COE1_RAT
ID COE1_RAT Reviewed; 584 AA.
AC Q63398;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transcription factor COE1;
DE Short=O/E-1;
DE Short=OE-1;
DE AltName: Full=Early B-cell factor;
DE AltName: Full=Olf-1;
DE AltName: Full=Olfactory neuronal transcription factor;
GN Name=Ebf1; Synonyms=Coe1, Ebf, Olf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=8321284; DOI=10.1038/364121a0;
RA Wang M.M., Reed R.R.;
RT "Molecular cloning of the olfactory neuronal transcription factor Olf-1 by
RT genetic selection in yeast.";
RL Nature 364:121-126(1993).
RN [2]
RP INTERACTION WITH ZNF423.
RX PubMed=9151733; DOI=10.1523/jneurosci.17-11-04159.1997;
RA Tsai R.Y.L., Reed R.R.;
RT "Cloning and functional characterization of Roaz, a zinc finger protein
RT that interacts with O/E-1 to regulate gene expression: implications for
RT olfactory neuronal development.";
RL J. Neurosci. 17:4159-4169(1997).
CC -!- FUNCTION: Key pioneer transcription factor of B-cell specification and
CC commitment. Recognizes variations of the palindromic sequence 5'-
CC ATTCCCNNGGGAATT-3'. Operates in a transcription factor network to
CC activate B-cell-specific genes and repress genes associated with
CC alternative cell fates. For instance, positively regulates many B-cell
CC specific genes including BCR or CD40 while repressing genes that direct
CC cells into alternative lineages, including GATA3 and TCF7 for the T-
CC cell lineage. In addition to its role during lymphopoiesis, controls
CC the thermogenic gene program in adipocytes during development and in
CC response to environmental cold. {ECO:0000250|UniProtKB:Q07802}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ZNF423 and ZNF521,
CC leading to prevent EBF1 to bind DNA and activate target genes
CC (PubMed:9151733). Interacts with CCR4-NOT component CNOT3 (By
CC similarity). {ECO:0000250|UniProtKB:Q07802,
CC ECO:0000250|UniProtKB:Q9UH73, ECO:0000269|PubMed:9151733}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in olfactory receptor neurons
CC and their precursors.
CC -!- SIMILARITY: Belongs to the COE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L24051; AAA41759.1; ALT_INIT; mRNA.
DR PIR; S35069; S35069.
DR RefSeq; NP_446272.2; NM_053820.2.
DR AlphaFoldDB; Q63398; -.
DR SMR; Q63398; -.
DR BioGRID; 250478; 1.
DR STRING; 10116.ENSRNOP00000068319; -.
DR PaxDb; Q63398; -.
DR GeneID; 116543; -.
DR KEGG; rno:116543; -.
DR UCSC; RGD:620953; rat.
DR CTD; 1879; -.
DR RGD; 620953; Ebf1.
DR VEuPathDB; HostDB:ENSRNOG00000028845; -.
DR eggNOG; KOG3836; Eukaryota.
DR HOGENOM; CLU_016320_3_1_1; -.
DR InParanoid; Q63398; -.
DR OMA; DDLFLHR; -.
DR OrthoDB; 817293at2759; -.
DR PhylomeDB; Q63398; -.
DR TreeFam; TF313391; -.
DR PRO; PR:Q63398; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000028845; Expressed in spleen and 17 other tissues.
DR ExpressionAtlas; Q63398; baseline and differential.
DR Genevisible; Q63398; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
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; ISO:RGD.
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 Acetylation; Activator; Developmental protein; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..584
FT /note="Transcription factor COE1"
FT /id="PRO_0000107827"
FT DOMAIN 255..338
FT /note="IPT/TIG"
FT ZN_FING 151..170
FT /note="C5-type"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
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:0000250|UniProtKB:Q07802"
FT REGION 197..204
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 236..239
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
FT REGION 450..473
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:0000250|UniProtKB:Q07802"
FT SITE 172
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q07802"
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"
SQ SEQUENCE 584 AA; 63650 MW; 1E903A9801BBCFEA 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 EAATPCIKAI SPSEGWTTGG ATVIIIGDNF FDGLQVIFGT MLVWSELITP
HAIRVQTPPR HIPGVVEVTL SYKSKQFCKG TPGRFIYTAL NEPTIDYGFQ RLQKVIPRHP
GDPERLPKEV ILKRAADLVE ALYGMPHNNQ EIILKRAADI AEALYSVPRN HNQLPALANT
SVHAGMMGVN SFSGQLAVNV SEASQATNQG FTRNSSSVSP HGYVPSTTPQ QTNYNSVTTS
MNGYGSAAMS NLGGSPTFLN GSAANSPYAI VPSSPTMASS TSLPSNCSSS SGIFSFSPAN
MVSAVKQKSA FAPVVRPQTS PPPTCTSTNG NSLQAISGMI VPPM
