ETV4_MOUSE
ID ETV4_MOUSE Reviewed; 485 AA.
AC P28322; Q3UMZ6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=ETS translocation variant 4;
DE AltName: Full=Polyomavirus enhancer activator 3;
DE Short=Protein PEA3;
GN Name=Etv4; Synonyms=Pea-3, Pea3;
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] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1547944; DOI=10.1101/gad.6.3.481;
RA Xin J.-H., Cowie A., Lachance P., Hassell J.A.;
RT "Molecular cloning and characterization of PEA3, a new member of the Ets
RT oncogene family that is differentially expressed in mouse embryonic
RT cells.";
RL Genes Dev. 6:481-496(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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).
CC -!- FUNCTION: Transcriptional activator (PubMed:1547944). May play a role
CC in keratinocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:P43268, ECO:0000269|PubMed:1547944}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28322-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28322-2; Sequence=VSP_047943, VSP_047944, VSP_047945;
CC -!- TISSUE SPECIFICITY: Epididymis and brain. {ECO:0000269|PubMed:1547944}.
CC -!- PTM: Sumoylated; enhanced upon ERK/MAP kinase pathway activation it
CC positively regulates the transcriptional activator capacity.
CC Sumoylation at Lys-95 probably requires phosphorylation at Ser-100.
CC Transiently polysumoylated and desumoylated by SENP1. Sumoylation is a
CC prerequisite to polyubiquitination which in turn increases proteasomal-
CC mediated degradation. Probably polyubiquitinated by RNF4 and
CC deubiquitinated by USP2. {ECO:0000250|UniProtKB:P43268}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; X63190; CAA44872.1; -; mRNA.
DR EMBL; AK144590; BAE25952.1; -; mRNA.
DR EMBL; AL591436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48937.1; -. [P28322-1]
DR PIR; S24061; S24061.
DR RefSeq; NP_032841.2; NM_008815.3. [P28322-1]
DR AlphaFoldDB; P28322; -.
DR SMR; P28322; -.
DR BioGRID; 202104; 3.
DR DIP; DIP-60466N; -.
DR IntAct; P28322; 1.
DR STRING; 10090.ENSMUSP00000017868; -.
DR iPTMnet; P28322; -.
DR PhosphoSitePlus; P28322; -.
DR MaxQB; P28322; -.
DR PaxDb; P28322; -.
DR PRIDE; P28322; -.
DR ProteomicsDB; 267664; -. [P28322-1]
DR ProteomicsDB; 267665; -. [P28322-2]
DR Antibodypedia; 890; 317 antibodies from 37 providers.
DR DNASU; 18612; -.
DR Ensembl; ENSMUST00000164750; ENSMUSP00000129261; ENSMUSG00000017724. [P28322-1]
DR GeneID; 18612; -.
DR KEGG; mmu:18612; -.
DR UCSC; uc007lpt.1; mouse. [P28322-1]
DR CTD; 2118; -.
DR MGI; MGI:99423; Etv4.
DR VEuPathDB; HostDB:ENSMUSG00000017724; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000158142; -.
DR InParanoid; P28322; -.
DR OrthoDB; 536648at2759; -.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR BioGRID-ORCS; 18612; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Etv4; mouse.
DR PRO; PR:P28322; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P28322; protein.
DR Bgee; ENSMUSG00000017724; Expressed in secondary palate and 186 other tissues.
DR ExpressionAtlas; P28322; baseline and differential.
DR Genevisible; P28322; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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:0060444; P:branching involved in mammary gland duct morphogenesis; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR006715; ETS_PEA3_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF04621; ETS_PEA3_N; 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 2: Evidence at transcript level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..485
FT /note="ETS translocation variant 4"
FT /id="PRO_0000204117"
FT DNA_BIND 342..422
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 79..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50549"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43268"
FT VAR_SEQ 1
FT /note="M -> MTKSSNHNCLLRPENKPGLWGPGAQAASLRPSPATLVVSSPGHAEHP
FT PAAPAQTPGPQVSASARGPGPVAGGSGRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1547944"
FT /id="VSP_047943"
FT VAR_SEQ 86
FT /note="S -> LA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1547944"
FT /id="VSP_047944"
FT VAR_SEQ 127..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1547944"
FT /id="VSP_047945"
FT CONFLICT 316
FT /note="E -> K (in Ref. 1; CAA44872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54008 MW; 3A5FF4EFD7E828EF CRC64;
MERRMKGGYL DQRVPYTFCS KSPGNGSLGE ALMVPQGKLM DPGSLPPSDS EDLFQDLSHF
QETWLAEAQV PDSDEQFVPD FHSENSFHSP TTRIKKEPQS PRTDPALSCS RKPPLPYHHG
EQCLYSSAYD SPRQIAIKSP APGAPGQSPL QPFSRAEQQQ SLLRASSSSQ SHPGHGYLGE
HSSVFQQPVD MCHSFTSPQG GGREPLPAPY QHQLSEPCPP YPQQNFKQEY HDPLYEQAGQ
PASSQGGVSG HRYPGAGVVI KQERTDFAYD SDVPGCASMY LHPEGFSGPS PGDGVMGYGY
EKSLRPFPDD VCIVPEKFEG DIKQEGIGAF REGPPYQRRG ALQLWQFLVA LLDDPTNAHF
IAWTGRGMEF KLIEPEEVAR LWGIQKNRPA MNYDKLSRSL RYYYEKGIMQ KVAGERYVYK
FVCEPEALFS LAFPDNQRPA LKAEFDRPVS EEDTVPLSHL DESPAYLPEL TGPAPPFGHR
GGYSY
