EDF1_RAT
ID EDF1_RAT Reviewed; 148 AA.
AC P69736;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Endothelial differentiation-related factor 1;
DE Short=EDF-1;
DE AltName: Full=Calmodulin-associated peptide 19;
DE Short=CAP-19;
DE AltName: Full=Multiprotein-bridging factor 1;
DE Short=MBF1;
GN Name=Edf1;
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], IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH CALM.
RC TISSUE=Brain cortex;
RX PubMed=9795107; DOI=10.1016/s0169-328x(98)00207-1;
RA Smith M.L., Johanson R.A., Rogers K.E., Coleman P.D., Slemmon J.R.;
RT "Identification of a neuronal calmodulin-binding peptide, CAP-19,
RT containing an IQ motif.";
RL Brain Res. Mol. Brain Res. 62:12-24(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH CALM AND JUN, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF SER-87, AND FUNCTION.
RX PubMed=12729799; DOI=10.1016/s0014-4827(03)00091-0;
RA Busk P.K., Wulf-Andersen L., Stroem C.C., Enevoldsen M., Thirstrup K.,
RA Haunsoe S., Sheikh S.P.;
RT "Multiprotein bridging factor 1 cooperates with c-Jun and is necessary for
RT cardiac hypertrophy in vitro.";
RL Exp. Cell Res. 286:102-114(2003).
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, ECO:0000269|PubMed:12729799}.
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 (By similarity). Interacts with JUN. Binding to calmodulin is
CC regulated by calcium and phosphorylation of the IQ motif. {ECO:0000250,
CC ECO:0000269|PubMed:12729799, ECO:0000269|PubMed:9795107}.
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 (By similarity). Localized mainly in soma and dendritic
CC processes of neurons. {ECO:0000250, ECO:0000269|PubMed:12729799}.
CC -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes, cortical and
CC hippocampal neurons. {ECO:0000269|PubMed:12729799,
CC ECO:0000269|PubMed:9795107}.
CC -!- DEVELOPMENTAL STAGE: Expressed in newborn and adult heart and brain
CC tissues. Expression is not evident in prenatal days.
CC {ECO:0000269|PubMed:12729799, ECO:0000269|PubMed:9795107}.
CC -!- INDUCTION: Up-regulated upon cardiomyocytes hypertrophy.
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.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; CO400850; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001100027.1; NM_001106557.1.
DR AlphaFoldDB; P69736; -.
DR BMRB; P69736; -.
DR SMR; P69736; -.
DR BioGRID; 255402; 1.
DR IntAct; P69736; 1.
DR MINT; P69736; -.
DR STRING; 10116.ENSRNOP00000022196; -.
DR iPTMnet; P69736; -.
DR PhosphoSitePlus; P69736; -.
DR jPOST; P69736; -.
DR PaxDb; P69736; -.
DR PRIDE; P69736; -.
DR GeneID; 296570; -.
DR KEGG; rno:296570; -.
DR UCSC; RGD:1308073; rat.
DR CTD; 8721; -.
DR RGD; 1308073; Edf1.
DR VEuPathDB; HostDB:ENSRNOG00000016272; -.
DR eggNOG; KOG3398; Eukaryota.
DR HOGENOM; CLU_112609_0_1_1; -.
DR InParanoid; P69736; -.
DR OMA; NKAHQGT; -.
DR OrthoDB; 1571466at2759; -.
DR PhylomeDB; P69736; -.
DR TreeFam; TF300064; -.
DR PRO; PR:P69736; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016272; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; P69736; baseline and differential.
DR Genevisible; P69736; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; 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_0000149797"
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 34..67
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 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"
FT MUTAGEN 87
FT /note="S->D: Loss of binding to CALM."
FT /evidence="ECO:0000269|PubMed:12729799"
SQ SEQUENCE 148 AA; 16369 MW; ADC000D8492A8C11 CRC64;
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK
LDRETEELHH DRVTLEVGKV IQRGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV
LGKIERAIGL KLRGKDIGKP IEKGPKAK
