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ETV6_BOVIN
ID   ETV6_BOVIN              Reviewed;         452 AA.
AC   Q0VC65;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Transcription factor ETV6;
GN   Name=ETV6;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'-
CC       CCGGAAGT-3'. Plays a role in hematopoiesis and malignant
CC       transformation. {ECO:0000250|UniProtKB:P41212}.
CC   -!- SUBUNIT: Can form homodimers or heterodimers with TEL2 or FLI1.
CC       Interacts with L3MBTL1 and HDAC9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR   EMBL; BC120331; AAI20332.1; -; mRNA.
DR   RefSeq; NP_001015514.2; NM_001015514.2.
DR   AlphaFoldDB; Q0VC65; -.
DR   BMRB; Q0VC65; -.
DR   SMR; Q0VC65; -.
DR   STRING; 9913.ENSBTAP00000052186; -.
DR   PaxDb; Q0VC65; -.
DR   PRIDE; Q0VC65; -.
DR   Ensembl; ENSBTAT00000074978; ENSBTAP00000071376; ENSBTAG00000014605.
DR   GeneID; 504512; -.
DR   KEGG; bta:504512; -.
DR   CTD; 2120; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014605; -.
DR   VGNC; VGNC:28632; ETV6.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000159508; -.
DR   HOGENOM; CLU_037998_1_0_1; -.
DR   InParanoid; Q0VC65; -.
DR   OMA; NPRHSMD; -.
DR   OrthoDB; 827924at2759; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000014605; Expressed in parenchyma of mammary gland and 104 other tissues.
DR   ExpressionAtlas; Q0VC65; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; ISS:UniProtKB.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
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; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..452
FT                   /note="Transcription factor ETV6"
FT                   /id="PRO_0000287134"
FT   DOMAIN          40..124
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        339..420
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          154..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97360"
FT   MOD_RES         257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         302
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         323
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97360"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        288
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        302
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        403
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        421
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
SQ   SEQUENCE   452 AA;  52992 MW;  167E08D699953633 CRC64;
     MSETPAQCSI KQERISYTPP ESPVPSYASS TPLHVPVPRA LRMEEDSIRL PAHLRLQPMF
     WSRDDVAQWL KWAENEFSLR PIDSNTFEMN GKALLLLTKE DFRYRSPHSG DVLYELLQHI
     LKQRKPRILF SPFFHPGNSI HTQQEVILHQ NHEEDNGVQR TSRPSAENVH QNPPTIELLH
     RSRSPITTNH RPSPDPEQRP LRSPLDNMIR RLSPAERAQG PRLHQENNHQ EPYPLSVSPM
     ENNHCPPSSE PHPRPSSPRQ EGTRVIQLMP SPIMHPLILN PRHSVDFKQP RLSEDGLHRE
     GKPINLSHRE DLAYMNHIMV SVSPPEEHAV PIGRIADCRL LWDYVYQLLS DSRYENFIRW
     EDKESKIFRI VDPNGLARLW GNHKNRTNMT YEKMSRALRH YYKLNIIRKE PGQRLLFRFM
     KTPDEIMSGR TDRLEHLESQ ELDEQIYQED EC
 
 
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