene-induced p16
RT activation to promote transformation.";
RL Mol. Cell. Biol. 29:3687-3699(2009).
RN [5]
RP FUNCTION.
RX PubMed=19412182; DOI=10.1038/ni.1730;
RA Yamada T., Park C.S., Mamonkin M., Lacorazza H.D.;
RT "Transcription factor ELF4 controls the proliferation and homing of CD8+ T
RT cells via the Kruppel-like factors KLF4 and KLF2.";
RL Nat. Immunol. 10:618-626(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Transcriptional activator that binds to DNA sequences
CC containing the consensus 5'-WGGA-3'. Transactivates promoters of the
CC hematopoietic growth factor genes CSF2, IL3, IL8, and of LYZ. Acts
CC synergistically with RUNX1 to transactivate the IL3 promoter (By
CC similarity). Also transactivates the PRF1 promoter in natural killer
CC (NK) cells. Plays a role in the development and function of NK and NK
CC T-cells and in innate immunity. Controls the proliferation and homing
CC of CD8+ T-cells via the Kruppel-like factors KLF4 and KLF2. Controls
CC cell senescence in a p53-dependent manner. Can also promote cellular
CC transformation through inhibition of the p16 pathway. {ECO:0000250,
CC ECO:0000269|PubMed:12387738, ECO:0000269|PubMed:19380490,
CC ECO:0000269|PubMed:19412182}.
CC -!- SUBUNIT: Interacts with RUNX1 (via the Runt domain); the interaction
CC transactivates the IL3 promoter. Interacts (via its C-terminus) with
CC PML; the interaction translocates ELF4 to PML nuclear bodies and
CC enhances transactivation of LYZ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}.
CC Note=Accumulation into PML nuclear bodies is mediated by PML.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
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DR EMBL; AF016714; AAD01601.1; -; mRNA.
DR EMBL; AL844594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30108.1; -.
DR RefSeq; NP_062654.2; NM_019680.2.
DR RefSeq; XP_006541589.1; XM_006541526.2.
DR RefSeq; XP_006541590.1; XM_006541527.1.
DR AlphaFoldDB; Q9Z2U4; -.
DR SMR; Q9Z2U4; -.
DR BioGRID; 208021; 1.
DR STRING; 10090.ENSMUSP00000110608; -.
DR iPTMnet; Q9Z2U4; -.
DR PhosphoSitePlus; Q9Z2U4; -.
DR EPD; Q9Z2U4; -.
DR jPOST; Q9Z2U4; -.
DR MaxQB; Q9Z2U4; -.
DR PaxDb; Q9Z2U4; -.
DR PRIDE; Q9Z2U4; -.
DR ProteomicsDB; 275740; -.
DR Antibodypedia; 16200; 392 antibodies from 30 providers.
DR DNASU; 56501; -.
DR Ensembl; ENSMUST00000033429; ENSMUSP00000033429; ENSMUSG00000031103.
DR Ensembl; ENSMUST00000114958; ENSMUSP00000110608; ENSMUSG00000031103.
DR GeneID; 56501; -.
DR KEGG; mmu:56501; -.
DR UCSC; uc009tce.2; mouse.
DR CTD; 2000; -.
DR MGI; MGI:1928377; Elf4.
DR VEuPathDB; HostDB:ENSMUSG00000031103; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000161870; -.
DR HOGENOM; CLU_027279_1_0_1; -.
DR InParanoid; Q9Z2U4; -.
DR OMA; IVEQLPC; -.
DR OrthoDB; 837296at2759; -.
DR PhylomeDB; Q9Z2U4; -.
DR TreeFam; TF318679; -.
DR BioGRID-ORCS; 56501; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Elf4; mouse.
DR PRO; PR:Q9Z2U4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2U4; protein.
DR Bgee; ENSMUSG00000031103; Expressed in granulocyte and 100 other tissues.
DR ExpressionAtlas; Q9Z2U4; baseline and differential.
DR Genevisible; Q9Z2U4; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR GO; GO:0001787; P:natural killer cell proliferation; IDA:UniProtKB.
DR GO; GO:0001866; P:NK T cell proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR033070; Elf4.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR022084; TF_Elf_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF170; PTHR11849:SF170; 1.
DR Pfam; PF12310; Elf-1_N; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..655
FT /note="ETS-related transcription factor Elf-4"
FT /id="PRO_0000204090"
FT DNA_BIND 208..290
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 86..205
FT /note="RUNX1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q99607"
FT REGION 136..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99607"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99607"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99607"
FT CONFLICT 132
FT /note="N -> K (in Ref. 1; AAD01601)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="T -> A (in Ref. 1; AAD01601)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="N -> S (in Ref. 1; AAD01601)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="Q -> A (in Ref. 1; AAD01601)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="S -> T (in Ref. 1; AAD01601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 70800 MW; 44CAFA1D3D77153C CRC64;
MAIALQPSDL VFEFASNGMD DIHQLEDPSV FPAVIVEQVP YPELVHLCSG LDLDEVHNGI
IRDRTLCMTQ DQILEGSILL TDDDVSTSNN VSSTEVLFNV ATPSDVLDEK QIFSSPEVLS
DSNSVQAINL PNFLLSTPEP DDLKKTSDAG DQKEHSEEEK VSREENLRKM GKARKRNRKT
KNNRSTSPVT DPSMPIRKKS KDGKGSTIYL WEFLLALLQD RNTCPKYIKW TQREKGIFKL
VDSKAVSKLW GKQKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK EMPKDLVVID
DEEESPETPE DSSQASTSST PSTSTIRRAS SRVGTRASPE DKDNPPWEKP KVQHTGLQPS
ASLELGLSVD EEVPTTSTML ASPLQSQARL TKTVSSSPAP SNIHLGVAPV GPGSTVTLQT
IPLTTVLTNG PPASTTAPTQ LVLQSVPQVS TFKDTFTLQT SFPLNTNLQE NQVATQGAPL
ILSGLPQLLA GANPQSNPAP SQVIGAGSAG PSSQPPGTVI AAFIRTSSGT SVPVVKEGPL
RSSSYVQGVV TGAPVEGLLV PEETLRELLR DQGHLQPLPS QVLSRGSHNL SLVGNQTLSP
PSHPTVGLTP VAELELSSGS GPLFVTEPSV TRSPTQAPFS PFNPTSLIKM EPQDI
