LHX2_MOUSE
ID LHX2_MOUSE Reviewed; 406 AA.
AC Q9Z0S2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=LIM/homeobox protein Lhx2;
DE Short=Homeobox protein LH-2;
DE Short=LIM homeobox protein 2;
GN Name=Lhx2;
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=10051612; DOI=10.1073/pnas.96.5.2165;
RA Rincon-Limas D.E., Lu C.-H., Canal I., Calleja M., Rodriguez-Esteban C.,
RA Izpisua-Belmonte J.-C., Botas J.;
RT "Conservation of the expression and function of apterous orthologs in
RT Drosophila and mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2165-2170(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, INTERACTION WITH CITED2, AND MUTAGENESIS OF CYS-53 AND CYS-56.
RX PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
RA Glenn D.J., Maurer R.A.;
RT "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to
RT stimulate glycoprotein hormone alpha-subunit gene expression.";
RL J. Biol. Chem. 274:36159-36167(1999).
RN [4]
RP INTERACTION WITH POU4F2.
RX PubMed=24643061; DOI=10.1371/journal.pone.0092105;
RA Li R., Wu F., Ruonala R., Sapkota D., Hu Z., Mu X.;
RT "Isl1 and Pou4f2 form a complex to regulate target genes in developing
RT retinal ganglion cells.";
RL PLoS ONE 9:E92105-E92105(2014).
CC -!- FUNCTION: Acts as a transcriptional activator. Stimulates the promoter
CC of the alpha-glycoprotein gene. Transcriptional regulatory protein
CC involved in the control of cell differentiation in developing lymphoid
CC and neural cell types. {ECO:0000269|PubMed:10593900}.
CC -!- SUBUNIT: Interacts (via LIM domains) with CITED2 (PubMed:10593900).
CC Interacts with POU4F2 isoform 1 (PubMed:24643061).
CC {ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:24643061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: LIM domains are necessary for transcription activation.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF124734; AAD20012.1; -; mRNA.
DR EMBL; BC055741; AAH55741.1; -; mRNA.
DR CCDS; CCDS16008.1; -.
DR RefSeq; NP_034840.1; NM_010710.4.
DR AlphaFoldDB; Q9Z0S2; -.
DR SMR; Q9Z0S2; -.
DR BioGRID; 201155; 6.
DR IntAct; Q9Z0S2; 6.
DR STRING; 10090.ENSMUSP00000000253; -.
DR PhosphoSitePlus; Q9Z0S2; -.
DR MaxQB; Q9Z0S2; -.
DR PaxDb; Q9Z0S2; -.
DR PRIDE; Q9Z0S2; -.
DR ProteomicsDB; 291945; -.
DR Antibodypedia; 16286; 384 antibodies from 35 providers.
DR DNASU; 16870; -.
DR Ensembl; ENSMUST00000000253; ENSMUSP00000000253; ENSMUSG00000000247.
DR GeneID; 16870; -.
DR KEGG; mmu:16870; -.
DR UCSC; uc008jnk.2; mouse.
DR CTD; 9355; -.
DR MGI; MGI:96785; Lhx2.
DR VEuPathDB; HostDB:ENSMUSG00000000247; -.
DR eggNOG; KOG0490; Eukaryota.
DR GeneTree; ENSGT00940000158540; -.
DR InParanoid; Q9Z0S2; -.
DR OMA; AIFHLEC; -.
DR PhylomeDB; Q9Z0S2; -.
DR TreeFam; TF315442; -.
DR BioGRID-ORCS; 16870; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Lhx2; mouse.
DR PRO; PR:Q9Z0S2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z0S2; protein.
DR Bgee; ENSMUSG00000000247; Expressed in ventricular zone and 135 other tissues.
DR ExpressionAtlas; Q9Z0S2; baseline and differential.
DR Genevisible; Q9Z0S2; MM.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IMP:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IGI:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IGI:MGI.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR GO; GO:0021978; P:telencephalon regionalization; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Homeobox; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..406
FT /note="LIM/homeobox protein Lhx2"
FT /id="PRO_0000075779"
FT DOMAIN 53..105
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 115..168
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 266..325
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 250..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..323
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 330..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 53
FT /note="C->A: Reduces transcriptional activation; when
FT associated with A-56."
FT /evidence="ECO:0000269|PubMed:10593900"
FT MUTAGEN 56
FT /note="C->A: Reduces transcriptional activation; when
FT associated with A-53."
FT /evidence="ECO:0000269|PubMed:10593900"
SQ SEQUENCE 406 AA; 44419 MW; FE7B4E76454D6A90 CRC64;
MLFHSLSGPE VHGVIDEMDR RAKSEAPAIS SAIDRGDTET TMPSISSDRA ALCAGCGGKI
SDRYYLLAVD KQWHMRCLKC CECKLNLESE LTCFSKDGSI YCKEDYYRRF SVQRCARCHL
GISASEMVMR ARDLVYHLNC FTCTTCNKML TTGDHFGMKD SLVYCRLHFE ALLQGEYPAH
FNHADVAAAA AAAAAAKSAG LGSAGANPLG LPYYNGVGTV QKGRPRKRKS PGPGADLAAY
NAALSCNEND AEHLDRDQPY PSSQKTKRMR TSFKHHQLRT MKSYFAINHN PDAKDLKQLA
QKTGLTKRVL QVWFQNARAK FRRNLLRQEN TGVDKTSDAT LQTGTPSGPA SELSNASLSP
SSTPTTLTDL TSPTLPTVTS VLTSVPGNLE GHEPHSPSQT TLTNLF
