ID   GLI1_XENLA              Reviewed;        1360 AA.
AC   Q91690;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Zinc finger protein GLI1;
DE            Short=GLI-1;
DE   Flags: Fragment;
GN   Name=gli1;
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], AND FUNCTION.
RX   PubMed=9216996; DOI=10.1242/dev.124.13.2537;
RA   Lee J., Platt K.A., Censullo P., Ruiz i Altaba A.;
RT   "Gli1 is a target of Sonic hedgehog that induces ventral neural tube
RT   development.";
RL   Development 124:2537-2552(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Lee J., Platt K.A., Censullo P., Ruiz i Altaba A.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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:9216996). Mediates SHH signaling (PubMed:9216996). Plays a role
CC       in cell proliferation and differentiation via its role in SHH signaling
CC       (By similarity). {ECO:0000250|UniProtKB:P08151,
CC       ECO:0000305|PubMed:9216996}.
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; U57454; AAC24946.1; -; mRNA.
DR   PIR; T12064; T12064.
DR   AlphaFoldDB; Q91690; -.
DR   SMR; Q91690; -.
DR   Proteomes; UP000186698; Genome assembly.
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: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: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: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:0007224; P:smoothened signaling pathway; IEA:InterPro.
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; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..>1360
FT                   /note="Zinc finger protein GLI1"
FT                   /id="PRO_0000047200"
FT   ZN_FING         250..275
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         316..340
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         346..371
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         377..402
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          198..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..306
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P08151"
FT   REGION          360..365
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P08151"
FT   REGION          390..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..396
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P08151"
FT   REGION          457..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1120..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..419
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1360
SQ   SEQUENCE   1360 AA;  149422 MW;  5A32B8086794EC2D CRC64;
     MASRQCPPAA VFNSMNPPVN SYVEHCYLRS PNVMAEGMNE MPYCHQTNLM TSHHGFGLAQ
     GSDHLAGTDG SRFSTPRSTM KLSKKRAMSI SPLSDASIDL QTMIRTSPNS LVAFINSRCS
     SASGSYGHLS IGTISPSLGY QNCLNHQRPQ AGPYGSNPLM PYNSHEHLSS RGMSMLQPRS
     SVKHCQLKSE PLSITGLDTI GSKRLEDGSE GDISSPASVG TQDPLLGLLD GRDDLEKDDG
     KHEPETVYET NCHWESCTKE FDTQEHLVHH INNEHIHGEK KEFVCHWQDC SRELRPFKAQ
     YMLVVHMRRH TGEKPHKCTF EGCNKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA
     SDRAKHQNRT HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHITK KHRGDGMLRA
     QPGHEGPGNQ NVKGENQLDM EASSACKEDG RLAVPDITLK SQPSPGGQSS CSSERSPLGS
     TNNNDSGVEM NANTGGSFED LTNLDDIPSV DSMGTAGASA LRKLENLRID KLNQLRKTPS
     SGKMVKLPSI HNSGPQGDMS VVCGPLGMSH NQHGIELPAS SHVNHLNDRR NSTTSTMSSA
     YTVSRRSSVV SPYLPNQRAG DSGNMVDSYD ISTDPSGHSN EAVCASGLPG LTPAQQYRLK
     AKYAAATGGP PPTPLPNMER MNTNNRMAFA SSDYRGSAIS SLQRRHSSNE YHNYGTGIIH
     PAQAPGAGIR RASDPARTGG DIQAVPKVQR FKSMTNMNVS MMGRQGTSIQ QAYGGSDANL
     QRHMFSPRPP SITENVFMET AGPDEVCHTK EQGFIQSNEM QHYMNYQGQG SQLTAPNDHM
     NFNPQIHGLD GQSQNVYSHS QRAISNMHLN AENYSGQSNV SNFNQCQMTA HNQHFQNTRQ
     AYNCANLPVQ WNEVSSGTMD NPVQRPNHQI MHQNMSPGNH CQSQLSNCTV PESTKQGCPV
     NRNSCQQGMY MNNQKYNHGG QVQVKPEQQF HHSAPAMMSC QNMKHPSRQE HHFTKTNTMP
     LSSEATNCDY QGQQDSTQNS CFNVGLNLNL LSPPGRRSQT PIMQVKEIMV RNYVQSQQAL
     MWEQHPKSMA MMTNSGDDVD TRQNQHKNTL NAAVYMGPKY MNYQGKPSPN NLMSPSSQDS
     QSSHTKAMGS PSSQCYNFDM MPHPPCGPKP LSRQHSVSSQ STYMGSPNQL SPSYQSSESS
     PRRMACLPPI QPQSEVTNNT SMMYYTGQME MHQSKPGVHK LTTPLNLNQT SCDGHQHGQY
     NASHSFLKTV PYTSSCPAAN TLDSLDLENT QIDFTAIIDD ADNALMPGNI SPNVLAGSSQ
     ASSHLTTLRN TGAVVPNMVV GDLNSMLSSL AGENKYLNTM