GenomeNet

Database: UniProt
Entry: ELF3_MOUSE
LinkDB: ELF3_MOUSE
Original site: ELF3_MOUSE 
ID   ELF3_MOUSE              Reviewed;         391 AA.
AC   Q3UPW2; B7ZNQ9; B9EI01; O35275;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-OCT-2019, entry version 122.
DE   RecName: Full=ETS-related transcription factor Elf-3;
DE   AltName: Full=E74-like factor 3;
DE   AltName: Full=Epithelial-restricted with serine box;
DE   AltName: Full=Epithelium-restricted Ets protein ESX;
DE   AltName: Full=Epithelium-specific Ets transcription factor 1;
DE            Short=ESE-1;
GN   Name=Elf3 {ECO:0000312|MGI:MGI:1101781}; Synonyms=Ert, Esx, Jen;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB96585.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Lung {ECO:0000312|EMBL:AAB96585.1};
RX   PubMed=9395241; DOI=10.1038/sj.onc.1201427;
RA   Tymms M.J., Ng A.Y.N., Thomas R.S., Schutte B.C., Zhou J., Eyre H.J.,
RA   Sutherland G.R., Seth A., Rosenberg M., Papas T., Debouck C., Kola I.;
RT   "A novel epithelial-expressed ETS gene, ELF3: human and murine cDNA
RT   sequences, murine genomic organization, human mapping to 1q32.2 and
RT   expression in tissues and cancer.";
RL   Oncogene 15:2449-2462(1997).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAE25282.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25282.1};
RC   TISSUE=Eye {ECO:0000312|EMBL:BAE25282.1};
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=9806763; DOI=10.1096/fasebj.12.14.1541;
RA   Neve R., Chang C.-H., Scott G.K., Wong A., Friis R.R., Hynes N.E.,
RA   Benz C.C.;
RT   "The epithelium-specific ets transcription factor ESX is associated
RT   with mammary gland development and involution.";
RL   FASEB J. 12:1541-1550(1998).
RN   [5] {ECO:0000305}
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11025204; DOI=10.1016/s0925-4773(00)00419-6;
RA   Yoshida N., Yoshida S., Araie M., Handa H., Nabeshima Y.;
RT   "Ets family transcription factor ESE-1 is expressed in corneal
RT   epithelial cells and is involved in their differentiation.";
RL   Mech. Dev. 97:27-34(2000).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11984530; DOI=10.1053/gast.2002.32990;
RA   Ng A.-Y.N., Waring P., Ristevski S., Wang C., Wilson T., Pritchard M.,
RA   Hertzog P., Kola I.;
RT   "Inactivation of the transcription factor Elf3 in mice results in
RT   dysmorphogenesis and altered differentiation of intestinal
RT   epithelium.";
RL   Gastroenterology 122:1455-1466(2002).
RN   [7] {ECO:0000305}
RP   FUNCTION, AND MUTAGENESIS OF ASP-153 AND LEU-162.
RX   PubMed=11893733; DOI=10.1074/jbc.m110434200;
RA   Kim J.-H., Wilder P.J., Hou J., Nowling T., Rizzino A.;
RT   "Activation of the murine type II transforming growth factor-beta
RT   receptor gene: up-regulation and function of the transcription factor
RT   Elf-3/Ert/Esx/Ese-1.";
RL   J. Biol. Chem. 277:17520-17530(2002).
RN   [8] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16630543; DOI=10.1016/j.bbrc.2006.03.192;
RA   Kageyama S., Liu H., Nagata M., Aoki F.;
RT   "The role of ETS transcription factors in transcription and
RT   development of mouse preimplantation embryos.";
RL   Biochem. Biophys. Res. Commun. 344:675-679(2006).
RN   [9] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 264-LYS--ARG-267;
RP   269-ARG--LYS-272 AND 338-LYS--LYS-340.
RX   PubMed=16516205; DOI=10.1016/j.febslet.2006.02.049;
RA   Do H.-J., Song H., Yang H.-M., Kim D.-K., Kim N.-H., Kim J.-H.,
RA   Cha K.-Y., Chung H.-M., Kim J.-H.;
RT   "Identification of multiple nuclear localization signals in murine
RT   Elf3, an ETS transcription factor.";
RL   FEBS Lett. 580:1865-1871(2006).
CC   -!- FUNCTION: Transcriptional activator that binds and transactivates
CC       ETS sequences containing the consensus nucleotide core sequence
CC       GGA[AT]. Acts synergistically with POU2F3 to transactivate the
CC       SPRR2A promoter and with RUNX1 to transactivate the ANGPT1
CC       promoter (By similarity). Also transactivates collagenase, CCL20,
CC       CLND7, FLG, KRT8, NOS2, PTGS2, SPRR2B, TGFBR2 and TGM3 promoters.
CC       Represses KRT4 promoter activity (By similarity). Involved in
CC       mediating vascular inflammation. May play an important role in
CC       epithelial cell differentiation and tumorigenesis. May be a
CC       critical downstream effector of the ERBB2 signaling pathway (By
CC       similarity). May be associated with mammary gland development and
CC       involution. Plays an important role in the regulation of
CC       transcription with TATA-less promoters in preimplantation embryos,
CC       which is essential in preimplantation development.
CC       {ECO:0000250|UniProtKB:P78545, ECO:0000269|PubMed:11893733,
CC       ECO:0000269|PubMed:11984530, ECO:0000269|PubMed:16630543,
CC       ECO:0000269|PubMed:9806763}.
CC   -!- SUBUNIT: Interacts with TBP. Interacts with CREBBP and EP300;
CC       these act as transcriptional coactivators of ELF3 and positively
CC       modulate its function. Interacts with XRCC5/KU86 and XRCC6/KU70;
CC       these inhibit the ability of ELF3 to bind DNA and negatively
CC       modulate its transcriptional activity. Associated with CLND7 and
CC       POU2F3 (By similarity). {ECO:0000250|UniProtKB:P78545}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78545}.
CC       Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237,
CC       ECO:0000269|PubMed:16516205}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q3UPW2-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:9395241};
CC         IsoId=Q3UPW2-2; Sequence=VSP_052434;
CC   -!- TISSUE SPECIFICITY: Expressed in small intestine, colon, lung,
CC       kidney and uterus. Also expressed in the corneal epithelium and
CC       conjunctiva of the developing and adult eye. Not detected in
CC       liver, spleen, thymus, brain, heart, skeletal muscle or ovary.
CC       {ECO:0000269|PubMed:11025204, ECO:0000269|PubMed:9395241}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases progressively from 7 dpc
CC       and is detectable in virgin mammary glands, then shows little if
CC       any change during pregnancy and declines to barely detectable
CC       levels after 3 days of lactation. Detected from 13.5 dpc in
CC       conjunctiva epithelium. In cornea, a weak signal is detected at
CC       16.5 dpc and persists throughout the later stages of development.
CC       {ECO:0000269|PubMed:11025204, ECO:0000269|PubMed:9806763}.
CC   -!- INDUCTION: Expression in HC11 cells from midpregnant mouse mammary
CC       epithelium increases upon reaching lactogenic competency, and is
CC       down-regulated upon exposure to lactogenic hormones that induce
CC       milk protein (Beta-casein) expression. Up-regulated upon
CC       differentiation in corneal epithelium.
CC       {ECO:0000269|PubMed:11025204, ECO:0000269|PubMed:9806763}.
CC   -!- DISRUPTION PHENOTYPE: Mice show about 30% fetal lethality at
CC       around 11.5 dpc. Approximately 70% of the mutant progeny are born
CC       and display severe alterations in tissue architecture in the small
CC       intestine. Elf3-deficient enterocytes express markedly reduced
CC       levels of TGFBR2. {ECO:0000269|PubMed:11984530}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
DR   EMBL; AF016294; AAB96585.1; -; mRNA.
DR   EMBL; AK143135; BAE25282.1; -; mRNA.
DR   EMBL; BC138692; AAI38693.1; -; mRNA.
DR   EMBL; BC145380; AAI45381.1; -; mRNA.
DR   CCDS; CCDS48372.1; -. [Q3UPW2-1]
DR   CCDS; CCDS78689.1; -. [Q3UPW2-2]
DR   RefSeq; NP_001156603.1; NM_001163131.1. [Q3UPW2-1]
DR   RefSeq; NP_031947.1; NM_007921.3. [Q3UPW2-2]
DR   PDB; 3JTG; X-ray; 2.20 A; A=289-391.
DR   PDBsum; 3JTG; -.
DR   SMR; Q3UPW2; -.
DR   STRING; 10090.ENSMUSP00000003135; -.
DR   iPTMnet; Q3UPW2; -.
DR   PhosphoSitePlus; Q3UPW2; -.
DR   PaxDb; Q3UPW2; -.
DR   PeptideAtlas; Q3UPW2; -.
DR   PRIDE; Q3UPW2; -.
DR   Ensembl; ENSMUST00000003135; ENSMUSP00000003135; ENSMUSG00000003051. [Q3UPW2-1]
DR   Ensembl; ENSMUST00000185752; ENSMUSP00000139769; ENSMUSG00000003051. [Q3UPW2-2]
DR   GeneID; 13710; -.
DR   KEGG; mmu:13710; -.
DR   UCSC; uc007csw.2; mouse. [Q3UPW2-2]
DR   UCSC; uc007csx.2; mouse. [Q3UPW2-1]
DR   CTD; 1999; -.
DR   MGI; MGI:1101781; Elf3.
DR   eggNOG; KOG3804; Eukaryota.
DR   eggNOG; ENOG4111K4J; LUCA.
DR   GeneTree; ENSGT00940000158955; -.
DR   HOGENOM; HOG000232188; -.
DR   InParanoid; Q3UPW2; -.
DR   KO; K09429; -.
DR   OMA; NCAPEEL; -.
DR   OrthoDB; 837296at2759; -.
DR   PhylomeDB; Q3UPW2; -.
DR   TreeFam; TF318679; -.
DR   Reactome; R-MMU-1912408; Pre-NOTCH Transcription and Translation.
DR   ChiTaRS; Elf3; mouse.
DR   EvolutionaryTrace; Q3UPW2; -.
DR   PRO; PR:Q3UPW2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000003051; Expressed in 179 organ(s), highest expression level in stomach.
DR   Genevisible; Q3UPW2; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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 proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR   GO; GO:0060056; P:mammary gland involution; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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; IDA:MGI.
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; 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: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   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Complete proteome;
KW   Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW   Inflammatory response; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    391       ETS-related transcription factor Elf-3.
FT                                /FTId=PRO_0000287682.
FT   DOMAIN       65    151       PNT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00762}.
FT   DNA_BIND    293    375       ETS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00237}.
FT   VAR_SEQ      54     73       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9395241}.
FT                                /FTId=VSP_052434.
FT   MUTAGEN     153    153       D->A: Slight reduction in transactivation
FT                                activity. {ECO:0000269|PubMed:11893733}.
FT   MUTAGEN     162    162       L->P: Significant loss of transactivation
FT                                activity. {ECO:0000269|PubMed:11893733}.
FT   MUTAGEN     264    267       KRKR->AAAA: Abrogates nuclear
FT                                localization activity.
FT                                {ECO:0000269|PubMed:16516205}.
FT   MUTAGEN     269    272       RPRK->APAA: Clear and exclusive nuclear
FT                                accumulation.
FT                                {ECO:0000269|PubMed:16516205}.
FT   MUTAGEN     338    340       KKK->AAA: Abolishes nuclear localization.
FT                                {ECO:0000269|PubMed:16516205}.
FT   HELIX       295    303       {ECO:0000244|PDB:3JTG}.
FT   HELIX       306    308       {ECO:0000244|PDB:3JTG}.
FT   STRAND      313    317       {ECO:0000244|PDB:3JTG}.
FT   TURN        318    321       {ECO:0000244|PDB:3JTG}.
FT   STRAND      322    327       {ECO:0000244|PDB:3JTG}.
FT   HELIX       328    338       {ECO:0000244|PDB:3JTG}.
FT   HELIX       346    354       {ECO:0000244|PDB:3JTG}.
FT   TURN        355    360       {ECO:0000244|PDB:3JTG}.
FT   STRAND      371    374       {ECO:0000244|PDB:3JTG}.
FT   TURN        383    385       {ECO:0000244|PDB:3JTG}.
SQ   SEQUENCE   391 AA;  44273 MW;  738DA753961622D4 CRC64;
     MAATCEISNV FSNYFNAMYS SEDPTLAPAP PTTFGTEDLV LTLNNQQMTL EGPGPQTRSQ
     RDRTDPLAVL HLAEKASWTS ERPQFWSKTQ VLEWISYQVE KNKYDASSID FSRCDMDGAT
     LCSCALEELR LVFGPLGDQL HAQLRDLTSN SSDELSWIIE LLEKDGMSFQ ESLGDSGPFD
     QGSPFAQELL DDGRQASPYY CSTYGPGAPS PGSSDVSTAR TATPQSSHAS DSGGSDVDLD
     LTESKVFPRD GFPDYKKGEP KHGKRKRGRP RKLSKEYWDC LEGKKSKHAP RGTHLWEFIR
     DILIHPELNE GLMKWENRHE GVFKFLRSEA VAQLWGQKKK NSNMTYEKLS RAMRYYYKRE
     ILERVDGRRL VYKFGKNSSG WKEEEVGESR N
//
DBGET integrated database retrieval system