ETV3_MOUSE
ID ETV3_MOUSE Reviewed; 513 AA.
AC Q8R4Z4; G5E907; Q9QZW1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ETS translocation variant 3;
DE AltName: Full=ETS domain transcriptional repressor PE1;
DE Short=PE-1;
DE AltName: Full=Mitogenic Ets transcriptional suppressor;
GN Name=Etv3; Synonyms=Mets, Pe1;
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], AND FUNCTION.
RX PubMed=12007404; DOI=10.1016/s0092-8674(02)00714-6;
RA Klappacher G.W., Lunyak V.V., Sykes D.B., Sawka-Verhelle D., Sage J.,
RA Brard G., Ngo S.D., Gangadharan D., Jacks T., Kamps M.P., Rose D.W.,
RA Rosenfeld M.G., Glass C.K.;
RT "An induced Ets repressor complex regulates growth arrest during terminal
RT macrophage differentiation.";
RL Cell 109:169-180(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=14754893; DOI=10.1074/jbc.m311991200;
RA Sawka-Verhelle D., Escoubet-Lozach L., Fong A.L., Hester K.D., Herzig S.,
RA Lebrun P., Glass C.K.;
RT "PE-1/METS, an antiproliferative Ets repressor factor, is induced by CREB-
RT 1/CREM-1 during macrophage differentiation.";
RL J. Biol. Chem. 279:17772-17784(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10913304; DOI=10.1021/bi000343+;
RA Bidder M., Loewy A.P., Latifi T., Newberry E.P., Ferguson G., Willis D.M.,
RA Towler D.A.;
RT "Ets domain transcription factor PE1 suppresses human interstitial
RT collagenase promoter activity by antagonizing protein-DNA interactions at a
RT critical AP1 element.";
RL Biochemistry 39:8917-8928(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 repressor that contribute to growth arrest
CC during terminal macrophage differentiation by repressing target genes
CC involved in Ras-dependent proliferation. Represses MMP1 promoter
CC activity. {ECO:0000269|PubMed:10913304, ECO:0000269|PubMed:12007404}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; AF218539; AAK56845.1; -; mRNA.
DR EMBL; AY274927; AAQ18663.1; -; Genomic_DNA.
DR EMBL; AF156530; AAF09185.1; -; mRNA.
DR EMBL; AC139241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466547; EDL15354.1; -; Genomic_DNA.
DR EMBL; BC078636; AAH78636.1; -; mRNA.
DR CCDS; CCDS17453.1; -.
DR RefSeq; NP_001076787.1; NM_001083318.2.
DR RefSeq; NP_001273773.1; NM_001286844.1.
DR RefSeq; NP_036181.3; NM_012051.4.
DR AlphaFoldDB; Q8R4Z4; -.
DR SMR; Q8R4Z4; -.
DR BioGRID; 205105; 2.
DR IntAct; Q8R4Z4; 1.
DR STRING; 10090.ENSMUSP00000112915; -.
DR iPTMnet; Q8R4Z4; -.
DR PhosphoSitePlus; Q8R4Z4; -.
DR EPD; Q8R4Z4; -.
DR MaxQB; Q8R4Z4; -.
DR PaxDb; Q8R4Z4; -.
DR PRIDE; Q8R4Z4; -.
DR ProteomicsDB; 275802; -.
DR Antibodypedia; 1438; 65 antibodies from 18 providers.
DR DNASU; 27049; -.
DR Ensembl; ENSMUST00000119109; ENSMUSP00000112915; ENSMUSG00000003382.
DR Ensembl; ENSMUST00000170036; ENSMUSP00000127419; ENSMUSG00000003382.
DR GeneID; 27049; -.
DR KEGG; mmu:27049; -.
DR UCSC; uc008psh.2; mouse.
DR CTD; 2117; -.
DR MGI; MGI:1350926; Etv3.
DR VEuPathDB; HostDB:ENSMUSG00000003382; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160963; -.
DR HOGENOM; CLU_023454_1_0_1; -.
DR InParanoid; Q8R4Z4; -.
DR OMA; GIYPDPH; -.
DR OrthoDB; 677533at2759; -.
DR PhylomeDB; Q8R4Z4; -.
DR TreeFam; TF351065; -.
DR BioGRID-ORCS; 27049; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Etv3; mouse.
DR PRO; PR:Q8R4Z4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R4Z4; protein.
DR Bgee; ENSMUSG00000003382; Expressed in mesenteric lymph node and 248 other tissues.
DR ExpressionAtlas; Q8R4Z4; baseline and differential.
DR Genevisible; Q8R4Z4; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
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:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR032929; ETV3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR PANTHER; PTHR11849:SF30; PTHR11849:SF30; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 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 Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..513
FT /note="ETS translocation variant 3"
FT /id="PRO_0000204115"
FT DNA_BIND 35..116
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 138..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41162"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41162"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P41162"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41162"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P41162"
FT CONFLICT 182
FT /note="G -> R (in Ref. 3; AAF09185)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="H -> R (in Ref. 3; AAF09185)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="M -> I (in Ref. 1; AAK56845, 2; AAQ18663, 3;
FT AAF09185 and 6; AAH78636)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="V -> A (in Ref. 1; AAK56845, 2; AAQ18663, 3;
FT AAF09185 and 6; AAH78636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57026 MW; 67BCFA849A3BF7E3 CRC64;
MKAGCSIVEK PEGGGGYQFP DWAYKAESSP GSRQIQLWHF ILELLQKEEF RHVIAWQQGE
YGEFVIKDPD EVARLWGRRK CKPQMNYDKL SRALRYYYNK RILHKTKGKR FTYKFNFNKL
VMPNYPFINI RSSGVVPQSA PPVPTASSRF HFPPLDSHSP TGDVQPGRFS ASSLSASGPE
SGVTTDRKVE PSDLEDGSAS DWHRGMDFMP SRNALGGGAV GHQKRKPDIL LPLFTRPAMY
PDPHSPFAIS PVPGRGGVLN VPISPALSLT PTMFSYSPSP GLSPFTSSSC FSFNPEEMKH
YLHSQACSVF NYHLSPRTFP RYPGLMVPPL QCQMHPEEPS QFSIKLQPPP AGRKNRERVE
SREEAVRGSV PASAPVPSRI KVEPATEKDP DSLRQSTQGK EEQTQEVDSM RSRTIEEGKG
TGFAHPSPTW PSVSISTPSD EPLEGTEDSE DRSVREPGVP EKKEDALMPP KLRLKRRWND
DPEARELNKT GKFLWNGAGP QGLATTATAA ADA
