LMO4_MOUSE
ID LMO4_MOUSE Reviewed; 165 AA.
AC P61969; O00158; O88894;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=LIM domain transcription factor LMO4;
DE AltName: Full=Breast tumor autoantigen;
DE AltName: Full=LIM domain only protein 4;
DE Short=LMO-4;
GN Name=Lmo4;
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].
RX PubMed=9736723; DOI=10.1073/pnas.95.19.11257;
RA Kenny D.A., Jurata L.W., Saga Y., Gill G.N.;
RT "Identification and characterization of LMO4, an LMO gene with a novel
RT pattern of expression during embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11257-11262(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9860983; DOI=10.1073/pnas.95.26.15418;
RA Sugihara T.M., Bach I., Kioussi C., Rosenfeld M.G., Andersen B.;
RT "Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain
RT factor, LMO-4, and CLIM coregulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15418-15423(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9840944; DOI=10.1038/sj.onc.1202502;
RA Grutz G., Forster A., Rabbitts T.H.;
RT "Identification of the LMO4 gene encoding an interaction partner of the
RT LIM-binding protein LDB1/NLI1: a candidate for displacement by LMO proteins
RT in T cell acute leukaemia.";
RL Oncogene 17:2799-2803(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 INTERACTION WITH BRCA1 AND RBBP8.
RX PubMed=11751867; DOI=10.1074/jbc.m110603200;
RA Sum E.Y., Peng B., Yu X., Chen J., Byrne J., Lindeman G.J., Visvader J.E.;
RT "The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor
RT suppressor BRCA1 and inhibits BRCA1 activity.";
RL J. Biol. Chem. 277:7849-7856(2002).
RN [6]
RP INTERACTION WITH DEAF1.
RX PubMed=22723967; DOI=10.1371/journal.pone.0039218;
RA Cubeddu L., Joseph S., Richard D.J., Matthews J.M.;
RT "Contribution of DEAF1 structural domains to the interaction with the
RT breast cancer oncogene LMO4.";
RL PLoS ONE 7:E39218-E39218(2012).
RN [7]
RP STRUCTURE BY NMR OF 16-86 IN COMPLEX WITH LDB1.
RX PubMed=12727888; DOI=10.1093/emboj/cdg196;
RA Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E.,
RA Matthews J.M.;
RT "Structural basis for the recognition of ldb1 by the N-terminal LIM domains
RT of LMO2 and LMO4.";
RL EMBO J. 22:2224-2233(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 16-152 IN COMPLEX WITH LDB1.
RX PubMed=15343268; DOI=10.1038/sj.emboj.7600376;
RA Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E.,
RA Matthews J.M.;
RT "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.";
RL EMBO J. 23:3589-3598(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 18-152 IN COMPLEX WITH LDB1.
RX PubMed=17001033; DOI=10.1110/ps.062377006;
RA Jeffries C.M., Graham S.C., Stokes P.H., Collyer C.A., Guss J.M.,
RA Matthews J.M.;
RT "Stabilization of a binary protein complex by intein-mediated
RT cyclization.";
RL Protein Sci. 15:2612-2618(2006).
CC -!- FUNCTION: Probable transcriptional factor.
CC -!- SUBUNIT: Interacts strongly with LDBS. Interacts with CLIM1 and CLIM2.
CC Interacts (via the LIM zinc-binding domain 1) with RBBP8. Interacts
CC with BRCA1 (via the BRCT domains); the interaction represses BRCA1
CC transcriptional activity. Interacts with DEAF1; LMO4 blocks export from
CC nucleus. {ECO:0000269|PubMed:11751867, ECO:0000269|PubMed:12727888,
CC ECO:0000269|PubMed:15343268, ECO:0000269|PubMed:17001033,
CC ECO:0000269|PubMed:22723967}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
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DR EMBL; AF074600; AAC62958.1; -; mRNA.
DR EMBL; AF102817; AAC98510.1; -; mRNA.
DR EMBL; AF096996; AAC83789.1; -; mRNA.
DR EMBL; BC003488; AAH03488.1; -; mRNA.
DR EMBL; BC004661; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC010278; AAH10278.3; -; mRNA.
DR CCDS; CCDS51085.1; -.
DR RefSeq; NP_001155241.1; NM_001161769.1.
DR RefSeq; NP_001155242.1; NM_001161770.1.
DR RefSeq; NP_034853.1; NM_010723.3.
DR PDB; 1M3V; NMR; -; A=16-86.
DR PDB; 1RUT; X-ray; 1.30 A; X=16-152.
DR PDB; 2DFY; X-ray; 1.65 A; C/X=18-161.
DR PDB; 2MBV; NMR; -; A=77-147.
DR PDBsum; 1M3V; -.
DR PDBsum; 1RUT; -.
DR PDBsum; 2DFY; -.
DR PDBsum; 2MBV; -.
DR AlphaFoldDB; P61969; -.
DR BMRB; P61969; -.
DR SMR; P61969; -.
DR BioGRID; 201180; 11.
DR IntAct; P61969; 3.
DR STRING; 10090.ENSMUSP00000113840; -.
DR iPTMnet; P61969; -.
DR PhosphoSitePlus; P61969; -.
DR PaxDb; P61969; -.
DR PeptideAtlas; P61969; -.
DR PRIDE; P61969; -.
DR ProteomicsDB; 292103; -.
DR Antibodypedia; 33592; 305 antibodies from 34 providers.
DR DNASU; 16911; -.
DR Ensembl; ENSMUST00000120539; ENSMUSP00000113840; ENSMUSG00000028266.
DR Ensembl; ENSMUST00000121112; ENSMUSP00000113865; ENSMUSG00000028266.
DR Ensembl; ENSMUST00000121796; ENSMUSP00000113513; ENSMUSG00000028266.
DR GeneID; 16911; -.
DR KEGG; mmu:16911; -.
DR UCSC; uc008rpl.2; mouse.
DR CTD; 8543; -.
DR MGI; MGI:109360; Lmo4.
DR VEuPathDB; HostDB:ENSMUSG00000028266; -.
DR eggNOG; KOG0490; Eukaryota.
DR GeneTree; ENSGT00940000157730; -.
DR HOGENOM; CLU_001357_7_1_1; -.
DR InParanoid; P61969; -.
DR OMA; NNVVRCC; -.
DR OrthoDB; 1307952at2759; -.
DR PhylomeDB; P61969; -.
DR TreeFam; TF351071; -.
DR BioGRID-ORCS; 16911; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Lmo4; mouse.
DR EvolutionaryTrace; P61969; -.
DR PRO; PR:P61969; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P61969; protein.
DR Bgee; ENSMUSG00000028266; Expressed in embryonic brain and 299 other tissues.
DR ExpressionAtlas; P61969; baseline and differential.
DR Genevisible; P61969; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0050865; P:regulation of cell activation; IMP:MGI.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IGI:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IDA:MGI.
DR GO; GO:0048538; P:thymus development; IGI:MGI.
DR GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IDA:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR IDEAL; IID50048; -.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; LIM domain; Metal-binding; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..165
FT /note="LIM domain transcription factor LMO4"
FT /id="PRO_0000075821"
FT DOMAIN 23..83
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 87..147
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2DFY"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2DFY"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2DFY"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2DFY"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:2DFY"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2DFY"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2DFY"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2DFY"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2DFY"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2DFY"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2DFY"
SQ SEQUENCE 165 AA; 17994 MW; C8AC295144AD7787 CRC64;
MVNPGSSSQP PPVTAGSLSW KRCAGCGGKI ADRFLLYAMD SYWHSRCLKC SCCQAQLGDI
GTSCYTKSGM ILCRNDYIRL FGNSGACSAC GQSIPASELV MRAQGNVYHL KCFTCSTCRN
RLVPGDRFHY INGSLFCEHD RPTALINGHL NSLQSNPLLP DQKVC
