GLI3_MOUSE
ID GLI3_MOUSE Reviewed; 1583 AA.
AC Q61602;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Transcriptional activator GLI3;
DE AltName: Full=GLI3 form of 190 kDa;
DE Short=GLI3-190;
DE AltName: Full=GLI3 full-length protein;
DE Short=GLI3FL;
DE Contains:
DE RecName: Full=Transcriptional repressor GLI3R;
DE AltName: Full=GLI3 C-terminally truncated form;
DE AltName: Full=GLI3 form of 83 kDa;
DE Short=GLI3-83;
GN Name=Gli3;
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 STRAIN=NIH Swiss;
RX PubMed=8688459; DOI=10.1016/0167-4781(96)00079-6;
RA Thien H., Buescher D., Ruether U.;
RT "Cloning and sequence analysis of the murine Gli3 cDNA.";
RL Biochim. Biophys. Acta 1307:267-269(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP DISEASE.
RX PubMed=1983115; DOI=10.1242/dev.110.4.1153;
RA Pohl T.M., Mattei M.G., Ruether U.;
RT "Evidence for allelism of the recessive insertional mutation add and the
RT dominant mouse mutation extra-toes (Xt).";
RL Development 110:1153-1157(1990).
RN [4]
RP DISEASE.
RX PubMed=10051311; DOI=10.1007/s003359900973;
RA Thien H., Ruether U.;
RT "The mouse mutation Pdn (Polydactyly Nagoya) is caused by the integration
RT of a retrotransposon into the Gli3 gene.";
RL Mamm. Genome 10:205-209(1999).
RN [5]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=10693759; DOI=10.1016/s0092-8674(00)80678-9;
RA Wang B., Fallon J.F., Beachy P.A.;
RT "Hedgehog-regulated processing of Gli3 produces an anterior/posterior
RT repressor gradient in the developing vertebrate limb.";
RL Cell 100:423-434(2000).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=11053430; DOI=10.1074/jbc.m004430200;
RA Mizugishi K., Aruga J., Nakata K., Mikoshiba K.;
RT "Molecular properties of Zic proteins as transcriptional regulators and
RT their relationship to GLI proteins.";
RL J. Biol. Chem. 276:2180-2188(2001).
RN [7]
RP FUNCTION.
RX PubMed=17400206; DOI=10.1016/j.ydbio.2007.02.029;
RA Wang C., Ruther U., Wang B.;
RT "The Shh-independent activator function of the full-length Gli3 protein and
RT its role in vertebrate limb digit patterning.";
RL Dev. Biol. 305:460-469(2007).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
RA Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
RA Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
RA Peterson A.S.;
RT "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh
RT signal transduction during development.";
RL Curr. Biol. 19:1320-1326(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH TRPS1.
RX PubMed=19389374; DOI=10.1016/j.ydbio.2009.01.012;
RA Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A.,
RA Depping R., Vortkamp A.;
RT "Trps1, a regulator of chondrocyte proliferation and differentiation,
RT interacts with the activator form of Gli3.";
RL Dev. Biol. 328:40-53(2009).
RN [10]
RP INTERACTION WITH KIF7.
RX PubMed=19549984; DOI=10.1126/scisignal.2000405;
RA Cheung H.O., Zhang X., Ribeiro A., Mo R., Makino S., Puviindran V.,
RA Law K.K., Briscoe J., Hui C.C.;
RT "The kinesin protein Kif7 is a critical regulator of Gli transcription
RT factors in mammalian hedgehog signaling.";
RL Sci. Signal. 2:RA29-RA29(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH SUFU.
RX PubMed=20360384; DOI=10.1101/gad.1902910;
RA Humke E.W., Dorn K.V., Milenkovic L., Scott M.P., Rohatgi R.;
RT "The output of Hedgehog signaling is controlled by the dynamic association
RT between Suppressor of Fused and the Gli proteins.";
RL Genes Dev. 24:670-682(2010).
RN [12]
RP INTERACTION WITH DZIP1, AND REGION.
RX PubMed=23955340; DOI=10.1074/jbc.m113.492066;
RA Wang C., Low W.C., Liu A., Wang B.;
RT "Centrosomal protein DZIP1 regulates Hedgehog signaling by promoting
RT cytoplasmic retention of transcription factor GLI3 and affecting
RT ciliogenesis.";
RL J. Biol. Chem. 288:29518-29529(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-175, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [14]
RP INTERACTION WITH WDR11.
RX PubMed=29263200; DOI=10.15252/embr.201744632;
RA Kim Y.J., Osborn D.P., Lee J.Y., Araki M., Araki K., Mohun T.,
RA Kaensaekoski J., Brandstack N., Kim H.T., Miralles F., Kim C.H.,
RA Brown N.A., Kim H.G., Martinez-Barbera J.P., Ataliotis P., Raivio T.,
RA Layman L.C., Kim S.H.;
RT "WDR11-mediated Hedgehog signalling defects underlie a new ciliopathy
RT related to Kallmann syndrome.";
RL EMBO Rep. 19:269-289(2018).
CC -!- FUNCTION: Has a dual function as a transcriptional activator and a
CC repressor of the sonic hedgehog (Shh) pathway, and plays a role in limb
CC development. The full-length GLI3 form (GLI3FL) after phosphorylation
CC and nuclear translocation, acts as an activator (GLI3A) while GLI3R,
CC its C-terminally truncated form, acts as a repressor. A proper balance
CC between the GLI3 activator and the repressor GLI3R, rather than the
CC repressor gradient itself or the activator/repressor ratio gradient,
CC specifies limb digit number and identity. In concert with TRPS1, plays
CC a role in regulating the size of the zone of distal chondrocytes, in
CC restricting the zone of PTHLH expression in distal cells and in
CC activating chondrocyte proliferation. Binds to the minimal GLI-
CC consensus sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:10693759,
CC ECO:0000269|PubMed:11053430, ECO:0000269|PubMed:17400206,
CC ECO:0000269|PubMed:19389374, ECO:0000269|PubMed:20360384}.
CC -!- SUBUNIT: The phosphorylated form interacts with BTRC (By similarity).
CC The full-length GLI3 form (GLI3FL) interacts with SUFU and this
CC interaction regulates the formation of either repressor or activator
CC forms of GLI3. Its association with SUFU is regulated by Hh signaling
CC and dissociation of the SUFU-GLI3 interaction requires the presence of
CC the ciliary motor KIF3A. Interacts with KIF7. The activator form of
CC GLI3 (GLI3A) but not the repressor form (GLI3R) can interact with
CC TRPS1. Interacts with ZIC1. Interacts with ZIC3 (via C2H2-type domains
CC 3, 4 and 5); the interaction enhances its transcriptional activity (By
CC similarity). Interacts with WRD11; the interaction associates EMX1 with
CC GLI3 (PubMed:29263200). Interacts with DZIP1; retains GLI3 within the
CC cytoplasm (PubMed:23955340). {ECO:0000250|UniProtKB:P10071,
CC ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:29263200}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20360384}. Cytoplasm
CC {ECO:0000269|PubMed:20360384}. Cell projection, cilium
CC {ECO:0000269|PubMed:20360384}. Note=Translocation to the nucleus is
CC promoted by interaction with ZIC1 (By similarity). GLI3FL is localized
CC predominantly in the cytoplasm while GLI3R resides mainly in the
CC nucleus. Ciliary accumulation requires the presence of KIF7 and SMO.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by DYRK2 (in vitro) (By similarity). Phosphorylated
CC on multiple sites by protein kinase A (PKA) and phosphorylation by PKA
CC primes further phosphorylation by CK1 and GSK3. Phosphorylation is
CC essential for its proteolytic processing. {ECO:0000250,
CC ECO:0000269|PubMed:20360384}.
CC -!- PTM: Transcriptional repressor GLI3R, a C-terminally truncated form, is
CC generated from the full-length GLI3 protein (GLI3FL/GLI3-190) through
CC proteolytic processing. This process requires PKA-primed
CC phosphorylation of GLI3, ubiquitination of GLI3 and the presence of
CC BTRC. GLI3FL is complexed with SUFU in the cytoplasm and is maintained
CC in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is
CC recruited to cilia, leading to the efficient processing of GLI3FL into
CC GLI3R. GLI3R formation leads to its dissociation from SUFU, allowing it
CC to translocate into the nucleus, and repress Hh target genes. When Hh
CC signaling is initiated, SUFU dissociates from GLI3FL and this has two
CC consequences. First, GLI3R production is halted. Second, free GLI3FL
CC translocates to the nucleus, where it is phosphorylated, destabilized,
CC and converted to a transcriptional activator (GLI3A). Phosphorylated in
CC vitro by ULK3. {ECO:0000269|PubMed:20360384}.
CC -!- DISEASE: Note=Several mutations result in developmental defects of
CC cranofacial and limb structures. In particular the add (anterior digit-
CC pattern deformity) and pdn (polydactyly Nagoya) alleles.
CC {ECO:0000269|PubMed:10051311, ECO:0000269|PubMed:1983115}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64543.1; Type=Frameshift; Evidence={ECO:0000305};
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; X95255; CAA64543.1; ALT_FRAME; mRNA.
DR EMBL; AC163610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC173115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC173210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36603.1; -.
DR RefSeq; NP_032156.2; NM_008130.2.
DR AlphaFoldDB; Q61602; -.
DR SMR; Q61602; -.
DR BioGRID; 199944; 30.
DR ComplexPortal; CPX-151; GLI3-SUFU complex.
DR CORUM; Q61602; -.
DR IntAct; Q61602; 2.
DR MINT; Q61602; -.
DR STRING; 10090.ENSMUSP00000106137; -.
DR iPTMnet; Q61602; -.
DR PhosphoSitePlus; Q61602; -.
DR jPOST; Q61602; -.
DR MaxQB; Q61602; -.
DR PaxDb; Q61602; -.
DR PRIDE; Q61602; -.
DR ProteomicsDB; 263366; -.
DR Antibodypedia; 647; 282 antibodies from 38 providers.
DR DNASU; 14634; -.
DR Ensembl; ENSMUST00000110510; ENSMUSP00000106137; ENSMUSG00000021318.
DR GeneID; 14634; -.
DR KEGG; mmu:14634; -.
DR UCSC; uc007pns.1; mouse.
DR CTD; 2737; -.
DR MGI; MGI:95729; Gli3.
DR VEuPathDB; HostDB:ENSMUSG00000021318; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155925; -.
DR HOGENOM; CLU_003666_3_0_1; -.
DR InParanoid; Q61602; -.
DR OMA; CGQRSAV; -.
DR OrthoDB; 56870at2759; -.
DR PhylomeDB; Q61602; -.
DR TreeFam; TF350216; -.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 14634; 7 hits in 60 CRISPR screens.
DR ChiTaRS; Gli3; mouse.
DR PRO; PR:Q61602; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61602; protein.
DR Bgee; ENSMUSG00000021318; Expressed in maxillary prominence and 288 other tissues.
DR ExpressionAtlas; Q61602; baseline and differential.
DR Genevisible; Q61602; MM.
DR GO; GO:0005930; C:axoneme; IDA:CACAO.
DR GO; GO:0005929; C:cilium; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990788; C:GLI-SUFU complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0036033; F:mediator complex binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0048856; P:anatomical structure development; IGI:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
DR GO; GO:0060873; P:anterior semicircular canal development; IMP:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0060840; P:artery development; IGI:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0061005; P:cell differentiation involved in kidney development; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0021801; P:cerebral cortex radial glia-guided migration; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; IMP:MGI.
DR GO; GO:0060364; P:frontal suture morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0007442; P:hindgut morphogenesis; IGI:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IGI:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0060366; P:lambdoid suture morphogenesis; IMP:MGI.
DR GO; GO:0120223; P:larynx morphogenesis; IMP:MGI.
DR GO; GO:0022018; P:lateral ganglionic eminence cell proliferation; IMP:MGI.
DR GO; GO:0060875; P:lateral semicircular canal development; IMP:MGI.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0060594; P:mammary gland specification; IGI:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; IGI:MGI.
DR GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IGI:MGI.
DR GO; GO:1990787; P:negative regulation of hh target transcription factor activity; ISO:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:BHF-UCL.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:BHF-UCL.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IGI:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IGI:MGI.
DR GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0021543; P:pallium development; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IGI:MGI.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IGI:MGI.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:1903010; P:regulation of bone development; IMP:MGI.
DR GO; GO:0045595; P:regulation of cell differentiation; IGI:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:1901620; P:regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0060367; P:sagittal suture morphogenesis; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IGI:MGI.
DR GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IGI:MGI.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IGI:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0021544; P:subpallium development; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:BHF-UCL.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR GO; GO:0070242; P:thymocyte apoptotic process; IMP:BHF-UCL.
DR GO; GO:0043586; P:tongue development; IMP:MGI.
DR GO; GO:0035295; P:tube development; IGI:MGI.
DR GO; GO:0071625; P:vocalization behavior; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR032851; GLI3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR PANTHER; PTHR45718:SF5; PTHR45718:SF5; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell projection; Cilium; Cytoplasm; DNA-binding;
KW Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1583
FT /note="Transcriptional activator GLI3"
FT /id="PRO_0000047203"
FT CHAIN 1..?
FT /note="Transcriptional repressor GLI3R"
FT /id="PRO_0000406138"
FT ZN_FING 480..505
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..540
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 546..570
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 576..601
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..632
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..845
FT /note="Mediates interaction with DZIP1"
FT /evidence="ECO:0000269|PubMed:23955340"
FT REGION 809..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 849
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 865
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 877
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 907
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 980
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT MOD_RES 1006
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 462
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 773
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 784
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CROSSLNK 800
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P10071"
FT CONFLICT 209
FT /note="S -> C (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="D -> G (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="R -> A (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="A -> P (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="A -> D (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185..1186
FT /note="SA -> R (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
FT CONFLICT 1475..1476
FT /note="NG -> TC (in Ref. 1; CAA64543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1583 AA; 171655 MW; 37ECC0C3ACF26C24 CRC64;
MEAQAHSSTA TERKKAENSI GKCPTRTDVS EKAVASSTTS NEDESPGQIY HRERRNAITM
QPQSVQGLNK ISEEPSTSSD ERASLIKKEI HGSLPHLAEP SLPYRGTVFA MDPRNGYMEP
HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP SPIPPLHVPS ALSSSPTYPD LPFIRISPHR
NPTAASESPF SPPHPYINPY MDYIRSLHSS PSLSMISAAR GLSPTDAPHA GVSPAEYYHQ
MALLTGQRSP YADILPSAAT AGAGAIHMEY LHAMDSTRFP SPRLSARPSR KRTLSISPLS
DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY PSAPVSLHMH
QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL NPVQVSSGPS ESSQSKPTSE
SAVSSTGDPM HNKRSKIKPD EDLPSPGSRG QQEQPEGTTL VKEEADKDES KQEPEVIYET
NCHWEGCTRE FDTQDQLVHH INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH
TGEKPHKCTF EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT
HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDMHPRP PPPRDSGSHS
QSRSPGRPTQ GAFGEQKELS NTTSKREECL QVKTVKAEKP MTSQPSPGGQ SSCSSQQSPI
SNYSNSGLEL PLTDGGSVAD LSAIDETPIM DSTISTATTA LALQARRNPA GTKWMEHIKL
ERLKQVNGMF PRLNPILPSK APAVSPLIGN GTQSNNNYSS GGPGTLLPSR SDLSGVDFTV
LNTLNRRDSN TSTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST
DASRRSSEAS QGDGLPSLLS LTPVQQYRLK AKYAAATGGP PPTPLPHMER LSLKTKMALL
GEGRDSGVTL PPVHPPRRCS DGGGHTYRGR HLMPHDALAN SVRRASDPVR TVSENMSLAR
VQRFSSLNSF NPPNLPPSVE KRSLVLQNYT RQESSQPRYF QASPCPPSIT ENVALEALTM
DADANLNDED LLPDDVVQYL NSQNQTGYGQ QLQSGISEDS KVAHEPEDLD LAGLPDSHVG
QEYPALEQPC SEGSKTDLPI QWNEVSSGTS DLSSSKLKCG QQRPSAQQPR GFGLYNNMVV
HPHNLWKVGT GPAGGYQTLG ENSSTYNGPE HFAIHSGDGL GTNGNTFHEQ PFKTQQYGSQ
LNRQPLTSSA LDHACGTGIQ GSKLKGNSLQ ENGGLLDFSL SVAPNELAGN TVNGMQTQDQ
MGQGYIAHQL LSGSMQHQGP SRPGQQVLGQ VGATSHINIY QGTESCLPGT QDNSSQPSSM
AAIRGYQPCA SYGGNRRQAM PRGNLTLQQG QLSDMSQSSR VNSIKMEAQG QSQQLCSTVQ
NYSGQFYDQT MGFSQQDRKA GSFSLSDANC LLQGNGTENS ELLSPGANQV TSTVDSFESH
DLEGVQIDFD AIIDDGDHTS LMSGALSPSI IQNLSHSSSR LTTPRASLPF PSLSMGTTNM
AIGDMSSLLT SLAEESKFLA VMQ
