ID GLI1_CHICK Reviewed; 556 AA. AC P55878; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 02-SEP-2026, entry version 132. DE RecName: Full=Transcription activator GLI1; DE Short=GLI; DE Flags: Fragment; GN Name=GLI1; Synonyms=GLI; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=8948590; DOI=10.1006/dbio.1996.0300; RA Marigo V., Johnson R.L., Vortkamp A., Tabin C.J.; RT "Sonic hedgehog differentially regulates expression of GLI and GLI3 during RT limb development."; RL Dev. Biol. 180:273-283(1996). CC -!- FUNCTION: Transcription activator that acts as a key effector of the CC smoothened signaling pathway, and which plays a role in craniofacial CC development and digital development, as well as development of the CC central nervous system and gastrointestinal tract (PubMed:8948590). CC Binds to the DNA consensus sequence 5'-GACCACCCA-3' (By similarity). CC Activated in response to smoothened signaling: in presence of hedgehog CC (DHH, IHH or SHH) and subsequent activation of smoothened, GLI1 CC translocates to the nucleus and promotes expression of target genes (By CC similarity). In contrast to GLI2 and GLI3, does not contain a repressor CC domain and only acts as a transcription activator (By similarity). CC {ECO:0000250|UniProtKB:P08151, ECO:0000269|PubMed:8948590}. CC -!- ACTIVITY REGULATION: Maintained in an inactive state by SUFU, which CC sequesters GLI1 in the cytoplasm. In presence of hedgehog (DHH, IHH or CC SHH), smoothened is activated, leading to dissociation from SUFU and CC translocation to the nucleus. {ECO:0000250|UniProtKB:P08151}. CC -!- SUBUNIT: Interacts with SUFU; sequestering GLI1 in the cytoplasm. CC {ECO:0000250|UniProtKB:P08151}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08151}. Nucleus CC {ECO:0000250|UniProtKB:P08151}. Cell projection, cilium CC {ECO:0000250|UniProtKB:P08151}. Note=Sequestered in the cytoplasm by CC SUFU in absence of smoothened signaling. Accumulates in primary cilia CC following smoothened activation. It then translocates to the nucleus, CC where is activates transcription of target genes. CC {ECO:0000250|UniProtKB:P08151}. CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family. CC {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; U60762; AAB51659.1; -; mRNA. DR AlphaFoldDB; P55878; -. DR SMR; P55878; -. DR FunCoup; P55878; 316. DR STRING; 9031.ENSGALP00000049322; -. DR GlyGen; P55878; 1 site. DR PaxDb; 9031-ENSGALP00000049322; -. DR VEuPathDB; HostDB:geneid_396045; -. DR eggNOG; KOG1721; Eukaryota. DR InParanoid; P55878; -. DR OrthoDB; 3214149at2759; -. DR PhylomeDB; P55878; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central. DR FunFam; 3.30.160.60:FF:000019; GLI family zinc finger 3; 1. DR FunFam; 3.30.160.60:FF:000031; GLI family zinc finger 3; 1. DR FunFam; 3.30.160.60:FF:000036; GLI family zinc finger 3; 1. DR FunFam; 3.30.160.60:FF:000048; GLI family zinc finger 3; 1. DR FunFam; 3.30.160.60:FF:000068; GLI family zinc finger 3; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 5. DR InterPro; IPR043359; GLI-like. DR InterPro; IPR056436; Znf-C2H2_ZIC1-5/GLI1-3-like. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR45718; TRANSCRIPTIONAL ACTIVATOR CUBITUS INTERRUPTUS; 1. DR PANTHER; PTHR45718:SF2; ZINC FINGER PROTEIN GLI1; 1. DR Pfam; PF00096; zf-C2H2; 3. DR Pfam; PF23561; zf-C2H2_15; 1. DR SMART; SM00355; ZnF_C2H2; 5. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. PE 2: Evidence at transcript level; KW Activator; Cell projection; Cytoplasm; Developmental protein; KW Differentiation; DNA-binding; Metal-binding; Nucleus; Proto-oncogene; KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..>556 FT /note="Transcription activator GLI1" FT /id="PRO_0000047199" FT ZN_FING 247..272 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 280..307 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 313..337 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 343..368 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 374..399 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 57..83 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 133..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 295..303 FT /note="Interaction with DNA" FT /evidence="ECO:0000250|UniProtKB:P08151" FT REGION 357..362 FT /note="Interaction with DNA" FT /evidence="ECO:0000250|UniProtKB:P08151" FT REGION 387..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..393 FT /note="Interaction with DNA" FT /evidence="ECO:0000250|UniProtKB:P08151" FT COMPBIAS 135..148 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 454..472 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 556 SQ SEQUENCE 556 AA; 60216 MW; 722D2AA5A1CA4D98 CRC64; MFNPVTPQAR PYAEHCCPRP LHGASAGTPG LQGLDFPVCH QPNLASSHHG YGLVPGTEHP GGAADGSRFS TPRGAGKLGK KRALSISPLS DSSVDLQTVI RTSPNSLVAF INSRCASAGG SYGHLSISTI SPSLGYQNPP GQQKGQGQLF SHTPPLPPCS SHETLSSRPG LLHPTPARGT IKHCQQLKLE RSLSSPLTAK YPEEKSEGDI SSPASTGTQD PLLGMLSVRD DLEKEDGKPE SETIYETNCY WDGCAKEFDT QEQLVHHINN EHIHGEKKEF VCHWAACSRE QRPFKAQYML VVHMRRHTGE KPHKCTFEGC NKAYSRLENL KTHLRSHTGE KPYVCEHEGC NKAFSNASDR AKHQNRTHSN EKPYICKIPG CTKRYTDPSS LRKHVKTVHG PDAHVTKKHR GSVVPGHALP ASAAPQDMKQ EKNTNGPAEI RKDDGKLLVP DLVSKPQPSP GGQSSCSSDR SPLGSTTNND SGVEMTGNTG GSYEDLVHAG GCGARGSHGH LGADGLQKLE NLRIDKLKQM RKPSTKGLNL PAIPEPVCRR CVRVCV //