ELF3_RAT
ID ELF3_RAT Reviewed; 395 AA.
AC Q4V7E1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=ETS-related transcription factor Elf-3;
DE AltName: Full=E74-like factor 3;
GN Name=Elf3 {ECO:0000312|EMBL:AAH97980.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH97980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH97980.1};
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).
CC -!- FUNCTION: Transcriptional activator that binds and transactivates ETS
CC sequences containing the consensus nucleotide core sequence GGA[AT].
CC Acts synergistically with POU2F3 to transactivate the SPRR2A promoter
CC and with RUNX1 to transactivate the ANGPT1 promoter. Also
CC transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2,
CC SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity.
CC Involved in mediating vascular inflammation. May play an important role
CC in epithelial cell differentiation and tumorigenesis. May be a critical
CC downstream effector of the ERBB2 signaling pathway. May be associated
CC with mammary gland development and involution. Plays an important role
CC in the regulation of transcription with TATA-less promoters in
CC preimplantation embryos, which is essential in preimplantation
CC development (By similarity). {ECO:0000250|UniProtKB:P78545,
CC ECO:0000250|UniProtKB:Q3UPW2}.
CC -!- SUBUNIT: Interacts with TBP. Interacts with CREBBP and EP300; these act
CC as transcriptional coactivators of ELF3 and positively modulate its
CC function. Interacts with XRCC5/KU86 and XRCC6/KU70; these inhibit the
CC ability of ELF3 to bind DNA and negatively modulate its transcriptional
CC activity. Associated with CLND7 and POU2F3 (By similarity).
CC {ECO:0000250|UniProtKB:P78545}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250|UniProtKB:P78545, ECO:0000255|PROSITE-ProRule:PRU00237}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
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DR EMBL; BC097980; AAH97980.1; -; mRNA.
DR RefSeq; NP_001019939.1; NM_001024768.1.
DR AlphaFoldDB; Q4V7E1; -.
DR SMR; Q4V7E1; -.
DR STRING; 10116.ENSRNOP00000008753; -.
DR iPTMnet; Q4V7E1; -.
DR PhosphoSitePlus; Q4V7E1; -.
DR PaxDb; Q4V7E1; -.
DR GeneID; 304815; -.
DR KEGG; rno:304815; -.
DR UCSC; RGD:1310687; rat.
DR CTD; 1999; -.
DR RGD; 1310687; Elf3.
DR VEuPathDB; HostDB:ENSRNOG00000006330; -.
DR eggNOG; KOG3804; Eukaryota.
DR HOGENOM; CLU_048172_0_0_1; -.
DR InParanoid; Q4V7E1; -.
DR OMA; ASWSGKQ; -.
DR OrthoDB; 837296at2759; -.
DR PhylomeDB; Q4V7E1; -.
DR TreeFam; TF318679; -.
DR Reactome; R-RNO-1912408; Pre-NOTCH Transcription and Translation.
DR PRO; PR:Q4V7E1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000006330; Expressed in stomach and 15 other tissues.
DR Genevisible; Q4V7E1; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0009653; P:anatomical structure morphogenesis; ISO:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0060056; P:mammary gland involution; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd08537; SAM_PNT-ESE-1-like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR042693; Elf-3_PNT.
DR InterPro; IPR033074; Elf3.
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 PANTHER; PTHR11849:SF13; PTHR11849:SF13; 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; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Inflammatory response; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..395
FT /note="ETS-related transcription factor Elf-3"
FT /id="PRO_0000287683"
FT DOMAIN 69..155
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 297..379
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 200..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 44521 MW; BBE321B85A73458A CRC64;
MAATCEISNV FSNYFNAMYS SEDPTLAPAP LTTFGTEDFV LTLNNQHMSP EGPVGCVGPQ
TRSQRDRTEP PAVLHLAEKA SWTGERPQFW SKTQVLDWIS YQVEKNKYDA SSIDFSRCDM
DGATLCNCAL EELRLVFGPL GDQLHAQLRD LTSSSSDELS WIIELLEKDG MTFQEGLGDS
GPFDQGSPFA QELLDDGRQA SPYYGSSYGP GAPSPGSSDF STSGTDTPQS SHSSDSGGSD
VDLDLTDSKV FPRDGFPDYK KGEPKHGKRK RGRPRKLSKE YWDCLEGKKS KHAPRGTHLW
EFIRDILIHP ELNEGLMKWE NRHEGVFKFL RSEAVAQLWG QKKKNSNMTY EKLSRAMRYY
YKREILERVD GRRLVYKFGK NSSGWKEEEV GESQN