ETV5_MOUSE
ID ETV5_MOUSE Reviewed; 510 AA.
AC Q9CXC9; Q3TG49; Q8C0F3; Q9JHB1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ETS translocation variant 5;
GN Name=Etv5;
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].
RC STRAIN=C57BL/6J;
RX PubMed=9285689; DOI=10.1038/sj.onc.1201261;
RA Chotteau-Lelievre A., Desbiens X., Pelczar H., Defossez P.-A.,
RA de Launoit Y.;
RT "Differential expression patterns of the PEA3 group transcription factors
RT through murine embryonic development.";
RL Oncogene 15:937-952(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Lung, and Testis;
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 MRNA].
RC STRAIN=FVB/N; 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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=27280443; DOI=10.1371/journal.pgen.1006104;
RA Williams M.J., Klockars A., Eriksson A., Voisin S., Dnyansagar R.,
RA Wiemerslage L., Kasagiannis A., Akram M., Kheder S., Ambrosi V.,
RA Hallqvist E., Fredriksson R., Schioeth H.B.;
RT "The Drosophila ETV5 homologue Ets96B: molecular link between obesity and
RT bipolar disorder.";
RL PLoS Genet. 12:E1006104-E1006104(2016).
CC -!- FUNCTION: Binds to DNA sequences containing the consensus nucleotide
CC core sequence 5'-GGAA.-3'. {ECO:0000250|UniProtKB:P41161}.
CC -!- SUBUNIT: Interacts (via C-terminal) with ZMYM5 (via N-terminal 120
CC amino acid region). {ECO:0000250|UniProtKB:P41161}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- TISSUE SPECIFICITY: In the brain, expressed predominantly in the
CC cerebral cortex, the amygdala and the hypothalamus. Within the cerebral
CC cortex, there is conspicuously high expression in cortical layers 2, 4
CC and 6 while expression is almost absent from layers 1, 3 and 5. High
CC expression is also observed in the dorsal and ventral endopiriform
CC claustrum. Strong expression is observed in limited parts of the
CC amygdala including the basolateral amygdaloid nucleus, the bed stria
CC terminalis and the central amygdaloid nucleus. Low to moderate levels
CC are found in the hypothalamus while expression is almost absent in the
CC thalamus. Hypothalamic expression is seen in the dorsomedial
CC hypothalamic nucleus and also the central, dorsomedial and
CC ventrolateral parts of the ventromedial hypothalamic nucleus. Strong
CC expression is also identified in the nigrostriatal tract. In the
CC mesencephalon, expression is restricted to the ventral tegmental area
CC including the parabrachial pigmented nucleus. In the hippocampus,
CC strongly expressed in the pyramidal cell layer. Some expression is also
CC found in the lacunosum moleculare layer. Low levels of expression in
CC the cerebellum, including the granular, molecular and Purkinje cell
CC layers. {ECO:0000269|PubMed:27280443}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; AY004174; AAF85761.1; -; mRNA.
DR EMBL; AK018368; BAB31180.1; -; mRNA.
DR EMBL; AK031452; BAC27412.1; -; mRNA.
DR EMBL; AK168881; BAE40699.1; -; mRNA.
DR EMBL; BC034680; AAH34680.1; -; mRNA.
DR CCDS; CCDS37299.1; -.
DR RefSeq; NP_076283.2; NM_023794.2.
DR RefSeq; XP_006521720.1; XM_006521657.3.
DR AlphaFoldDB; Q9CXC9; -.
DR SMR; Q9CXC9; -.
DR BioGRID; 222408; 1.
DR DIP; DIP-60467N; -.
DR IntAct; Q9CXC9; 1.
DR STRING; 10090.ENSMUSP00000078551; -.
DR iPTMnet; Q9CXC9; -.
DR PhosphoSitePlus; Q9CXC9; -.
DR PaxDb; Q9CXC9; -.
DR PRIDE; Q9CXC9; -.
DR ProteomicsDB; 275787; -.
DR Antibodypedia; 34851; 361 antibodies from 34 providers.
DR DNASU; 104156; -.
DR Ensembl; ENSMUST00000079601; ENSMUSP00000078551; ENSMUSG00000013089.
DR GeneID; 104156; -.
DR KEGG; mmu:104156; -.
DR UCSC; uc007yse.1; mouse.
DR CTD; 2119; -.
DR MGI; MGI:1096867; Etv5.
DR VEuPathDB; HostDB:ENSMUSG00000013089; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160680; -.
DR HOGENOM; CLU_030025_1_0_1; -.
DR InParanoid; Q9CXC9; -.
DR OMA; SYCAYDR; -.
DR OrthoDB; 536648at2759; -.
DR TreeFam; TF316214; -.
DR BioGRID-ORCS; 104156; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Etv5; mouse.
DR PRO; PR:Q9CXC9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CXC9; protein.
DR Bgee; ENSMUSG00000013089; Expressed in embryonic post-anal tail and 174 other tissues.
DR ExpressionAtlas; Q9CXC9; baseline and differential.
DR Genevisible; Q9CXC9; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IDA:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; 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 DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..510
FT /note="ETS translocation variant 5"
FT /id="PRO_0000204119"
FT DNA_BIND 368..448
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 132..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41161"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P41161"
FT CONFLICT 271
FT /note="Y -> F (in Ref. 1; AAF85761)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> V (in Ref. 1; AAF85761)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="F -> I (in Ref. 2; BAC27412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57712 MW; 371560F7E84A8F74 CRC64;
MDGFCDQQVP FMVPGKSRSE DCRGRPLIDR KRKFVDTDLA HDSEELFQDL SQLQEAWLAE
AQVPDDEQFV PDFQSDNLVL HAPPPTKIKR ELHSPSSELS SCSHEQALGA KYGEKCLYNY
CAYDRKPPSG FKPLTPPATP LSPTHQNSLF PPPQATLPTS GLTPGAGPVQ GVGPAPTPHS
LPEPGSQQQT FAVPRPPHQP LQMPKMMPES QYPSEQRFQR QLSEPSHPFP PQSGVPGDSR
PSYHRQMSEP IVPAAPPPLQ GFKQEYHDPL YEHGVPGMPG PPAHGFQSPM GIKQEPRDYC
ADSEVPNCQS SYMRGGYFSS SHEGFPYEKD PRLYFDDTCV VPERLEGKVK QEPTMYREGP
PYQRRGSLQL WQFLVTLLDD PANAHFIAWT GRGMEFKLIE PEEVARRWGI QKNRPAMNYD
KLSRSLRYYY EKGIMQKVAG ERYVYKFVCD PDALFSMAFP DNQRPFLKAE SECPLNEEDT
LPLTHFEDNP AYLLDMDRCS SLPYTEGFAY
