GLI3_CHICK
ID GLI3_CHICK Reviewed; 1544 AA.
AC Q9IA31;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Transcriptional activator GLI3;
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 Flags: Fragment;
GN Name=GLI3;
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], FUNCTION, PROTEOLYTIC PROCESSING,
RP PHOSPHORYLATION, AND DEVELOPMENTAL STAGE.
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).
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) acts as an activator
CC (GLI3A) while GLI3R, its C-terminally truncated form, acts as a
CC repressor. {ECO:0000269|PubMed:10693759}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Detected in limb buds at embryonic stages 22-23
CC (at protein level). {ECO:0000269|PubMed:10693759}.
CC -!- PTM: Phosphorylation is essential for its proteolytic processing.
CC {ECO:0000269|PubMed:10693759}.
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:0000269|PubMed:10693759}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF222990; AAF37273.1; -; mRNA.
DR RefSeq; NP_001258832.1; NM_001271903.1.
DR AlphaFoldDB; Q9IA31; -.
DR SMR; Q9IA31; -.
DR STRING; 9031.ENSGALP00000036642; -.
DR PaxDb; Q9IA31; -.
DR GeneID; 420769; -.
DR KEGG; gga:420769; -.
DR CTD; 2737; -.
DR VEuPathDB; HostDB:geneid_420769; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9IA31; -.
DR OrthoDB; 56870at2759; -.
DR PhylomeDB; Q9IA31; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0060173; P:limb development; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA: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; 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 Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..>1544
FT /note="Transcriptional activator GLI3"
FT /id="PRO_0000406140"
FT CHAIN 1..?
FT /note="Transcriptional repressor GLI3R"
FT /id="PRO_0000406141"
FT ZN_FING 482..509
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 520..542
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 548..572
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 578..603
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 609..634
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1368
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 22..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1544
SQ SEQUENCE 1544 AA; 167791 MW; 1B1E7285E096EB6C CRC64;
MEAQSHSSTT TEKKKVENSI VKCSNRTDVS EKAVASSTTS NEDESPGQTY HRERRNAITM
QPQGGQGLSK ISEEPSTSSE ERASLIKKEI HGSISHLPEP SVPYRGTLVT MDPRNGYMDP
HYHPPHLFQA FHPPVPIDAR HHEGRYHYEP SPIPPLHVPS ALSSSPTYSD LPFIRISPHR
NPAAASESPF STPHPYINPY MDYIRSLHSS PSLSMISAAR GLSPTDAPHA GVSPAEYYHQ
MALLAGQRSP YADIIPSAAT AGAGALHMEY LHAMDSTRFP SPRLSARPSR KRTLSISPLS
DHSFDLQTMI RTSPNSLVTI LNNSCSSWSA SGSYGHLSAS AISPALSFTY PPTPVSLQQM
HQQIISRQQT LGSAFGHSPP LIHPAPTFPT QRPIPGIPSV LNPVQVSSGP SESTQHNKPT
SESAVSSTGD PMHNKRSKIK PDEDLPSPGA GSVQEQPEGM TPVKEEGDKD ESKQEPEVVY
ETNCHWEGCS REFDTQEQLV HHINNDHIHG EKKEFVCRWL DCSREQKPFK AQYMLVVHMR
RHTGEKPHKC TFEGCTKAYS RLENLKTHLR SHTGEKPYVC EHEGCNKAFS NASDRAKHQN
RTHSNEKPYV CKIPGCTKRY TDPSSLRKHV KTVHGPEAHV TKKQRGDIHP RPPPPRDPGS
HSQTRSPGQQ TQGATGEQKD LNSTTSRREE CLQVKAVKSE KPMTSQPSPG GQSTCSSEQS
PISNYSNNGI ELTLTGGGSV GDLSVIDETP IMDSTISTAT TALGLQARRN MTGTKWMEQV
KLERLKQVNG MLPRLNPVPP SKAPTLPPLI GNGTQSNSSC SVGGSMTILP NRNELSSTDI
TVLNMLNRRD SNTSTISSAY LSSRRSSGIS PCFSSRRSSD ASQAEGRPQN VSVADSYDPI
STDASRRSSE ASQCDDLPSL LSLTPAQQYR LKAKYAAATG GPPPTPLPNM ERMSLKTRMA
LLGDCRESGI SPLPPVNAPR RCSDGGANGY SRRHLLSHDA LGNGTRRASD PVRMVSNNLS
VPRVQHFNSL NSFNSPALPP SMEKRNLVLQ NCTHSEGGVF RGFSSPCPPS ISENVTLEAV
TMEAGGSLND EDLLPDDVVQ YLNSQNQGTC DHLLNNVLDS NKMHHSVVLG NNNPSSFDRA
PPASSQPAGS EVSKSDLPIQ WNEVSSGSSD LSPTKLKCSQ RSAVQQARAF GLYNNMMVQQ
QNLQRGNVYQ QNGYQNLMEN NGSYSLQQNT VLGSGASSSF GMQPNKPYGE SVSRQPMIFG
AMDSSCGITV QGQKLRSSNM PVSGNQQNFG HPIASSDQAT SMANGMQNRN VMEQEYLQNE
LVGDGIHYQG VNQSSPMTLG QVSPTSQSSL HQGPQSCPPV SHTIGNQSSG LSVAKSYQPC
ANYSGNRRQN VLRNNLAQQQ GHVSDGNQTY RVNTIKLEMQ GQSQQFCSNM QNYSGQLYDQ
TTGFSHQAMK IGSSFFVSEA NCLLQETATA NSSELLSPGA NQVSSTVDSL DSNSLEGVQI
DFDAIIDDGD HVSLISGALS PSIIQNLSRN SSRLTTPRAS LTFP
