EDF1_BOVIN
ID EDF1_BOVIN Reviewed; 148 AA.
AC Q3T0V7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Endothelial differentiation-related factor 1;
DE Short=EDF-1;
GN Name=EDF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional coactivator stimulating NR5A1 and ligand-
CC dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the
CC DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric
CC oxid synthase activity probably by sequestering calmodulin in the
CC cytoplasm. Might function in endothelial cells differentiation,
CC hormone-induced cardiomyocytes hypertrophy and lipid metabolism (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TBP and the transcription factor IID (TFIID)
CC complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by
CC phosphorylation. Binds NR5A1, ATF1 and FOS via their conserved basic
CC region. Interacts with JUN. Binding to calmodulin is regulated by
CC calcium and phosphorylation of the IQ motif (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA
CC or forskolin. {ECO:0000250}.
CC -!- DOMAIN: The IQ motif, which is involved in calmodulin binding, overlaps
CC with the binding domain for nuclear receptors and transcription
CC factors. Its phosphorylation probably allows a switch between the two
CC activities of the protein (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC102246; AAI02247.1; -; mRNA.
DR RefSeq; NP_001030384.1; NM_001035307.2.
DR AlphaFoldDB; Q3T0V7; -.
DR BMRB; Q3T0V7; -.
DR SMR; Q3T0V7; -.
DR STRING; 9913.ENSBTAP00000040410; -.
DR PaxDb; Q3T0V7; -.
DR PeptideAtlas; Q3T0V7; -.
DR PRIDE; Q3T0V7; -.
DR Ensembl; ENSBTAT00000042787; ENSBTAP00000040410; ENSBTAG00000030302.
DR GeneID; 515380; -.
DR KEGG; bta:515380; -.
DR CTD; 8721; -.
DR VEuPathDB; HostDB:ENSBTAG00000030302; -.
DR VGNC; VGNC:28325; EDF1.
DR eggNOG; KOG3398; Eukaryota.
DR GeneTree; ENSGT00390000008519; -.
DR HOGENOM; CLU_112609_0_1_1; -.
DR InParanoid; Q3T0V7; -.
DR OMA; NKAHQGT; -.
DR OrthoDB; 1571466at2759; -.
DR TreeFam; TF300064; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000030302; Expressed in laryngeal cartilage and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Calmodulin-binding; Cytoplasm;
KW Developmental protein; Differentiation; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60869"
FT CHAIN 2..148
FT /note="Endothelial differentiation-related factor 1"
FT /id="PRO_0000247012"
FT DOMAIN 81..135
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 92..111
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT REGION 33..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..113
FT /note="Interaction with NR5A2, PPARG and NR1H3"
FT /evidence="ECO:0000250"
FT REGION 69..108
FT /note="Interaction with TBP and NR5A1"
FT /evidence="ECO:0000250"
FT MOTIF 81..88
FT /note="IQ motif"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60869"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60869"
FT MOD_RES 25
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60869"
SQ SEQUENCE 148 AA; 16369 MW; ADC2C5384BF85C11 CRC64;
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK
LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV
LGKIERAIGL KLRGKDIGKP IEKGPRAK
