GenomeNet

Database: UniProt
Entry: Q3UPW2
LinkDB: Q3UPW2
Original site: Q3UPW2 
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   07-OCT-2020, entry version 128.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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., 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] (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 project:
RT   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 with
RT   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 epithelial
RT   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 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 receptor
RT   gene: up-regulation and function of the transcription factor Elf-
RT   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 development of
RT   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; 269-ARG--LYS-272
RP   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., Cha K.-Y.,
RA   Chung H.-M., Kim J.-H.;
RT   "Identification of multiple nuclear localization signals in murine Elf3, an
RT   ETS transcription factor.";
RL   FEBS Lett. 580:1865-1871(2006).
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 (By similarity).
CC       Also transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2,
CC       SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity (By
CC       similarity). Involved in mediating vascular inflammation. May play an
CC       important role in epithelial cell differentiation and tumorigenesis.
CC       May be a critical downstream effector of the ERBB2 signaling pathway
CC       (By similarity). May be associated with mammary gland development and
CC       involution. Plays an important role in the regulation of transcription
CC       with TATA-less promoters in preimplantation embryos, which is essential
CC       in preimplantation development. {ECO:0000250|UniProtKB:P78545,
CC       ECO:0000269|PubMed:11893733, ECO:0000269|PubMed:11984530,
CC       ECO:0000269|PubMed:16630543, ECO:0000269|PubMed:9806763}.
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|UniProtKB:P78545}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00237, 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, kidney
CC       and uterus. Also expressed in the corneal epithelium and conjunctiva of
CC       the developing and adult eye. Not detected in liver, spleen, thymus,
CC       brain, heart, skeletal muscle or ovary. {ECO:0000269|PubMed:11025204,
CC       ECO:0000269|PubMed:9395241}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases progressively from 7 dpc and
CC       is detectable in virgin mammary glands, then shows little if any change
CC       during pregnancy and declines to barely detectable levels after 3 days
CC       of lactation. Detected from 13.5 dpc in conjunctiva epithelium. In
CC       cornea, a weak signal is detected at 16.5 dpc and persists throughout
CC       the later stages of development. {ECO:0000269|PubMed:11025204,
CC       ECO:0000269|PubMed:9806763}.
CC   -!- INDUCTION: Expression in HC11 cells from midpregnant mouse mammary
CC       epithelium increases upon reaching lactogenic competency, and is down-
CC       regulated upon exposure to lactogenic hormones that induce milk protein
CC       (Beta-casein) expression. Up-regulated upon differentiation in corneal
CC       epithelium. {ECO:0000269|PubMed:11025204, ECO:0000269|PubMed:9806763}.
CC   -!- DISRUPTION PHENOTYPE: Mice show about 30% fetal lethality at around
CC       11.5 dpc. Approximately 70% of the mutant progeny are born and display
CC       severe alterations in tissue architecture in the small intestine. Elf3-
CC       deficient enterocytes express markedly reduced levels of TGFBR2.
CC       {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   Antibodypedia; 924; 420 antibodies.
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   GeneTree; ENSGT00940000158955; -.
DR   HOGENOM; CLU_048172_0_0_1; -.
DR   InParanoid; Q3UPW2; -.
DR   KO; K09429; -.
DR   OMA; ASWSGKQ; -.
DR   OrthoDB; 837296at2759; -.
DR   PhylomeDB; Q3UPW2; -.
DR   TreeFam; TF318679; -.
DR   Reactome; R-MMU-1912408; Pre-NOTCH Transcription and Translation.
DR   BioGRID-ORCS; 13710; 1 hit in 18 CRISPR screens.
DR   ChiTaRS; Elf3; mouse.
DR   EvolutionaryTrace; Q3UPW2; -.
DR   PRO; PR:Q3UPW2; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q3UPW2; protein.
DR   Bgee; ENSMUSG00000003051; Expressed in stomach and 203 other tissues.
DR   Genevisible; Q3UPW2; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
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 cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
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; IEA:InterPro.
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: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; Cytoplasm;
KW   Developmental protein; Differentiation; DNA-binding; Inflammatory response;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..391
FT                   /note="ETS-related transcription factor Elf-3"
FT                   /id="PRO_0000287682"
FT   DOMAIN          65..151
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        293..375
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   VAR_SEQ         54..73
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9395241"
FT                   /id="VSP_052434"
FT   MUTAGEN         153
FT                   /note="D->A: Slight reduction in transactivation activity."
FT                   /evidence="ECO:0000269|PubMed:11893733"
FT   MUTAGEN         162
FT                   /note="L->P: Significant loss of transactivation activity."
FT                   /evidence="ECO:0000269|PubMed:11893733"
FT   MUTAGEN         264..267
FT                   /note="KRKR->AAAA: Abrogates nuclear localization
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:16516205"
FT   MUTAGEN         269..272
FT                   /note="RPRK->APAA: Clear and exclusive nuclear
FT                   accumulation."
FT                   /evidence="ECO:0000269|PubMed:16516205"
FT   MUTAGEN         338..340
FT                   /note="KKK->AAA: Abolishes nuclear localization."
FT                   /evidence="ECO:0000269|PubMed:16516205"
FT   HELIX           295..303
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   HELIX           306..308
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   STRAND          313..317
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   TURN            318..321
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   STRAND          322..327
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   HELIX           328..338
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   HELIX           346..354
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   TURN            355..360
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   STRAND          371..374
FT                   /evidence="ECO:0000244|PDB:3JTG"
FT   TURN            383..385
FT                   /evidence="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