LHX3_HUMAN
ID LHX3_HUMAN Reviewed; 397 AA.
AC Q9UBR4; Q5TB39; Q5TB40; Q9NZB5; Q9P0I8; Q9P0I9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=LIM/homeobox protein Lhx3;
DE Short=LIM homeobox protein 3;
GN Name=LHX3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=10598593; DOI=10.1210/mend.13.12.0395;
RA Sloop K.W., Meier B.C., Bridwell J.L., Parker G.E., Schiller A.M.,
RA Rhodes S.J.;
RT "Differential activation of pituitary hormone genes by human Lhx3 isoforms
RT with distinct DNA binding properties.";
RL Mol. Endocrinol. 13:2212-2225(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RA Sobrier M.-L.;
RT "Human LHX3: cloning, mapping, genomic structure.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA You X., Imperato-McGinley J., Zhu Y.-S.;
RT "Molecular cloning and expression pattern of human Lhx3 gene.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION AT THR-63; SER-71; TYR-227; SER-234 AND SER-238.
RX PubMed=15517599; DOI=10.1002/jcb.20287;
RA Parker G.E., West B.E., Witzmann F.A., Rhodes S.J.;
RT "Serine/threonine/tyrosine phosphorylation of the LHX3 LIM-homeodomain
RT transcription factor.";
RL J. Cell. Biochem. 94:67-80(2005).
RN [7]
RP FUNCTION.
RX PubMed=21149718; DOI=10.1073/pnas.1009501108;
RA Colvin S.C., Malik R.E., Showalter A.D., Sloop K.W., Rhodes S.J.;
RT "Model of pediatric pituitary hormone deficiency separates the endocrine
RT and neural functions of the LHX3 transcription factor in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:173-178(2011).
RN [8]
RP INTERACTION WITH POU1F1.
RX PubMed=26612202; DOI=10.1093/hmg/ddv486;
RA Sobrier M.L., Tsai Y.C., Perez C., Leheup B., Bouceba T., Duquesnoy P.,
RA Copin B., Sizova D., Penzo A., Stanger B.Z., Cooke N.E., Liebhaber S.A.,
RA Amselem S.;
RT "Functional characterization of a human POU1F1 mutation associated with
RT isolated growth hormone deficiency: a novel etiology for IGHD.";
RL Hum. Mol. Genet. 25:472-483(2016).
RN [9]
RP VARIANT CPHD3 CYS-111.
RX PubMed=10835633; DOI=10.1038/76041;
RA Netchine I., Sobrier M.-L., Krude H., Schnabel D., Maghnie M., Marcos E.,
RA Duriez B., Cacheux V., Moers A.V., Goossens M., Gruters A., Amselem S.;
RT "Mutations in LHX3 result in a new syndrome revealed by combined pituitary
RT hormone deficiency.";
RL Nat. Genet. 25:182-186(2000).
RN [10]
RP VARIANT CPHD3 VAL-210, AND CHARACTERIZATION OF VARIANT CPHD3 VAL-210.
RX PubMed=17327381; DOI=10.1210/jc.2006-2177;
RA Pfaeffle R.W., Savage J.J., Hunter C.S., Palme C., Ahlmann M., Kumar P.,
RA Bellone J., Schoenau E., Korsch E., Braemswig J.H., Stobbe H.M., Blum W.F.,
RA Rhodes S.J.;
RT "Four novel mutations of the LHX3 gene cause combined pituitary hormone
RT deficiencies with or without limited neck rotation.";
RL J. Clin. Endocrinol. Metab. 92:1909-1919(2007).
RN [11]
RP VARIANTS CPHD3 PHE-141 AND 151-ARG--PHE-397 DEL.
RX PubMed=28302169; DOI=10.1186/s12902-017-0164-8;
RA Ramzan K., Bin-Abbas B., Al-Jomaa L., Allam R., Al-Owain M., Imtiaz F.;
RT "Two novel LHX3 mutations in patients with combined pituitary hormone
RT deficiency including cervical rigidity and sensorineural hearing loss.";
RL BMC Endocr. Disord. 17:17-17(2017).
CC -!- FUNCTION: Acts as a transcriptional activator. Binds to and activates
CC the promoter of the alpha-glycoprotein gene, and synergistically
CC enhances transcription from the prolactin promoter in cooperation with
CC POU1F1/Pit-1 (By similarity). Required for the establishment of the
CC specialized cells of the pituitary gland and the nervous system.
CC Involved in the development of interneurons and motor neurons in
CC cooperation with LDB1 and ISL1. {ECO:0000250,
CC ECO:0000269|PubMed:21149718}.
CC -!- SUBUNIT: Interacts with POU1F1 (PubMed:26612202). At neuronal
CC promoters, interacts with LDB1, in motor neurons LDB1 is displaced by
CC ISL1 and a ternary complex is formed in which ISL1 contacts both LHX3
CC and LDB1 (By similarity). {ECO:0000250|UniProtKB:P50481,
CC ECO:0000269|PubMed:26612202}.
CC -!- INTERACTION:
CC Q9UBR4-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12039345, EBI-11096309;
CC Q9UBR4-2; Q08043: ACTN3; NbExp=5; IntAct=EBI-12039345, EBI-2880652;
CC Q9UBR4-2; Q9BQI0-4: AIF1L; NbExp=3; IntAct=EBI-12039345, EBI-12351549;
CC Q9UBR4-2; Q5TZF3-1: ANKRD45; NbExp=3; IntAct=EBI-12039345, EBI-22011535;
CC Q9UBR4-2; O75348: ATP6V1G1; NbExp=3; IntAct=EBI-12039345, EBI-711802;
CC Q9UBR4-2; Q13895: BYSL; NbExp=3; IntAct=EBI-12039345, EBI-358049;
CC Q9UBR4-2; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-12039345, EBI-739879;
CC Q9UBR4-2; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-12039345, EBI-10749669;
CC Q9UBR4-2; Q16204: CCDC6; NbExp=3; IntAct=EBI-12039345, EBI-1045350;
CC Q9UBR4-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-12039345, EBI-396137;
CC Q9UBR4-2; Q00526: CDK3; NbExp=3; IntAct=EBI-12039345, EBI-1245761;
CC Q9UBR4-2; P61024: CKS1B; NbExp=3; IntAct=EBI-12039345, EBI-456371;
CC Q9UBR4-2; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-12039345, EBI-11980535;
CC Q9UBR4-2; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-12039345, EBI-12012272;
CC Q9UBR4-2; P68400: CSNK2A1; NbExp=3; IntAct=EBI-12039345, EBI-347804;
CC Q9UBR4-2; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-12039345, EBI-5453285;
CC Q9UBR4-2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12039345, EBI-744099;
CC Q9UBR4-2; Q9NVQ4-2: FAIM; NbExp=3; IntAct=EBI-12039345, EBI-12039347;
CC Q9UBR4-2; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-12039345, EBI-11986315;
CC Q9UBR4-2; A4D161: FAM221A; NbExp=3; IntAct=EBI-12039345, EBI-11960181;
CC Q9UBR4-2; Q6QHK4: FIGLA; NbExp=5; IntAct=EBI-12039345, EBI-11976617;
CC Q9UBR4-2; Q8NHY3: GAS2L2; NbExp=5; IntAct=EBI-12039345, EBI-7960826;
CC Q9UBR4-2; O95995: GAS8; NbExp=3; IntAct=EBI-12039345, EBI-1052570;
CC Q9UBR4-2; O75603: GCM2; NbExp=3; IntAct=EBI-12039345, EBI-10188645;
CC Q9UBR4-2; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-12039345, EBI-11978177;
CC Q9UBR4-2; Q00444: HOXC5; NbExp=3; IntAct=EBI-12039345, EBI-11955357;
CC Q9UBR4-2; P31273: HOXC8; NbExp=3; IntAct=EBI-12039345, EBI-1752118;
CC Q9UBR4-2; Q0VD86: INCA1; NbExp=5; IntAct=EBI-12039345, EBI-6509505;
CC Q9UBR4-2; Q1MX18: INSC; NbExp=3; IntAct=EBI-12039345, EBI-12081118;
CC Q9UBR4-2; Q96HW7-3: INTS4; NbExp=3; IntAct=EBI-12039345, EBI-12240836;
CC Q9UBR4-2; Q8NA54: IQUB; NbExp=3; IntAct=EBI-12039345, EBI-10220600;
CC Q9UBR4-2; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-12039345, EBI-2556193;
CC Q9UBR4-2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-12039345, EBI-6426443;
CC Q9UBR4-2; P12035: KRT3; NbExp=3; IntAct=EBI-12039345, EBI-2430095;
CC Q9UBR4-2; Q86U70-2: LDB1; NbExp=5; IntAct=EBI-12039345, EBI-11979761;
CC Q9UBR4-2; P45984: MAPK9; NbExp=3; IntAct=EBI-12039345, EBI-713568;
CC Q9UBR4-2; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12039345, EBI-10271199;
CC Q9UBR4-2; Q9H7Z3: NRDE2; NbExp=3; IntAct=EBI-12039345, EBI-1042642;
CC Q9UBR4-2; Q16656-4: NRF1; NbExp=3; IntAct=EBI-12039345, EBI-11742836;
CC Q9UBR4-2; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-12039345, EBI-10297093;
CC Q9UBR4-2; Q01968-2: OCRL; NbExp=3; IntAct=EBI-12039345, EBI-11749425;
CC Q9UBR4-2; Q9NR21-1: PARP11; NbExp=3; IntAct=EBI-12039345, EBI-17644640;
CC Q9UBR4-2; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-12039345, EBI-3921217;
CC Q9UBR4-2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-12039345, EBI-10171633;
CC Q9UBR4-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-12039345, EBI-1053424;
CC Q9UBR4-2; P20618: PSMB1; NbExp=3; IntAct=EBI-12039345, EBI-372273;
CC Q9UBR4-2; Q9UIG4: PSORS1C2; NbExp=7; IntAct=EBI-12039345, EBI-11974061;
CC Q9UBR4-2; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-12039345, EBI-2798044;
CC Q9UBR4-2; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-12039345, EBI-1504830;
CC Q9UBR4-2; Q96CC6: RHBDF1; NbExp=3; IntAct=EBI-12039345, EBI-3865223;
CC Q9UBR4-2; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-12039345, EBI-11984663;
CC Q9UBR4-2; P21673: SAT1; NbExp=5; IntAct=EBI-12039345, EBI-711613;
CC Q9UBR4-2; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-12039345, EBI-748391;
CC Q9UBR4-2; O60880: SH2D1A; NbExp=3; IntAct=EBI-12039345, EBI-6983382;
CC Q9UBR4-2; Q9BV90: SNRNP25; NbExp=7; IntAct=EBI-12039345, EBI-9675976;
CC Q9UBR4-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-12039345, EBI-11955057;
CC Q9UBR4-2; Q8IWB6: TEX14; NbExp=5; IntAct=EBI-12039345, EBI-6674697;
CC Q9UBR4-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12039345, EBI-11741437;
CC Q9UBR4-2; Q7Z6J9: TSEN54; NbExp=5; IntAct=EBI-12039345, EBI-2559824;
CC Q9UBR4-2; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-12039345, EBI-3918381;
CC Q9UBR4-2; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-12039345, EBI-17208936;
CC Q9UBR4-2; O75604: USP2; NbExp=3; IntAct=EBI-12039345, EBI-743272;
CC Q9UBR4-2; Q14119: VEZF1; NbExp=5; IntAct=EBI-12039345, EBI-11980193;
CC Q9UBR4-2; P25490: YY1; NbExp=3; IntAct=EBI-12039345, EBI-765538;
CC Q9UBR4-2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-12039345, EBI-740727;
CC Q9UBR4-2; Q6ZN55-2: ZNF574; NbExp=3; IntAct=EBI-12039345, EBI-17189720;
CC Q9UBR4-2; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-12039345, EBI-6427977;
CC Q9UBR4-2; P36508: ZNF76; NbExp=5; IntAct=EBI-12039345, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=Q9UBR4-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9UBR4-2; Sequence=VSP_003107;
CC -!- DOMAIN: The LIM domain specifically interacts with the Pit-1 POU domain
CC and is required for synergistic interactions with Pit-1, but not for
CC basal transcriptional activation events. {ECO:0000250}.
CC -!- DISEASE: Pituitary hormone deficiency, combined, 3 (CPHD3)
CC [MIM:221750]: Combined pituitary hormone deficiency is defined as the
CC impaired production of growth hormone and one or more of the other five
CC anterior pituitary hormones. CPHD3 is characterized by a complete
CC deficit in all but one (adrenocorticotropin) anterior pituitary hormone
CC and a rigid cervical spine leading to limited head rotation.
CC {ECO:0000269|PubMed:10835633, ECO:0000269|PubMed:17327381,
CC ECO:0000269|PubMed:28302169}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF156888; AAF36808.1; -; mRNA.
DR EMBL; AF156889; AAF36809.1; -; mRNA.
DR EMBL; AH008761; AAF17291.1; -; Genomic_DNA.
DR EMBL; AF096169; AAF17292.1; -; mRNA.
DR EMBL; AF214637; AAF26412.1; -; Genomic_DNA.
DR EMBL; AF367089; AAL26314.1; -; Genomic_DNA.
DR EMBL; AF367085; AAL26314.1; JOINED; Genomic_DNA.
DR EMBL; AF367086; AAL26314.1; JOINED; Genomic_DNA.
DR EMBL; AF367087; AAL26314.1; JOINED; Genomic_DNA.
DR EMBL; AF367088; AAL26314.1; JOINED; Genomic_DNA.
DR EMBL; AL138781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88205.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88206.1; -; Genomic_DNA.
DR CCDS; CCDS6994.1; -. [Q9UBR4-1]
DR CCDS; CCDS6995.1; -. [Q9UBR4-2]
DR RefSeq; NP_055379.1; NM_014564.4. [Q9UBR4-2]
DR RefSeq; NP_835258.1; NM_178138.5. [Q9UBR4-1]
DR AlphaFoldDB; Q9UBR4; -.
DR SMR; Q9UBR4; -.
DR BioGRID; 113718; 175.
DR IntAct; Q9UBR4; 158.
DR STRING; 9606.ENSP00000360811; -.
DR iPTMnet; Q9UBR4; -.
DR PhosphoSitePlus; Q9UBR4; -.
DR BioMuta; LHX3; -.
DR DMDM; 12643415; -.
DR MassIVE; Q9UBR4; -.
DR PaxDb; Q9UBR4; -.
DR PeptideAtlas; Q9UBR4; -.
DR PRIDE; Q9UBR4; -.
DR Antibodypedia; 18678; 152 antibodies from 26 providers.
DR DNASU; 8022; -.
DR Ensembl; ENST00000371746.9; ENSP00000360811.3; ENSG00000107187.17. [Q9UBR4-2]
DR Ensembl; ENST00000371748.10; ENSP00000360813.4; ENSG00000107187.17. [Q9UBR4-1]
DR GeneID; 8022; -.
DR KEGG; hsa:8022; -.
DR MANE-Select; ENST00000371748.10; ENSP00000360813.4; NM_178138.6; NP_835258.1.
DR UCSC; uc004cgz.3; human. [Q9UBR4-1]
DR CTD; 8022; -.
DR DisGeNET; 8022; -.
DR GeneCards; LHX3; -.
DR HGNC; HGNC:6595; LHX3.
DR HPA; ENSG00000107187; Tissue enriched (pituitary).
DR MalaCards; LHX3; -.
DR MIM; 221750; phenotype.
DR MIM; 600577; gene.
DR neXtProt; NX_Q9UBR4; -.
DR OpenTargets; ENSG00000107187; -.
DR Orphanet; 226307; Hypothyroidism due to deficient transcription factors involved in pituitary development or function.
DR Orphanet; 231720; Non-acquired combined pituitary hormone deficiency-sensorineural hearing loss-spine abnormalities syndrome.
DR PharmGKB; PA30366; -.
DR VEuPathDB; HostDB:ENSG00000107187; -.
DR eggNOG; KOG4577; Eukaryota.
DR GeneTree; ENSGT00940000160316; -.
DR InParanoid; Q9UBR4; -.
DR OMA; CTFRGTR; -.
DR PhylomeDB; Q9UBR4; -.
DR TreeFam; TF315442; -.
DR PathwayCommons; Q9UBR4; -.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR SignaLink; Q9UBR4; -.
DR SIGNOR; Q9UBR4; -.
DR BioGRID-ORCS; 8022; 15 hits in 1090 CRISPR screens.
DR ChiTaRS; LHX3; human.
DR GeneWiki; LHX3; -.
DR GenomeRNAi; 8022; -.
DR Pharos; Q9UBR4; Tbio.
DR PRO; PR:Q9UBR4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UBR4; protein.
DR Bgee; ENSG00000107187; Expressed in pituitary gland and 21 other tissues.
DR ExpressionAtlas; Q9UBR4; baseline and differential.
DR Genevisible; Q9UBR4; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
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; ISA:NTNU_SB.
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; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEP:UniProtKB.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0021526; P:medial motor column neuron differentiation; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001890; P:placenta development; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0060127; P:prolactin secreting cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060126; P:somatotropin secreting cell differentiation; IEA:Ensembl.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IEA:Ensembl.
DR GO; GO:0021520; P:spinal cord motor neuron cell fate specification; IEA:Ensembl.
DR GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IEA:Ensembl.
DR GO; GO:0021521; P:ventral spinal cord interneuron specification; IEA:Ensembl.
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; Alternative splicing; Disease variant; DNA-binding; Dwarfism;
KW Homeobox; LIM domain; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..397
FT /note="LIM/homeobox protein Lhx3"
FT /id="PRO_0000075781"
FT DOMAIN 31..81
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 90..144
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 157..216
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 212..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15517599"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15517599"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:15517599"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15517599"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15517599"
FT VAR_SEQ 1..25
FT /note="MLLETGLERDRARPGAAAVCTLGGT -> MEARGELGPARESAGGDLLLALL
FT ARRADLR (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_003107"
FT VARIANT 111
FT /note="Y -> C (in CPHD3; dbSNP:rs104894117)"
FT /evidence="ECO:0000269|PubMed:10835633"
FT /id="VAR_010713"
FT VARIANT 141
FT /note="C -> F (in CPHD3; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28302169"
FT /id="VAR_079378"
FT VARIANT 151..397
FT /note="Missing (in CPHD3)"
FT /evidence="ECO:0000269|PubMed:28302169"
FT /id="VAR_079379"
FT VARIANT 210
FT /note="A -> V (in CPHD3; associated with diminished DNA
FT binding and pituitary gene activation; dbSNP:rs137854503)"
FT /evidence="ECO:0000269|PubMed:17327381"
FT /id="VAR_063240"
FT CONFLICT 34
FT /note="C -> R (in Ref. 2; AAF17291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 43358 MW; FB4A2E48C015C249 CRC64;
MLLETGLERD RARPGAAAVC TLGGTREIPL CAGCDQHILD RFILKALDRH WHSKCLKCSD
CHTPLAERCF SRGESVYCKD DFFKRFGTKC AACQLGIPPT QVVRRAQDFV YHLHCFACVV
CKRQLATGDE FYLMEDSRLV CKADYETAKQ REAEATAKRP RTTITAKQLE TLKSAYNTSP
KPARHVREQL SSETGLDMRV VQVWFQNRRA KEKRLKKDAG RQRWGQYFRN MKRSRGGSKS
DKDSVQEGQD SDAEVSFPDE PSLAEMGPAN GLYGSLGEPT QALGRPSGAL GNFSLEHGGL
AGPEQYRELR PGSPYGVPPS PAAPQSLPGP QPLLSSLVYP DTSLGLVPSG APGGPPPMRV
LAGNGPSSDL STGSSGGYPD FPASPASWLD EVDHAQF
