GLIS2_XENLA
ID GLIS2_XENLA Reviewed; 492 AA.
AC Q98T94; Q5U4V3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Zinc finger protein GLIS2;
DE AltName: Full=GLI-similar 2;
DE AltName: Full=Neuronal Krueppel-like protein;
GN Name=glis2; Synonyms=nkl;
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], DEVELOPMENTAL STAGE, INDUCTION BY NGN1, AND
RP FUNCTION.
RX PubMed=11262234; DOI=10.1242/dev.128.8.1335;
RA Lamar E., Kintner C., Goulding M.;
RT "Identification of NKL, a novel Gli-Kruppel zinc-finger protein that
RT promotes neuronal differentiation.";
RL Development 128:1335-1346(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can act either as a transcription repressor or as a
CC transcription activator, depending on the cell context. May be involved
CC in neuron differentiation. {ECO:0000269|PubMed:11262234}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: In neural plate stage embryos, expressed in
CC precursors of primary sensory and motor neurons. At tailbud stages,
CC expression persists in neural tube and is up-regulated in anterior
CC structures such as eye and brain, and in branchial arches.
CC {ECO:0000269|PubMed:11262234}.
CC -!- INDUCTION: By ngn1. {ECO:0000269|PubMed:11262234}.
CC -!- DOMAIN: The C2H2-type zinc finger 1 has a major repressor function.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF249341; AAK28411.1; -; mRNA.
DR EMBL; BC084941; AAH84941.1; -; mRNA.
DR RefSeq; NP_001082092.1; NM_001088623.1.
DR AlphaFoldDB; Q98T94; -.
DR SMR; Q98T94; -.
DR GeneID; 398220; -.
DR KEGG; xla:398220; -.
DR CTD; 398220; -.
DR Xenbase; XB-GENE-6251812; glis2.S.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 398220; Expressed in lung and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR030432; Glis2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19818:SF84; PTHR19818:SF84; 1.
DR Pfam; PF00096; zf-C2H2; 3.
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; 4.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..492
FT /note="Zinc finger protein GLIS2"
FT /id="PRO_0000286985"
FT ZN_FING 158..183
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..219
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 225..247
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..277
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 283..307
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 49..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..129
FT /note="Transcription activation"
FT /evidence="ECO:0000250"
FT REGION 138..161
FT /note="Transcription repression"
FT /evidence="ECO:0000250"
FT REGION 423..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 136
FT /note="P -> L (in Ref. 2; AAH84941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 53959 MW; 0433A5446F14A790 CRC64;
MHSLDEPLDL KLSISKLRAA REKRERIGAN ARKRSVHHEL MIRDDGTTVI TPICSSPPPG
FRYRDGDSPP FSSPPIVDLS LSPPSGTDSP SRSSLSPDRA AGDTLIDNPL LRCGGDSASS
PFQFFLPLGS GLQLPPSMFM SPPKENRLSL EFTEQKQLVC QWAKCNRLFE LLQELVDHVN
DFHVKPEKDA GYCCHWEGCA RRGRGFNARY KMLIHIRTHT NERPHCCPTC HKSFSRLENL
KIHNRSHTGE KPYMCPYEGC NKRYSNSSDR FKHTRTHYVD KPYYCKMPGC QKRYTDPSSL
RKHIKAHGHF ISHQQRQLLK IHQPPKLPAT GDSNYTNGTQ LIIPNPAAIF GSQSLPIPLT
PGPLDLSSLA CSSVASALAG LPNPMLTLAG SPLNLAKGSL LSQAYSAAGL GLPLISLVTS
GKVENEKRPK GQRGDSSERT DGSKLRPGSI EGLSLLPRGV LDLSPGVGSE SLLPGWVVIP
PGSVLLKPAV VN
