ID   GLI4_XENLA              Reviewed;        1361 AA.
AC   Q91661;
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 GLI4;
DE   AltName: Full=Neural-specific DNA-binding protein xGLI4;
DE            Short=xGLI-4;
GN   Name=gli4;
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 an essential role in the early embryonic patterning of
CC       mesoderm and neuroectoderm.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; U42462; AAA98467.1; -; mRNA.
DR   PIR; T30884; T30884.
DR   RefSeq; NP_001081442.1; NM_001087973.1.
DR   AlphaFoldDB; Q91661; -.
DR   SMR; Q91661; -.
DR   GeneID; 397838; -.
DR   KEGG; xla:397838; -.
DR   CTD; 397838; -.
DR   Xenbase; XB-GENE-17342592; gli2.L.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 397838; Expressed in neurula embryo and 17 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
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; 5.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1361
FT                   /note="Zinc finger protein GLI4"
FT                   /id="PRO_0000047207"
FT   ZN_FING         289..314
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         322..349
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..379
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         385..410
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         416..441
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          185..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..824
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1188
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1361 AA;  149555 MW;  03AC399BAF4CC4DC CRC64;
     MEHYLRSVHN SPTLSMISAA RGLSPAEVAH EHLKERGIYG LAPPPPPGTT PTEYCHQMAF
     LASHASPYGE LLVQSAAAGN TSHLHDYLTP MDVSRFSSPR VTPRLSRKRA LSISPLSDAS
     IDLQTMIRTS PNSLVAYINN SRSSSAASGS YGHLSAGAIS PAFSFPIHKP CSLSAALSQQ
     RSLSSSFGHT PLLHPSPTFA SRQQGALTSA NPAPPSNNSS APDSVLNKVS SESAVSSTVN
     QVIHKRSKVK TEEEADSVRF PQPPDHLTDL KEDLDKDECK QEPEHIYETN CHWDGCSKEF
     DTQDQLVHHI NNDHIHGEKK EFVCRWQDCS REQKPFKAQY MLVVHMRRHT GEKPHKCTFE
     GCFKAYSRLE NLKTHLRSHT GEKPYVCDHE GCNKAFSNAS DRAKHQNRTH SNEKPYICKV
     PGCTKRYTDP SSLRKHVKTV HGPEAHVTKK HRNDIIQKPS LPKENGDNEA SAKLSGREHS
     DSVSRDQEHC LQTRTIKTED NMMHQSSPGG QSSCSSEPSP YGNTNNIDSG VDVSLAWQGS
     LGDLFGLEET SPVVDSTVSS WQRSGRPATP ETQRIHSAET GTAEEREIKD NERFLLIYEP
     NATCQNTRLP TISANGFDVI GVPSSVLINP RAIELSMNDV TMMNQLNERR DSTSSTLSSA
     YTSRRSSGIS PYFSSRRSSE TSQFGGRLNN SSSADSYDPI STDASRRSSE ASQHSGLPNL
     LNLTPAQHYR LKAKYAAATG GPPPTPLPNM DRIGLRNKLS LMDGADFPLP PFRQLPVPRR
     CSDGGGNAGL TPMYPHEIPG NNSRRASDPV RRTAGIDDKP LPRFSRFHSM NSMNTLHPPS
     LSERRNGGLQ HYTCSDGGLH RHVYSPRPPS ISENVAMEAI SCDADVPGGD DDLMLPDDVV
     QYIRSQNREA PEQNLQTEYS SPARNLQSNT KSFHNNTPEQ PRAPGAYLSR NFPALAECLG
     QTANMQDNNM PVQWNEVSSG TVDVSDLPKQ QFAAGNLAVV QQKQNFAQYQ SFNQAPMQRA
     HNIMGQGQES VQRNISVNGQ RFNYLQQRQQ QMSQCQIVSS DFIPQQRYSQ SQSMLSSRAM
     QEGQSQISPS CNNMVERPGV HTHAAPSNTL NHQRLAVHGA PTQGFANNFS VNQDGLHPPN
     AYTVQPQKNG LEPQQNTLGM SGQAFNHGMI QPRPPAAPHP PNRPRNIHPV HHPPYMRSPH
     PVSELSPGQQ TAEATPKRTS ENTDPTPKDN NLLYYSGQIH MYEPNGNFGS GIDCTVRQLP
     TMPSPGANQV TSTVDSQGLE HPPVIDFDAM MDDGDHSSLM SGTLSPGLLQ SFSQTSSRLT
     TPRNSLTLPS IPAGINNMAI GDMSSMLTTL AEESKFLNLM S