GLI3_XENLA
ID GLI3_XENLA Reviewed; 1569 AA.
AC Q91660;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Zinc finger protein GLI3;
DE AltName: Full=Neural-specific DNA-binding protein xGLI3;
DE Short=xGLI-3;
GN Name=gli3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9203143; DOI=10.1016/s0925-4773(97)00050-6;
RA Marine J.C., Bellefroid E.J., Pendeville H., Martial J.A., Pieler T.;
RT "A role for Xenopus Gli-type zinc finger proteins in the early embryonic
RT patterning of mesoderm and neuroectoderm.";
RL Mech. Dev. 63:211-225(1997).
CC -!- FUNCTION: Has a dual function as a transcriptional activator and a
CC repressor of the sonic hedgehog (Shh) pathway, and may play a role in
CC limb development. May bind to the minimal GLI-consensus sequence 5'-
CC GGGTGGTC-3' (By similarity). Has an essential role in the early
CC embryonic patterning of mesoderm and neuroectoderm. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylation is essential for its proteolytic processing.
CC {ECO:0000250}.
CC -!- PTM: The repressor form (GLI3R), a C-terminally truncated form is
CC generated from the full-length GLI3 protein (GLI3FL) through
CC proteolytic processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; U42461; AAA98466.1; -; mRNA.
DR RefSeq; NP_001081440.1; NM_001087971.1.
DR AlphaFoldDB; Q91660; -.
DR SMR; Q91660; -.
DR PRIDE; Q91660; -.
DR GeneID; 397837; -.
DR KEGG; xla:397837; -.
DR CTD; 397837; -.
DR Xenbase; XB-GENE-865509; gli3.L.
DR OrthoDB; 56870at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397837; Expressed in neurula embryo and 14 other tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:InterPro.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:InterPro.
DR GO; GO:0048568; P:embryonic organ development; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:InterPro.
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 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1569
FT /note="Zinc finger protein GLI3"
FT /id="PRO_0000047206"
FT ZN_FING 485..510
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..545
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..575
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..606
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 612..637
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..29
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 414..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1569 AA; 172594 MW; 71F5DC117A930B82 CRC64;
MEAQSRSTTA SEKKKVENSI VKGHSRTEVS EKAVASSTTS NEDESPGQTY HRERRNAIAM
QPQGGQGLGK ISEEPSTSSE ERASLIKKEL HGSITHLPEP SVPYRGTVFA MDPRNGYIDP
HYRSDLDLFP AFHPPVPIDA RHHEGRYHYE PTPIPPLHVP TALASSPTYP DLPFFRISPH
RNPASASDSP FSPPHPYISP YMDYIRSLHS SPSLSMISAA RGLSPTDVPH AGISPAEYYH
QMALLAGQRS PYADIFPSPA TAGAGANALH MEYLHAMESS RFSSPRLSAR PSRKRTLSIS
PLSDHSFDLQ TMIRNSPNSL VTILNNSRSS SSASGSYGHL AASAISPALN FAYQPTPVSL
QQMHQQIMSR QHSIGSAFGH SPPLLHPAPT FPSQRTIPGI PSVLNPVQVS IGPSEAAQQN
KPTSESAVSS TGDLLHNKRS KVKPEEDHPS PGAVCIQDQP DGMTLVKEEG VKDESKQEAE
VVYETNCHWE GCSREFDTQE QLVHHINNDH IHGEKKEFVC RWLDCSREQK PFKAQYMLVV
HMRRHTGEKP HKCTFEGCSK AYSRLENLKT HLRSHTGEKP YVCEHEGCNK AFSNASDRAK
HQNRTHSNEK PYVCKIPGCT KRYTDPSSLR KHVKTVHGPE AHVTKKQRGD IHPRPPPPRE
PGSHSQSRSP GQQTQGIHGE HKDLSNTTSK HEECLQVRSV KTEKPMSSQP SPGGKSSCSR
QQSPISNYTN SGIELNLNSG GSIGDFSALD ETPIMDSTIS TATTGLGLHG RRVMTGTKWM
EQIKVEKMKQ VNGMLPRLNP VPPHRAPTLP PITGNGVQLN SNISLGGLAP VLPNRNDLSS
MDITVLNMLN RRDSNTSTIS SAYMSSRRSS GISPCFSSRR SSEASQFEGR VQNLSVAGSY
DPISTDASRR SSETSQCDGL PTLLSLTPAQ QYRLKAKYAA ATGGPPPTPL PNMERMSLKT
RMALLGDSRD CRLSPLPSVN VPRRCSDGGV GSYGRRHLLP NELQVNGMRR ASDPVKMVSD
NVSNTRVVRF NSLNNVIPPD VPPPMERRNL SLQNYTRNVY SPCPPSISEN VALEAMIMEA
EGNFDDEDLL PDDMVQYLNS RNQRLYETIE TDALQNNAGE RNGNNFEQSH VTSNVINEQF
HSSEQTDLIE NKNDLPIQWN EVSSGSAEYS PSRLKYGQRF PTQQNQPFGL YNNMMVQQQN
VPKSGLSQQR GYQHHTQNNP QAPQQNLDLY NNSNVWSGQL GRGNQYIDDI ERSSLGHSAT
GSLCNSAARG QKLTTNGLPM NTGQQNFGPS THYSVQSANR AEVVQNENII NQEFMQQMTA
EHLIYGMHLL GVTRSNQTTS GQNGNTTDGT RSFLSTTQNG GEQQPTLAKN FQSFVNSSGN
SRQNLHRNNL PYLQEQIYDT NQHIFKVNSI KMEMQSHPQQ HCANAQNFSG QLYDQTATYP
QQIMKSGSEP GMEANCLLQE SNNTNSSKLL SPGANHVTST VDNIDNSLAG VQIAFAAIID
DGDHASLISG VLSPSIIQNL SRNSSRLTTP RASLTFPAIP VSTSNMAIGD MSSLLTSLAE
ESKFLAIMQ
