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LIM/homeobox protein Lhx3 (LIM homeobox protein 3) (Homeobox protein LIM-3) (Homeobox protein P-LIM)

 LHX3_MOUSE              Reviewed;         400 AA.
P50481; A2ALD9; Q61800; Q61801;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 162.
RecName: Full=LIM/homeobox protein Lhx3;
Short=LIM homeobox protein 3;
AltName: Full=Homeobox protein LIM-3;
AltName: Full=Homeobox protein P-LIM;
Name=Lhx3; Synonyms=Lim-3, Lim3, Plim;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (LIM3A).
TISSUE=Pituitary;
PubMed=7811383; DOI=10.1089/dna.1994.13.1163;
Seidah N.G., Barale J.-C., Marcinkiewicz M., Mattei M.-G., Day R.,
Chretien M.;
"The mouse homeoprotein mLIM-3 is expressed early in cells derived
from the neuroepithelium and persists in adult pituitary.";
DNA Cell Biol. 13:1163-1180(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (LIM3A).
TISSUE=Pituitary;
PubMed=7708713; DOI=10.1073/pnas.92.7.2720;
Bach I., Rhodes S.J., Pearse R.V. II, Heinzel T., Gloss B.,
Scully K.M., Sawchenko P.E., Rosenfeld M.G.;
"P-Lim, a LIM homeodomain factor, is expressed during pituitary organ
and cell commitment and synergizes with Pit-1.";
Proc. Natl. Acad. Sci. U.S.A. 92:2720-2724(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (LIM3A AND LIM3B).
STRAIN=DBA/N, and NIH Swiss; TISSUE=Pituitary;
PubMed=7626792; DOI=10.1002/aja.1002020405;
Zhadanov A.B., Bertuzzi S., Taira M., Dawid I.B., Westphal H.;
"Expression pattern of the murine LIM class homeobox gene Lhx3 in
subsets of neural and neuroendocrine tissues.";
Dev. Dyn. 202:354-364(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:AAI50690.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=10593900; DOI=10.1074/jbc.274.51.36159;
Glenn D.J., Maurer R.A.;
"MRG1 binds to the LIM domain of Lhx2 and may function as a
coactivator to stimulate glycoprotein hormone alpha-subunit gene
expression.";
J. Biol. Chem. 274:36159-36167(1999).
[6]
FUNCTION, AND INTERACTION WITH LDB1 AND ISL1.
PubMed=12150931; DOI=10.1016/S0092-8674(02)00823-1;
Thaler J.P., Lee S.K., Jurata L.W., Gill G.N., Pfaff S.L.;
"LIM factor Lhx3 contributes to the specification of motor neuron and
interneuron identity through cell-type-specific protein-protein
interactions.";
Cell 110:237-249(2002).
[7]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 28-153 IN COMPLEX WITH ISL1.
PubMed=18583962; DOI=10.1038/emboj.2008.123;
Bhati M., Lee C., Nancarrow A.L., Lee M., Craig V.J., Bach I.,
Guss J.M., Mackay J.P., Matthews J.M.;
"Implementing the LIM code: the structural basis for cell type-
specific assembly of LIM-homeodomain complexes.";
EMBO J. 27:2018-2029(2008).
-!- FUNCTION: Required for the establishment of the specialized cells
of the pituitary gland and the nervous system (By similarity).
Involved in the development of interneurons and motor neurons in
cooperation with LDB1 and ISL1. Acts as a transcriptional
activator. Binds to and activates the promoter of the alpha-
glycoprotein gene, and synergistically enhances transcription from
the prolactin promoter in cooperation with Pou1f1/Pit-1.
{ECO:0000250, ECO:0000269|PubMed:10593900,
ECO:0000269|PubMed:12150931}.
-!- SUBUNIT: Interacts with POU1F1 (By similarity). At neuronal
promoters, interacts with LDB1, in motor neurons LDB1 is displaced
by ISL1 and a ternary complex is formed in which ISL1 contacts
both LHX3 and LDB1 (PubMed:12150931, PubMed:18583962).
{ECO:0000250|UniProtKB:Q9UBR4, ECO:0000269|PubMed:12150931,
ECO:0000269|PubMed:18583962}.
-!- INTERACTION:
P61372:Isl1; NbExp=7; IntAct=EBI-7988290, EBI-7988215;
P70662:Ldb1; NbExp=5; IntAct=EBI-7988290, EBI-6272082;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=LIM3A;
IsoId=P50481-1; Sequence=Displayed;
Name=LIM3B;
IsoId=P50481-2; Sequence=VSP_003108;
-!- TISSUE SPECIFICITY: Mostly expressed in the pituitary anterior and
intermediate lobes of the adult mouse. It is also expressed in the
pineal gland and transiently in the primordia of motor neurons
including the spinal cord, pons and medulla oblongata.
-!- DEVELOPMENTAL STAGE: Expressed throughout pituitary development.
Detected on embryonic day 11 (E11) in the primordium of the
hypophysis. Following a maximum between E12 and E14, lower levels
persisted into adulthood.
-!- DOMAIN: The LIM domain specifically interacts with the Pit-1 POU
domain and is required for synergistic interactions with Pit-1,
but not for basal transcriptional activation events.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L33776; AAA62369.1; -; Genomic_DNA.
EMBL; L38857; AAA73902.1; -; mRNA.
EMBL; L38249; AAA98998.1; -; mRNA.
EMBL; L38248; AAB64178.1; -; mRNA.
EMBL; BC150689; AAI50690.1; -; mRNA.
CCDS; CCDS38081.1; -. [P50481-2]
CCDS; CCDS71004.1; -. [P50481-1]
PIR; I59360; I59360.
RefSeq; NP_001034742.1; NM_001039653.2. [P50481-2]
RefSeq; NP_034841.2; NM_010711.2. [P50481-1]
UniGene; Mm.386765; -.
PDB; 2JTN; NMR; -; A=28-153.
PDB; 2RGT; X-ray; 2.05 A; A/B=28-153.
PDBsum; 2JTN; -.
PDBsum; 2RGT; -.
ProteinModelPortal; P50481; -.
SMR; P50481; -.
CORUM; P50481; -.
IntAct; P50481; 2.
MINT; P50481; -.
STRING; 10090.ENSMUSP00000028302; -.
PhosphoSitePlus; P50481; -.
PaxDb; P50481; -.
PRIDE; P50481; -.
Ensembl; ENSMUST00000028302; ENSMUSP00000028302; ENSMUSG00000026934. [P50481-2]
Ensembl; ENSMUST00000054099; ENSMUSP00000056822; ENSMUSG00000026934. [P50481-1]
GeneID; 16871; -.
KEGG; mmu:16871; -.
UCSC; uc008iug.1; mouse. [P50481-1]
CTD; 8022; -.
MGI; MGI:102673; Lhx3.
eggNOG; KOG4577; Eukaryota.
eggNOG; ENOG410XPDC; LUCA.
GeneTree; ENSGT00940000160316; -.
HOGENOM; HOG000231629; -.
HOVERGEN; HBG006263; -.
InParanoid; P50481; -.
KO; K09374; -.
OMA; PLCAGCN; -.
TreeFam; TF315442; -.
EvolutionaryTrace; P50481; -.
PRO; PR:P50481; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026934; Expressed in 80 organ(s), highest expression level in head.
CleanEx; MM_LHX3; -.
ExpressionAtlas; P50481; baseline and differential.
Genevisible; P50481; MM.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0021526; P:medial motor column neuron differentiation; IGI:MGI.
GO; GO:0008045; P:motor neuron axon guidance; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0021983; P:pituitary gland development; IMP:MGI.
GO; GO:0001890; P:placenta development; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0021527; P:spinal cord association neuron differentiation; IDA:MGI.
GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IGI:MGI.
GO; GO:0021521; P:ventral spinal cord interneuron specification; IDA:MGI.
CDD; cd00086; homeodomain; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017970; Homeobox_CS.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00046; Homeodomain; 1.
Pfam; PF00412; LIM; 2.
SMART; SM00389; HOX; 1.
SMART; SM00132; LIM; 2.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS00027; HOMEOBOX_1; 1.
PROSITE; PS50071; HOMEOBOX_2; 1.
PROSITE; PS00478; LIM_DOMAIN_1; 2.
PROSITE; PS50023; LIM_DOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
DNA-binding; Homeobox; LIM domain; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Zinc.
CHAIN 1 400 LIM/homeobox protein Lhx3.
/FTId=PRO_0000075782.
DOMAIN 34 84 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 93 147 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DNA_BIND 160 219 Homeobox. {ECO:0000255|PROSITE-
ProRule:PRU00108}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBR4}.
MOD_RES 230 230 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9UBR4}.
MOD_RES 237 237 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBR4}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBR4}.
VAR_SEQ 1 29 MLLEAELDCHRERPGAPGASALCTFSRTP -> MEARGELD
PSRESAGGDLLLALLARRADLRR (in isoform
LIM3B). {ECO:0000305}.
/FTId=VSP_003108.
CONFLICT 26 26 S -> N (in Ref. 3; AAA98998).
{ECO:0000305}.
CONFLICT 76 76 G -> R (in Ref. 2; AAA73902).
{ECO:0000305}.
CONFLICT 311 312 EL -> DV (in Ref. 2; AAA73902).
{ECO:0000305}.
CONFLICT 351 378 PSGPPGGPPPMRVLAGNGPSSDLSTESS -> LQGPQVDPG
PTHEGCWLEMARTCPQRAG (in Ref. 2).
{ECO:0000305}.
STRAND 33 40 {ECO:0000244|PDB:2RGT}.
STRAND 43 45 {ECO:0000244|PDB:2RGT}.
STRAND 52 54 {ECO:0000244|PDB:2JTN}.
TURN 56 58 {ECO:0000244|PDB:2RGT}.
TURN 62 64 {ECO:0000244|PDB:2RGT}.
STRAND 73 77 {ECO:0000244|PDB:2RGT}.
STRAND 78 80 {ECO:0000244|PDB:2JTN}.
HELIX 82 89 {ECO:0000244|PDB:2RGT}.
TURN 94 96 {ECO:0000244|PDB:2RGT}.
STRAND 104 109 {ECO:0000244|PDB:2RGT}.
STRAND 112 115 {ECO:0000244|PDB:2RGT}.
HELIX 116 118 {ECO:0000244|PDB:2RGT}.
TURN 122 124 {ECO:0000244|PDB:2RGT}.
STRAND 133 136 {ECO:0000244|PDB:2RGT}.
STRAND 142 144 {ECO:0000244|PDB:2RGT}.
HELIX 145 147 {ECO:0000244|PDB:2RGT}.
HELIX 148 153 {ECO:0000244|PDB:2RGT}.
SEQUENCE 400 AA; 44010 MW; AD7A9453CFACC730 CRC64;
MLLEAELDCH RERPGAPGAS ALCTFSRTPE IPMCAGCDQH ILDRFILKAL DRHWHSKCLK
CSDCHVPLAE RCFSRGESVY CKDDFFKRFG TKCAACQLGI PPTQVVRRAQ DFVYHLHCFA
CVVCKRQLAT GDEFYLMEDS RLVCKADYET AKQREAEATA KRPRTTITAK QLETLKSAYN
TSPKPARHVR EQLSSETGLD MRVVQVWFQN RRAKEKRLKK DAGRQRWGQY FRNMKRSRGS
SKSDKDSIQE GQDSDAEVSF TDEPSMADMG PANGLYSSLG EPAPALGRPV GGLGSFTLDH
GGLTGPEQYR ELRPGSPYGI PPSPAAPQSL PGPQPLLSSL VYPDTNLSLV PSGPPGGPPP
MRVLAGNGPS SDLSTESSSG YPDFPASPAS WLDEVDHAQF


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