ID COE1_MOUSE Reviewed; 591 AA. AC Q07802; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 180. DE RecName: Full=Transcription factor COE1; DE Short=O/E-1; DE Short=OE-1; DE AltName: Full=Early B-cell factor; GN Name=Ebf1; Synonyms=Coe1, Ebf; 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 PROTEIN SEQUENCE OF 87-99; 122-129; 342-358 RP AND 382-390. RC TISSUE=Lymphoid tissue; RX PubMed=8491377; DOI=10.1101/gad.7.5.760; RA Hagman J., Belanger C., Travis A., Turck W., Grosschedl R.; RT "Cloning and functional characterization of early B-cell factor, a RT regulator of lymphocyte-specific gene expression."; RL Genes Dev. 7:760-773(1993). RN [2] RP CHARACTERIZATION. RX PubMed=8497258; DOI=10.1128/mcb.13.6.3392-3400.1993; RA Travis A., Hagman J., Hwang L., Grosschedl R.; RT "Purification of early-B-cell factor and characterization of its DNA- RT binding specificity."; RL Mol. Cell. Biol. 13:3392-3400(1993). RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1915300; DOI=10.1002/j.1460-2075.1991.tb04905.x; RA Hagman J., Travis A., Grosschedl R.; RT "A novel lineage-specific nuclear factor regulates mb-1 gene transcription RT at the early stages of B cell differentiation."; RL EMBO J. 10:3409-3417(1991). RN [4] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=7542362; DOI=10.1038/376263a0; RA Lin H., Grosschedl R.; RT "Failure of B-cell differentiation in mice lacking the transcription factor RT EBF."; RL Nature 376:263-267(1995). RN [5] RP SUBUNIT, AND ALTERNATIVE SPLICING. 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-241 IN COMPLEX WITH TARGET DNA RP AND ZINC, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-63; ASN-66; ARG-163; RP GLY-203 AND HIS-235. RX PubMed=20876732; DOI=10.1101/gad.1976610; RA Treiber N., Treiber T., Zocher G., Grosschedl R.; RT "Structure of an Ebf1:DNA complex reveals unusual DNA recognition and RT structural homology with Rel proteins."; RL Genes Dev. 24:2270-2275(2010). RN [7] RP FUNCTION. RX PubMed=20451411; DOI=10.1016/j.immuni.2010.04.013; RA Treiber T., Mandel E.M., Pott S., Gyoery I., Firner S., Liu E.T., RA Grosschedl R.; RT "Early B cell factor 1 regulates B cell gene networks by activation, RT repression, and transcription- independent poising of chromatin."; RL Immunity 32:714-725(2010). RN [8] RP FUNCTION. RX PubMed=23812095; DOI=10.1038/ni.2641; RA Nechanitzky R., Akbas D., Scherer S., Gyoery I., Hoyler T., Ramamoorthy S., RA Diefenbach A., Grosschedl R.; RT "Transcription factor EBF1 is essential for the maintenance of B cell RT identity and prevention of alternative fates in committed cells."; RL Nat. Immunol. 14:867-875(2013). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=32130892; DOI=10.1016/j.celrep.2020.02.023; RA Angueira A.R., Shapira S.N., Ishibashi J., Sampat S., Sostre-Colon J., RA Emmett M.J., Titchenell P.M., Lazar M.A., Lim H.W., Seale P.; RT "Early B Cell Factor Activity Controls Developmental and Adaptive RT Thermogenic Gene Programming in Adipocytes."; RL Cell Rep. 30:2869-2878.e4(2020). CC -!- FUNCTION: Key pioneer transcription factor of B-cell specification and CC commitment (PubMed:1915300, PubMed:7542362, PubMed:23812095). CC Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' CC (PubMed:20876732). Operates in a transcription factor network to CC activate B-cell-specific genes and repress genes associated with CC alternative cell fates (PubMed:23812095, PubMed:20451411). For CC instance, positively regulates many B-cell specific genes including BCR CC or CD40 while repressing genes that direct cells into alternative CC lineages, including GATA3 and TCF7 for the T-cell lineage CC (PubMed:23812095, PubMed:20451411). In addition to its role during CC lymphopoiesis, controls the thermogenic gene program in adipocytes CC during development and in response to environmental cold CC (PubMed:32130892). {ECO:0000269|PubMed:1915300, CC ECO:0000269|PubMed:20451411, ECO:0000269|PubMed:20876732, CC ECO:0000269|PubMed:23812095, ECO:0000269|PubMed:32130892, CC ECO:0000269|PubMed:7542362}. CC -!- SUBUNIT: Homodimer (PubMed:9151732, PubMed:20876732). Interacts with CC ZNF423 and ZNF521, leading to prevent EBF1 to bind DNA and activate CC target genes (By similarity). Interacts with CCR4-NOT component CNOT3 CC (By similarity). {ECO:0000250|UniProtKB:Q9UH73, CC ECO:0000269|PubMed:20876732, ECO:0000269|PubMed:9151732}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1915300}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; Synonyms=8; CC IsoId=Q07802-1; Sequence=Displayed; CC Name=Short; Synonyms=O; CC IsoId=Q07802-2; Sequence=VSP_001112; CC -!- TISSUE SPECIFICITY: Expressed at high levels in early B-cells, spleen, CC lymph node and adipose tissue, and at low levels in heart, brain, CC skeletal muscle and kidney. In adult expressed in olfactory epithelium, CC in spleen, and at a lesser extent in Purkinje cells of the cerebellum, CC heart, kidney, lung, thymus and testis. In embryo expressed in dorsal CC thalamus and epithalamus, at a lower level in mesencephalon and in the CC caudal rhombencephalon, in the postmitotic cells of developing retina, CC highly in developing spinal cord, dorsal root ganglia, trigeminal CC ganglia and in glossopharyngeal nerve ganglia, in developing inner ear. CC -!- DEVELOPMENTAL STAGE: First detected at 9.5 dpc. CC -!- DISRUPTION PHENOTYPE: Targeted disruption in mice results in animals CC with a severe defect in early B-cell development. EBF1 heterozygous CC mice exhibit an approximately 2-fold decrease in the number of cells in CC the pro-B lymphocyte compartment, indicating that normal B-cell CC development depends on the presence of two wild-type EBF1 alleles CC (PubMed:7542362). Adipocyte-specific deletion mutant reveals a modest CC reduction of UCP1 expression, a mitochondrial protein responsible for CC thermogenic respiration. Double mutants EBF1/EBF2 show a more severe CC reduction of UCP1 expression (PubMed:32130892). CC {ECO:0000269|PubMed:32130892, ECO:0000269|PubMed:7542362}. CC -!- SIMILARITY: Belongs to the COE family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L12147; AAA37533.1; -; mRNA. DR CCDS; CCDS24566.1; -. [Q07802-1] DR PIR; A40684; A40684. DR RefSeq; NP_031923.1; NM_007897.3. [Q07802-1] DR RefSeq; XP_006532219.1; XM_006532156.3. DR PDB; 3MLN; X-ray; 2.40 A; A/B/E=24-241. DR PDB; 3MLO; X-ray; 3.01 A; A/B=24-241. DR PDB; 3MLP; X-ray; 2.80 A; A/B/E/F=24-421. DR PDBsum; 3MLN; -. DR PDBsum; 3MLO; -. DR PDBsum; 3MLP; -. DR AlphaFoldDB; Q07802; -. DR SMR; Q07802; -. DR BioGRID; 199358; 1. DR STRING; 10090.ENSMUSP00000099857; -. DR GlyGen; Q07802; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q07802; -. DR PhosphoSitePlus; Q07802; -. DR MaxQB; Q07802; -. DR PaxDb; 10090-ENSMUSP00000080020; -. DR ProteomicsDB; 283416; -. [Q07802-1] DR ProteomicsDB; 283417; -. [Q07802-2] DR Pumba; Q07802; -. DR Antibodypedia; 28482; 203 antibodies from 30 providers. DR DNASU; 13591; -. DR Ensembl; ENSMUST00000081265.12; ENSMUSP00000080020.6; ENSMUSG00000057098.15. [Q07802-1] DR GeneID; 13591; -. DR KEGG; mmu:13591; -. DR UCSC; uc007ink.2; mouse. [Q07802-1] DR AGR; MGI:95275; -. DR CTD; 1879; -. DR MGI; MGI:95275; Ebf1. DR VEuPathDB; HostDB:ENSMUSG00000057098; -. DR eggNOG; KOG3836; Eukaryota. DR GeneTree; ENSGT00950000182859; -. DR InParanoid; Q07802; -. DR OMA; LMIPRCL; -. DR OrthoDB; 3641706at2759; -. DR TreeFam; TF313391; -. DR BioGRID-ORCS; 13591; 6 hits in 79 CRISPR screens. DR ChiTaRS; Ebf1; mouse. DR EvolutionaryTrace; Q07802; -. DR PRO; PR:Q07802; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q07802; Protein. DR Bgee; ENSMUSG00000057098; Expressed in external carotid artery and 261 other cell types or tissues. DR ExpressionAtlas; Q07802; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO: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: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: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:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 1.10.287.4280; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.60.40.3180; Transcription factor COE1, DNA-binding domain; 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; TRANSCRIPTION FACTOR COE FAMILY MEMBER; 1. DR PANTHER; PTHR10747:SF26; TRANSCRIPTION FACTOR COE1; 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; E set domains; 1. DR PROSITE; PS01345; COE; 1. DR Genevisible; Q07802; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Developmental protein; Direct protein sequencing; DNA-binding; KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..591 FT /note="Transcription factor COE1" FT /id="PRO_0000107826" FT DOMAIN 262..345 FT /note="IPT/TIG" FT ZN_FING 151..170 FT /note="C5-type" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 63..66 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT REGION 197..204 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT REGION 236..239 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT REGION 457..480 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 163 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT SITE 172 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:20876732, FT ECO:0007744|PDB:3MLN, ECO:0007744|PDB:3MLO, FT ECO:0007744|PDB:3MLP" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9UH73" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9UH73" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q9UH73" FT VAR_SEQ 252..259 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000305" FT /id="VSP_001112" FT MUTAGEN 63 FT /note="R->A: Strongly reduced interaction with DNA." FT /evidence="ECO:0000269|PubMed:20876732" FT MUTAGEN 66 FT /note="N->A: Reduced interaction with DNA." FT /evidence="ECO:0000269|PubMed:20876732" FT MUTAGEN 163 FT /note="R->A: Strongly reduced interaction with DNA." FT /evidence="ECO:0000269|PubMed:20876732" FT MUTAGEN 203 FT /note="G->E: Strongly reduced interaction with DNA." FT /evidence="ECO:0000269|PubMed:20876732" FT MUTAGEN 235 FT /note="H->A: Strongly reduced interaction with DNA." FT /evidence="ECO:0000269|PubMed:20876732" FT CONFLICT 87 FT /note="T -> F (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="F -> L (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 39..44 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 66..76 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 83..93 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 108..115 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 121..132 FT /evidence="ECO:0007829|PDB:3MLN" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 157..160 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:3MLN" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:3MLN" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 187..194 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 221..228 FT /evidence="ECO:0007829|PDB:3MLN" FT STRAND 232..235 FT /evidence="ECO:0007829|PDB:3MLN" FT TURN 238..241 FT /evidence="ECO:0007829|PDB:3MLP" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 263..266 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 292..295 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 321..329 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:3MLP" FT STRAND 340..345 FT /evidence="ECO:0007829|PDB:3MLP" FT TURN 351..361 FT /evidence="ECO:0007829|PDB:3MLP" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:3MLP" SQ SEQUENCE 591 AA; 64464 MW; E47797B6FC1E5071 CRC64; MFGIQESIQR SGSSMKEEPL GSGMNAVRTW MQGAGVLDAN TAAQSGVGLA RAHFEKQPPS NLRKSNFFHF VLALYDRQGQ PVEIERTAFV GFVEKEKEAN SEKTNNGIHY RLQLLYSNGI RTEQDFYVRL IDSMTKQAIV YEGQDKNPEM CRVLLTHEIM CSRCCDKKSC GNRNETPSDP VIIDRFFLKF FLKCNQNCLK NAGNPRDMRR FQVVVSTTVN VDGHVLAVSD NMFVHNNSKH GRRARRLDPS EGTPSYLEHA TPCIKAISPS EGWTTGGATV IIIGDNFFDG LQVIFGTMLV WSELITPHAI RVQTPPRHIP GVVEVTLSYK SKQFCKGTPG RFIYTALNEP TIDYGFQRLQ KVIPRHPGDP ERLPKEVILK RAADLVEALY GMPHNNQEII LKRAADIAEA LYSVPRNHNQ LPALANTSVH AGMMGVNSFS GQLAVNVSEA SQATNQGFTR NSSSVSPHGY VPSTTPQQTN YNSVTTSMNG YGSAAMSNLG GSPTFLNGSA ANSPYAIVPS SPTMASSTSL PSNCSSSSGI FSFSPANMVS AVKQKSAFAP VVRPQTSPPP TCTSTNGNSL QAISGMIVPP M //