COE1_MOUSE
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 03-AUG-2022, entry version 172.
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}.
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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.ENSMUSP00000080020; -.
DR iPTMnet; Q07802; -.
DR PhosphoSitePlus; Q07802; -.
DR MaxQB; Q07802; -.
DR PaxDb; Q07802; -.
DR PRIDE; Q07802; -.
DR ProteomicsDB; 283416; -. [Q07802-1]
DR ProteomicsDB; 283417; -. [Q07802-2]
DR Antibodypedia; 28482; 188 antibodies from 30 providers.
DR DNASU; 13591; -.
DR Ensembl; ENSMUST00000081265; ENSMUSP00000080020; ENSMUSG00000057098. [Q07802-1]
DR GeneID; 13591; -.
DR KEGG; mmu:13591; -.
DR UCSC; uc007ink.2; mouse. [Q07802-1]
DR CTD; 1879; -.
DR MGI; MGI:95275; Ebf1.
DR VEuPathDB; HostDB:ENSMUSG00000057098; -.
DR eggNOG; KOG3836; Eukaryota.
DR GeneTree; ENSGT00950000182859; -.
DR InParanoid; Q07802; -.
DR OMA; DDLFLHR; -.
DR TreeFam; TF313391; -.
DR BioGRID-ORCS; 13591; 6 hits in 74 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 260 other tissues.
DR ExpressionAtlas; Q07802; baseline and differential.
DR Genevisible; Q07802; MM.
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: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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 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
