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Database: UniProt
Entry: A0A3Q3F7M4_9LABR
LinkDB: A0A3Q3F7M4_9LABR
Original site: A0A3Q3F7M4_9LABR 
ID   A0A3Q3F7M4_9LABR        Unreviewed;      1538 AA.
AC   A0A3Q3F7M4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Transcriptional activator GLI3-like {ECO:0000313|Ensembl:ENSLBEP00000014962.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000014962.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000014962.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000256|ARBA:ARBA00010831}.
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DR   STRING; 56723.ENSLBEP00000014962; -.
DR   Ensembl; ENSLBET00000015870.1; ENSLBEP00000014962.1; ENSLBEG00000011632.1.
DR   GeneTree; ENSGT00940000155925; -.
DR   InParanoid; A0A3Q3F7M4; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
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   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR043359; GLI-like.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45718; TRANSCRIPTIONAL ACTIVATOR CUBITUS INTERRUPTUS; 1.
DR   PANTHER; PTHR45718:SF5; TRANSCRIPTIONAL ACTIVATOR GLI3; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          472..504
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          510..537
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          538..567
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          568..598
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          599..629
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          43..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1158..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..853
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1158..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1538 AA;  168269 MW;  767BDFC641E86989 CRC64;
     LKLERQELAF NLKRKQERAL KFVQCSPSTI SLFLPLASRH LSDESSGTPY HRERRNAISS
     QAPTPTRTIS EEPSTSTEDR PSLLKKELHS SIPHLSDHAL PYRGTLFTMD PRNGYLDSHY
     HAPQFFPTFH PPVPIDDRHT QGRYIYEPSP VPPLHVPPSL AGSPAFSDIS LIRISPQRNP
     SVGAESPFHP PHPYINPYMD YIRSLHSSPS ISVLSATRGL SPADAPHTGL TTAEYYHQMA
     LLAGHRSPYA TDLLPSVAST AGASSASALH MEYLQAMENS RFSSPRLPSR PSRKRPLPIS
     PLSEHSFDLQ TMIRNSPNSL VTMLNNSRSS SSTSGSYGHL SAGAISPALS FAYPPTPVAL
     HVHQQLMGRQ PGLVGSAFGH SPPLIHPSPA FATQRPVPGI PPSGLSTKPT SESAVSSTGD
     PMHHKRSKMK PEEDLPSPGA VSVQDHPDGM TLVKEEGDKD ENKQEPEVVY ETNCHWENCC
     REFDTQEQLV QHINNDHIHG EKKEFVCRWE ECSREQKPFK AQYMLVVHMR RHTGEKPHKC
     TFEGCAKAYS RLENLKTHLR SHTGEKPYVC EHEGCNKAFS NASDRAKHQN RTHSNEKPYV
     CKIPGCTKRY TDPSSLRKHV KTVHGPEAHV TKKQRGDYPR PPPQHKEPGG NSQGRSPGHL
     PLGGYTDQRE YNHATSKQDE CLQVKSIKTE KPMASQPSPG GESTCSSDQS PFSTYPSSGV
     QLAVSCEGEP APIMDSTVST ATTAMLTLQA RRSVGRPVRW MEHIKMERLK QVNGGLPRPG
     TLSPTPPPKG STLPTILGKG SCLGRQWGVS APQPPAHAEL GSTELTVLNL LRDRRDSSGS
     ATSSAYLSSS RRSSATQHRR RHNLSSTDSY DPISTDASRR SSEARSQGML TLTPAQHYHL
     KAKYAAATGG PPPTPLPNME RMSLKTRMAM MDDGGSNHSL PPLVRPHRCS DGINGYTNGY
     MGHSGYRRRV LLPGEGPLNG NRRASDPVRT QAPDCCSLPP VQRFNSLNNL HPLPPLSQYS
     TPETRNFSLQ NYTRSEGNLQ RGLQHSPYTP SIAEHSALEA LAMEDEGEAG LLLGDEDMLP
     DDLVQYLHSH VQVDGGSYMN VEDQIVSSQR ENSHPSMEEI EQIQNGLNMA LSGSHCLQQQ
     QMVERRSPSK LPIQWNEVSS GSADRSPQRE QNHQTQCGRW SGTEHGPTAA PFGRFGNMVV
     QQQVPLDLQN SCAQANQSQS SCCVNPGVKL ETSPRSCMEM RGTGQNPTNP FGRPNFAQIN
     NGPLHELKQQ ASHGPRKQSH FLPNHNSSTS CQIGNNLVLT RASMDHLPSL SQGTAPLHNR
     QVHVPRPPNT HRNLVRAQQC LSLENSGEIQ GCLNQQQQLQ RSGDHCSLAY QVSGLKLEAP
     DHGYQEQGFG DCLSYEPVDH KASSYPVLED QCLLDSMAET VGQGSSSGSG NSVALLSPGA
     DQVTSTVDGT VPGVLDEGVS LDFSAMLEDG FDQGSLVSGV LSPSIFQGLS RTSSRLTTPR
     ASATFHSVAP GLNNMAIGDM SSLLTTLAEE SKFLAIMQ
//
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