GLI1_CHICK
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 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc finger protein 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: Acts as a transcriptional activator. Binds to the DNA
CC consensus sequence 5'-GACCACCCA-3' (By similarity). May regulate the
CC transcription of specific genes during normal development
CC (PubMed:8948590). May play a role in craniofacial development and
CC digital development, as well as development of the central nervous
CC system and gastrointestinal tract (PubMed:8948590). Mediates SHH
CC signaling (PubMed:8948590). Plays a role in cell proliferation and
CC differentiation via its role in SHH signaling.
CC {ECO:0000250|UniProtKB:P08151, ECO:0000305|PubMed:8948590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08151}. Nucleus
CC {ECO:0000250|UniProtKB:P08151}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U60762; AAB51659.1; -; mRNA.
DR AlphaFoldDB; P55878; -.
DR SMR; P55878; -.
DR STRING; 9031.ENSGALP00000023546; -.
DR PaxDb; P55878; -.
DR VEuPathDB; HostDB:geneid_396045; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P55878; -.
DR OrthoDB; 135929at2759; -.
DR PhylomeDB; P55878; -.
DR Proteomes; UP000000539; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021983; P:pituitary gland development; IEA:InterPro.
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:0045893; P:positive regulation of transcription, DNA-templated; 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 InterPro; IPR043359; GLI-like.
DR InterPro; IPR032850; GLI1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR PANTHER; PTHR45718:SF2; PTHR45718:SF2; 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 2: Evidence at transcript level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleus; Proto-oncogene; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..>556
FT /note="Zinc finger protein 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 133..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..488
FT /note="Polar residues"
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
