EDF1_MOUSE
ID EDF1_MOUSE Reviewed; 148 AA.
AC Q9JMG1; Q99NE6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Endothelial differentiation-related factor 1;
DE Short=EDF-1;
DE AltName: Full=Multiprotein-bridging factor 1;
DE Short=MBF1;
GN Name=Edf1;
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].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11587857; DOI=10.1016/s0378-1119(01)00660-6;
RA De Benedictis L., Mariotti M., Dragoni I., Maier J.A.M.;
RT "Cloning and characterization of murine EDF-1.";
RL Gene 275:299-304(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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, FOS and JUN via their conserved
CC basic region. Binding to calmodulin is regulated by calcium and
CC phosphorylation of the IQ motif (By similarity). {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 -!- TISSUE SPECIFICITY: Expressed in brain, liver, kidney and heart (at
CC protein level). Also expressed in testis.
CC {ECO:0000269|PubMed:11587857}.
CC -!- DEVELOPMENTAL STAGE: Very highly expressed seven days after
CC implantation, when gastrulation and neurulation occurs. Expression
CC decreases 11 days after implantation, when organogenesis is being
CC completed, and remains rather low up to late developmental stages.
CC {ECO:0000269|PubMed:11587857}.
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; AB030185; BAA92749.1; -; mRNA.
DR EMBL; AJ309569; CAC32040.1; -; mRNA.
DR EMBL; AK002345; BAB22026.1; -; mRNA.
DR EMBL; AK003557; BAB22854.1; -; mRNA.
DR EMBL; AK010191; BAB26758.1; -; mRNA.
DR EMBL; BC023472; AAH23472.1; -; mRNA.
DR CCDS; CCDS15780.1; -.
DR RefSeq; NP_067494.1; NM_021519.1.
DR AlphaFoldDB; Q9JMG1; -.
DR BMRB; Q9JMG1; -.
DR SMR; Q9JMG1; -.
DR BioGRID; 208490; 1.
DR STRING; 10090.ENSMUSP00000015236; -.
DR iPTMnet; Q9JMG1; -.
DR PhosphoSitePlus; Q9JMG1; -.
DR EPD; Q9JMG1; -.
DR jPOST; Q9JMG1; -.
DR MaxQB; Q9JMG1; -.
DR PaxDb; Q9JMG1; -.
DR PeptideAtlas; Q9JMG1; -.
DR PRIDE; Q9JMG1; -.
DR ProteomicsDB; 277796; -.
DR Antibodypedia; 18815; 221 antibodies from 33 providers.
DR DNASU; 59022; -.
DR Ensembl; ENSMUST00000015236; ENSMUSP00000015236; ENSMUSG00000015092.
DR GeneID; 59022; -.
DR KEGG; mmu:59022; -.
DR UCSC; uc008isn.1; mouse.
DR CTD; 8721; -.
DR MGI; MGI:1891227; Edf1.
DR VEuPathDB; HostDB:ENSMUSG00000015092; -.
DR eggNOG; KOG3398; Eukaryota.
DR GeneTree; ENSGT00390000008519; -.
DR HOGENOM; CLU_112609_0_1_1; -.
DR InParanoid; Q9JMG1; -.
DR OMA; NKAHQGT; -.
DR OrthoDB; 1571466at2759; -.
DR PhylomeDB; Q9JMG1; -.
DR TreeFam; TF300064; -.
DR BioGRID-ORCS; 59022; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Edf1; mouse.
DR PRO; PR:Q9JMG1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JMG1; protein.
DR Bgee; ENSMUSG00000015092; Expressed in paneth cell and 270 other tissues.
DR Genevisible; Q9JMG1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:MGI.
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; 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_0000149796"
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 /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"
FT CONFLICT 146
FT /note="K -> R (in Ref. 2; CAC32040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16369 MW; ADC000D8492A8C11 CRC64;
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK
LDRETEELHH DRVTLEVGKV IQRGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV
LGKIERAIGL KLRGKDIGKP IEKGPKAK
