GLI2_CHICK
ID GLI2_CHICK Reviewed; 663 AA.
AC P55879;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Zinc finger protein GLI2 {ECO:0000305};
DE Flags: Fragment;
GN Name=GLI2 {ECO:0000250|UniProtKB:P10070};
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].
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: Functions as transcription regulator in the hedgehog (Hh)
CC pathway. Functions as transcriptional activator. May also function as
CC transcriptional repressor. Binds to the DNA sequence 5'-GAACCACCCA-3'
CC (By similarity). Is involved in the smoothened (SHH) signaling pathway.
CC Required for normal skeleton development (By similarity).
CC {ECO:0000250|UniProtKB:P10070, ECO:0000250|UniProtKB:Q0VGT2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q0VGT2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q0VGT2}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q0VGT2}.
CC -!- DOMAIN: The N-terminal domain confers transcriptional repressor
CC activity, while the C-terminal domain mediates transcriptional
CC activation. {ECO:0000250|UniProtKB:Q0VGT2}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U60763; AAB51660.1; -; mRNA.
DR AlphaFoldDB; P55879; -.
DR SMR; P55879; -.
DR STRING; 9031.ENSGALP00000018975; -.
DR PaxDb; P55879; -.
DR PRIDE; P55879; -.
DR VEuPathDB; HostDB:geneid_395956; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P55879; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
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 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; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 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; 4.
PE 2: Evidence at transcript level;
KW Activator; Cell projection; Cilium; Cytoplasm; Developmental protein;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..>663
FT /note="Zinc finger protein GLI2"
FT /id="PRO_0000047205"
FT ZN_FING 234..259
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..294
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..324
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 330..355
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..386
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 159..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 663
SQ SEQUENCE 663 AA; 73107 MW; 46E32C33FF6BD4FF CRC64;
LMAGHPNYGD ILMQSGGAAG TAHLHEYLSP VDVSRFSSPR VTPRLSRKRA LSISPLSDAS
IDLQTMIRTS PNSLVAYINN SRSSSAASGS YGHLSAGTIS PAFSFPHPIN PVTYQQILTQ
QRGLSSAFGH TPPLIQPSPT FPPRQHMAVI SVNPPPAQIS SNSNCISDSS QSKQSSESAV
SSTVNPVINK RTKVKTEVEG LPQYPQPRQE HLTDLKEDLD KDECKQEPEV IYETNCHWEG
CTKEYDTQEQ LVHHINNDHI HGEKKEFVCR WQDCTREQKP FKAQYMLVVH MRRHTGEKPH
KCTFEGCSKA YSRLENLKTH LRSHTGEKPY VCEHEGCNKA FSNASDRAKH QNRTHSNEKP
YVCKIPGCTK RYTDPSSLRK HVKTVHGPDA HVTKKQRNDV HPRPPPLKEN GDNEASAKQS
SKVSEESPEA NSTTRSMEDC LQVKTIKTEN SVMCQSSPGG QSSCSSEPSP LGSTNNNDSG
VEMNMHGGGS LGDLTGWMTR LPVVDSTVSS GNLTVSLQLR KHMTTMQRLE QLKKEKLKTV
KDSCSWVNPA PQGRNTKLPP ISGNGSILEN SGGSSRTLPN PRIMELSVNE VTMLNQINER
RDSTTSTISS AYTVSRRSSG ISPYFSSRRS SEASQLGHRP NNTSSADSYD PISTGGREFD
IKL
