GLIS1_MOUSE
ID GLIS1_MOUSE Reviewed; 789 AA.
AC Q8K1M4; Q6NZF6; Q8R4Z3;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger protein GLIS1;
DE AltName: Full=GLI-similar 1;
DE AltName: Full=Gli homologous protein 1 {ECO:0000303|PubMed:12385751};
DE Short=GliH1 {ECO:0000303|PubMed:12385751};
GN Name=Glis1 {ECO:0000312|MGI:MGI:2386723}; Synonyms=Gli5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM93156.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAM93156.1};
RC TISSUE=Kidney {ECO:0000269|PubMed:12042312};
RX PubMed=12042312; DOI=10.1074/jbc.m203563200;
RA Kim Y.-S., Lewandoski M., Perantoni A.O., Kurebayashi S., Nakanishi G.,
RA Jetten A.M.;
RT "Identification of Glis1, a novel Gli-related, Kruppel-like zinc finger
RT protein containing transactivation and repressor functions.";
RL J. Biol. Chem. 277:30901-30913(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAM12150.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12385751; DOI=10.1016/s0925-4773(02)00291-5;
RA Nakashima M., Tanese N., Ito M., Auerbach W., Bai C., Furukawa T.,
RA Toyono T., Akamine A., Joyner A.L.;
RT "A novel gene, GliH1, with homology to the Gli zinc finger domain not
RT required for mouse development.";
RL Mech. Dev. 119:21-34(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH66157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-789 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH66157.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH66157.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=21654807; DOI=10.1038/nature10106;
RA Maekawa M., Yamaguchi K., Nakamura T., Shibukawa R., Kodanaka I.,
RA Ichisaka T., Kawamura Y., Mochizuki H., Goshima N., Yamanaka S.;
RT "Direct reprogramming of somatic cells is promoted by maternal
RT transcription factor Glis1.";
RL Nature 474:225-229(2011).
RN [5]
RP FUNCTION.
RX PubMed=30544251; DOI=10.1093/nar/gky1240;
RA Gerard D., Schmidt F., Ginolhac A., Schmitz M., Halder R., Ebert P.,
RA Schulz M.H., Sauter T., Sinkkonen L.;
RT "Temporal enhancer profiling of parallel lineages identifies AHR and GLIS1
RT as regulators of mesenchymal multipotency.";
RL Nucleic Acids Res. 47:1141-1163(2019).
CC -!- FUNCTION: Acts as both a repressor and activator of transcription
CC (PubMed:12042312, PubMed:12385751, PubMed:21654807). Binds to the
CC consensus sequence 5'-GACCACCCAC-3' (PubMed:12042312). By controlling
CC the expression of genes involved in cell differentiation inhibits the
CC lineage commitment of multipotent cells (PubMed:21654807,
CC PubMed:30544251). Prevents, for instance, the differentiation of
CC multipotent mesenchymal cells into adipocyte and osteoblast
CC (PubMed:30544251). {ECO:0000269|PubMed:12042312,
CC ECO:0000269|PubMed:12385751, ECO:0000269|PubMed:21654807,
CC ECO:0000269|PubMed:30544251}.
CC -!- SUBUNIT: Interacts with KLF4. Interacts with POU5F1 and/or POU5F1B.
CC Interacts with SOX2. {ECO:0000250|UniProtKB:Q8NBF1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12042312}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12042312};
CC IsoId=Q8K1M4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12385751};
CC IsoId=Q8K1M4-2; Sequence=VSP_051623;
CC -!- TISSUE SPECIFICITY: In the adult, expressed highly in placenta and
CC kidney and at lower levels in the testis, brain, colon, brown fat
CC tissue and thymus. During embryo development, expressed in the frontal
CC nasal region, branchial arches, somites, vibrissal and hair follicles,
CC limb buds, craniofacial regions, ventral part of the tail,
CC intervertebral disks, teeth, eyes and kidney.
CC {ECO:0000269|PubMed:12042312, ECO:0000269|PubMed:12385751}.
CC -!- DEVELOPMENTAL STAGE: Higher expression is detected in unfertilized eggs
CC and one-cell embryos compared to two-cells embryos and adult tissues
CC (PubMed:21654807). In the embryo, expression is detected at 10 dpc
CC becoming stronger by 11 dpc and continuing through to 16.5 dpc.
CC {ECO:0000269|PubMed:12042312, ECO:0000269|PubMed:12385751,
CC ECO:0000269|PubMed:21654807}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12385751}.
CC -!- BIOTECHNOLOGY: The combined transgenic expression of the OSK
CC transcription factors POU5F1/OCT4, SOX2 and KLF4, reprograms
CC differentiated cells into induced pluripotent stem cells/iSPCs. iPSCs
CC exhibit the morphology and properties of embryonic stem/ES cells. The
CC coexpression of GLIS1 can increase the efficiency of OSK-induced
CC pluripotent stem cells/iPSCs production. {ECO:0000269|PubMed:21654807}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH66157.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF486579; AAM93156.1; -; mRNA.
DR EMBL; AF220434; AAM12150.1; -; mRNA.
DR EMBL; BC066157; AAH66157.1; ALT_INIT; mRNA.
DR CCDS; CCDS38831.1; -. [Q8K1M4-1]
DR RefSeq; NP_671754.2; NM_147221.2. [Q8K1M4-1]
DR RefSeq; XP_006503036.1; XM_006502973.3. [Q8K1M4-1]
DR RefSeq; XP_006503037.1; XM_006502974.3. [Q8K1M4-1]
DR RefSeq; XP_006503038.1; XM_006502975.1. [Q8K1M4-1]
DR AlphaFoldDB; Q8K1M4; -.
DR SMR; Q8K1M4; -.
DR BioGRID; 230975; 16.
DR STRING; 10090.ENSMUSP00000035650; -.
DR iPTMnet; Q8K1M4; -.
DR PhosphoSitePlus; Q8K1M4; -.
DR MaxQB; Q8K1M4; -.
DR PaxDb; Q8K1M4; -.
DR PRIDE; Q8K1M4; -.
DR ProteomicsDB; 267451; -. [Q8K1M4-1]
DR ProteomicsDB; 267452; -. [Q8K1M4-2]
DR Antibodypedia; 748; 126 antibodies from 27 providers.
DR DNASU; 230587; -.
DR Ensembl; ENSMUST00000046005; ENSMUSP00000035650; ENSMUSG00000034762. [Q8K1M4-1]
DR GeneID; 230587; -.
DR KEGG; mmu:230587; -.
DR UCSC; uc008tzv.1; mouse. [Q8K1M4-1]
DR CTD; 148979; -.
DR MGI; MGI:2386723; Glis1.
DR VEuPathDB; HostDB:ENSMUSG00000034762; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159218; -.
DR InParanoid; Q8K1M4; -.
DR OMA; CYRTMDQ; -.
DR OrthoDB; 703190at2759; -.
DR PhylomeDB; Q8K1M4; -.
DR TreeFam; TF350216; -.
DR BioGRID-ORCS; 230587; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Glis1; mouse.
DR PRO; PR:Q8K1M4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K1M4; protein.
DR Bgee; ENSMUSG00000034762; Expressed in animal zygote and 110 other tissues.
DR ExpressionAtlas; Q8K1M4; baseline and differential.
DR Genevisible; Q8K1M4; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0010454; P:negative regulation of cell fate commitment; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR030430; GLIS1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR PANTHER; PTHR45718:SF3; PTHR45718:SF3; 1.
DR Pfam; PF00096; zf-C2H2; 2.
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 1: Evidence at protein level;
KW Activator; Alternative splicing; Differentiation; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..789
FT /note="Zinc finger protein GLIS1"
FT /id="PRO_0000047210"
FT ZN_FING 366..391
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..427
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 433..457
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..487
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 493..517
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 511..527
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 651..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12385751"
FT /id="VSP_051623"
FT CONFLICT 173
FT /note="V -> A (in Ref. 1; AAM93156)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="G -> R (in Ref. 1; AAM93156)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="E -> G (in Ref. 3; AAH66157)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="V -> E (in Ref. 3; AAH66157)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Q -> R (in Ref. 1; AAM93156)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="V -> A (in Ref. 3; AAH66157)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="Y -> S (in Ref. 3; AAH66157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 84172 MW; 98D87D9EA20D38FD CRC64;
MHCEVAEALS DKRPKEAPGA PGQGRGPVSL GAHMAFRIAV SGGGCGDGNP LDLLPRLPVP
PPRAHDLLRP RSPRDYGVSK TGSGKVNGSY GHSSEKSLLD LDLAEGPSPS CHQGLFLPAG
TPPPRGHPPV CEKLLHFPHP NRSPRPQATF VNGSLPAAQH IKQEALPDYQ AMVSAHTPLP
THCRAPSSMG LPSDLDFPDR GLTNPAPSCY LLGNEPISDL GPQPEAHLPE GSLKRCCLLG
LPPTSSASSS PCASSDINPV IHSSQTALVS CVNGLRSPPL PGDLGGPPKR SRPGPASSDG
QEGSLQLEAC RKSGFLKQEP MDEFSELFAP HHQGLPPPYP LPQLPTGPGL GGLGLGLAGR
MVAGRQACRW VDCCAAYEQQ EELVRHIEKS HIDQRKGEDF TCFWAGCVRR YKPFNARYKL
LIHMRVHSGE KPNKCMFEGC SKAFSRLENL KIHLRSHTGE KPYLCQHPGC QKAFSNSSDR
AKHQRTHLDT KPYACQIPGC SKRYTDPSSL RKHVKAHSAK EQQVRKKLHT GADPEADVLS
ECLSLQQLQA STLLPASRGK GSQTLSQELL PGVYPGSVTP QNGLASGILS PSHDVPSRHH
PLEVPTGSHH HLSPLPTAES TRDGLGPSLL SPMVSPLKGL GPPPLPPASQ SQSPGGQSFS
TVPSKPTYPS FQSPPPLPSP QGYQGSFHSI QNCFPYADCY RATEPAASRD GLVGDAHGFN
PLRPSTYSSL STPLSAPGYE TLAETPCPPA LQPQPAEDLV PSGPEDCGFF PNGAFDHCLS
HIPSIYTDT
