COE2_MOUSE
ID COE2_MOUSE Reviewed; 575 AA.
AC O08792; Q543D5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Transcription factor COE2;
DE AltName: Full=Early B-cell factor 2;
DE Short=EBF-2;
DE AltName: Full=Metencephalon-mesencephalon-olfactory transcription factor 1;
DE Short=MET-mesencephalon-olfactory TF1;
DE Short=MET-mesencephalon-olfactory transcription factor 1;
DE AltName: Full=Olf-1/EBF-like 3;
DE Short=O/E-3;
DE Short=OE-3;
GN Name=Ebf2; Synonyms=Coe2, Mmot1;
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], AND CHARACTERIZATION.
RC TISSUE=Embryo;
RX PubMed=9211912; DOI=10.1074/jbc.272.28.17632;
RA Malgaretti N., Pozzoli O., Bosetti A., Corradi A., Ciarmatori S.,
RA Panigada M., Bianchi M.E., Martinez S., Consalez G.G.;
RT "Mmot1, a new helix-loop-helix transcription factor gene displaying a sharp
RT expression boundary in the embryonic mouse brain.";
RL J. Biol. Chem. 272:17632-17639(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=9151732; DOI=10.1523/jneurosci.17-11-04149.1997;
RA Wang S.S., Tsai R.Y.L., Reed R.R.;
RT "The characterization of the Olf-1/EBF-like HLH transcription factor
RT family: implications in olfactory gene regulation and neuronal
RT development.";
RL J. Neurosci. 17:4149-4158(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9389446;
RX DOI=10.1002/(sici)1097-0177(199711)210:3<191::aid-aja1>3.0.co;2-b;
RA Garel S., Marin F., Mattei M.-G., Vesque C., Vincent A., Charnay P.;
RT "Family of Ebf/Olf-1-related genes potentially involved in neuronal
RT differentiation and regional specification in the central nervous system.";
RL Dev. Dyn. 210:191-205(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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 [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=16326388; DOI=10.1016/j.devcel.2005.10.009;
RA Kieslinger M., Folberth S., Dobreva G., Dorn T., Croci L., Erben R.,
RA Consalez G.G., Grosschedl R.;
RT "EBF2 regulates osteoblast-dependent differentiation of osteoclasts.";
RL Dev. Cell 9:757-767(2005).
RN [7]
RP INTERACTION WITH SIX1.
RX PubMed=27923061; DOI=10.1371/journal.pgen.1006474;
RA Brunmeir R., Wu J., Peng X., Kim S.Y., Julien S.G., Zhang Q., Xie W.,
RA Xu F.;
RT "Comparative Transcriptomic and Epigenomic Analyses Reveal New Regulators
RT of Murine Brown Adipogenesis.";
RL PLoS Genet. 12:E1006474-E1006474(2016).
CC -!- FUNCTION: Transcription factor that, in osteoblasts, activates the
CC decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast
CC differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1
CC pathway. Recognizes variations of the palindromic sequence 5'-
CC ATTCCCNNGGGAATT-3'. {ECO:0000269|PubMed:16326388}.
CC -!- SUBUNIT: Forms either a homodimer or a heterodimer with a related
CC family member (PubMed:9151732). Interacts with SIX1 (PubMed:27923061).
CC {ECO:0000269|PubMed:27923061, ECO:0000269|PubMed:9151732}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adult expressed in olfactory epithelium and at a
CC much lower level in Purkinje cells of the cerebellum. In embryo
CC expressed in epithalamus, in cells near the ventricular zone of
CC mesencephalon and on the ventral surface of rhombencephalon, in the
CC developing vomeronasal organ, at a lower level in developing spinal
CC cord. Not expressed in developing retina, inner ear, dorsal root
CC ganglia, trigeminal ganglia and glossopharyngeal ganglia.
CC -!- DEVELOPMENTAL STAGE: First detected at 9.0 dpc in the first and second
CC archial arches. At 10.0 dpc and 10.5 dpc, expressed in somites,
CC especially the forming sclerotomes. At 12.5 dpc, found in dorsal root
CC ganglia. At 16.5 dpc, expressed in bone-forming areas and adipose
CC tissues, as well as in specific neural tissues. In bone-forming areas,
CC expressed along the mesenchymal condensation at 14.5 dpc, in the
CC perichondrium and in cells invading the cartilagenous structures at
CC 16.5 dpc. In 18.5 dpc tibias, scattered throughout the
CC trabecular/cancellous bone area. In vitro, expression is induced during
CC differentiation of immature osteoblasts, and then declines.
CC {ECO:0000269|PubMed:16326388}.
CC -!- SIMILARITY: Belongs to the COE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB58423.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U71189; AAB58423.1; ALT_INIT; mRNA.
DR EMBL; U92703; AAB58323.1; -; mRNA.
DR EMBL; U82441; AAC64322.1; -; mRNA.
DR EMBL; AK053013; BAC35239.1; -; mRNA.
DR EMBL; AK139262; BAE23936.1; -; mRNA.
DR EMBL; BC049188; AAH49188.1; -; mRNA.
DR EMBL; BC050922; AAH50922.1; -; mRNA.
DR CCDS; CCDS27228.1; -.
DR RefSeq; NP_001263316.1; NM_001276387.1.
DR RefSeq; NP_034225.1; NM_010095.6.
DR RefSeq; XP_011243247.1; XM_011244945.2.
DR AlphaFoldDB; O08792; -.
DR SMR; O08792; -.
DR BioGRID; 199359; 1.
DR IntAct; O08792; 1.
DR MINT; O08792; -.
DR STRING; 10090.ENSMUSP00000022637; -.
DR iPTMnet; O08792; -.
DR PhosphoSitePlus; O08792; -.
DR MaxQB; O08792; -.
DR PaxDb; O08792; -.
DR PeptideAtlas; O08792; -.
DR PRIDE; O08792; -.
DR ProteomicsDB; 285236; -.
DR Antibodypedia; 22905; 110 antibodies from 21 providers.
DR DNASU; 13592; -.
DR Ensembl; ENSMUST00000022637; ENSMUSP00000022637; ENSMUSG00000022053.
DR Ensembl; ENSMUST00000176029; ENSMUSP00000135782; ENSMUSG00000022053.
DR Ensembl; ENSMUST00000176161; ENSMUSP00000135500; ENSMUSG00000022053.
DR GeneID; 13592; -.
DR KEGG; mmu:13592; -.
DR UCSC; uc007ukw.2; mouse.
DR CTD; 64641; -.
DR MGI; MGI:894332; Ebf2.
DR VEuPathDB; HostDB:ENSMUSG00000022053; -.
DR eggNOG; KOG3836; Eukaryota.
DR GeneTree; ENSGT00950000182859; -.
DR HOGENOM; CLU_016320_3_1_1; -.
DR InParanoid; O08792; -.
DR OMA; YGTSGGM; -.
DR OrthoDB; 817293at2759; -.
DR PhylomeDB; O08792; -.
DR TreeFam; TF313391; -.
DR BioGRID-ORCS; 13592; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ebf2; mouse.
DR PRO; PR:O08792; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O08792; protein.
DR Bgee; ENSMUSG00000022053; Expressed in olfactory epithelium and 167 other tissues.
DR Genevisible; O08792; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0001709; P:cell fate determination; IDA:MGI.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IDA:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
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; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd11606; COE_DBD; 1.
DR CDD; cd01175; IPT_COE; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.3180; -; 1.
DR InterPro; IPR032200; COE_DBD.
DR InterPro; IPR038173; COE_DBD_sf.
DR InterPro; IPR032201; COE_HLH.
DR InterPro; IPR038006; COE_IPT.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR003523; Transcription_factor_COE.
DR InterPro; IPR018350; Transcription_factor_COE_CS.
DR PANTHER; PTHR10747; PTHR10747; 1.
DR Pfam; PF16422; COE1_DBD; 1.
DR Pfam; PF16423; COE1_HLH; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS01345; COE; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..575
FT /note="Transcription factor COE2"
FT /id="PRO_0000107829"
FT DOMAIN 253..336
FT /note="IPT/TIG"
FT ZN_FING 150..169
FT /note="C5-type"
FT /evidence="ECO:0000255"
FT REGION 62..65
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 196..203
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 235..238
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 441..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 162
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT SITE 171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT CONFLICT 37
FT /note="D -> V (in Ref. 3; AAC64322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 62606 MW; E8CDD6DAC7637449 CRC64;
MFGIQDTLGR GPALKDKSLG AEMDSVRSWV RNVGVVDANV AAQSGVALSR AHFEKQPPSN
LRKSNFFHFV LALYDRQGQP VEIERTAFVD FVENDKEQGN EKTNNGTHYK LQLLYSNGVR
TEQDLYVRLI DSVTKQPIAY EGQNKNPEMC RVLLTHEVMC SRCCEKKSCG NRNETPSDPV
IIDRFFLKFF LKCNQNCLKT AGNPRDMRRF QVVLSTTVNV DGHVLAVSDN MFVHNNSKHG
RRARRLDPSE ATPCIKAISP SEGWTTGGAM VIIIGDNFFD GLQVVFGTML VWSELITPHA
IRVQTPPRHI PGVVEVTLSY KSKQFCKGAP GRFIYTALNE PTIDYGFQRL QKVIPRHPGD
PERLAKEMLL KRAADLVEAL YGTPHNNQDI ILKRAADIAE ALYSVPRNPS QIPALSSSPA
HSGMMGINSY GSQLGVSISE STQGNNQGYI RNTSSISPRG YSSSSTPQQS NYSTSSNSMN
GYSNVPMANL GVPGSPGFLN GSPTGSPYGI MSSSPTVGSS STSSILPFSS SVFPAVKQKS
AFAPVIRPQG SPSPACSSGN GNGFRAMTGL VVPPM
