GLIS3_MOUSE
ID GLIS3_MOUSE Reviewed; 780 AA.
AC Q6XP49; Q8BI60;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Zinc finger protein GLIS3;
DE AltName: Full=GLI-similar 3;
GN Name=Glis3 {ECO:0000312|EMBL:AAP59883.1};
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:AAP59883.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster {ECO:0000312|EMBL:AAP59883.1};
RC TISSUE=Kidney {ECO:0000269|PubMed:14500813};
RX PubMed=14500813; DOI=10.1093/nar/gkg776;
RA Kim Y.-S., Nakanishi G., Lewandoski M., Jetten A.M.;
RT "GLIS3, a novel member of the GLIS subfamily of Kruppel-like zinc finger
RT proteins with repressor and activation functions.";
RL Nucleic Acids Res. 31:5513-5525(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as both a repressor and activator of transcription.
CC Binds to the consensus sequence 5'-GACCACCCAC-3'.
CC {ECO:0000269|PubMed:14500813}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14500813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6XP49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6XP49-2; Sequence=VSP_012281, VSP_012282, VSP_012283;
CC -!- TISSUE SPECIFICITY: In the embryo, expressed at high levels in the
CC kidney and testis. In the adult, expressed at high levels in the kidney
CC and uterus and at lower levels in the brain, lung, skeletal muscle and
CC pancreas. {ECO:0000269|PubMed:14500813}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression is detected between days
CC 6.5 and 14.5, particularly during neurulation. At embryonic days 11.5
CC to 12.5, expression is high in the interdigital regions destined to
CC undergo apoptosis. {ECO:0000269|PubMed:14500813}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP59883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY220846; AAP59883.1; ALT_INIT; mRNA.
DR EMBL; AK054020; BAC35623.1; -; mRNA.
DR RefSeq; XP_006527048.1; XM_006526985.3. [Q6XP49-1]
DR AlphaFoldDB; Q6XP49; -.
DR SMR; Q6XP49; -.
DR BioGRID; 230466; 1.
DR CORUM; Q6XP49; -.
DR STRING; 10090.ENSMUSP00000124635; -.
DR iPTMnet; Q6XP49; -.
DR PhosphoSitePlus; Q6XP49; -.
DR MaxQB; Q6XP49; -.
DR PaxDb; Q6XP49; -.
DR PRIDE; Q6XP49; -.
DR ProteomicsDB; 270992; -. [Q6XP49-1]
DR ProteomicsDB; 270993; -. [Q6XP49-2]
DR Antibodypedia; 23977; 103 antibodies from 21 providers.
DR DNASU; 226075; -.
DR Ensembl; ENSMUST00000112612; ENSMUSP00000108231; ENSMUSG00000052942. [Q6XP49-2]
DR GeneID; 226075; -.
DR UCSC; uc008hch.2; mouse. [Q6XP49-1]
DR CTD; 169792; -.
DR MGI; MGI:2444289; Glis3.
DR VEuPathDB; HostDB:ENSMUSG00000052942; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156896; -.
DR HOGENOM; CLU_481988_0_0_1; -.
DR InParanoid; Q6XP49; -.
DR BioGRID-ORCS; 226075; 6 hits in 59 CRISPR screens.
DR ChiTaRS; Glis3; mouse.
DR PRO; PR:Q6XP49; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6XP49; protein.
DR Bgee; ENSMUSG00000052942; Expressed in animal zygote and 169 other tissues.
DR ExpressionAtlas; Q6XP49; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
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:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR030405; GLIS3.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR PANTHER; PTHR45718:SF1; PTHR45718:SF1; 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; 5.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..780
FT /note="Zinc finger protein GLIS3"
FT /id="PRO_0000047212"
FT ZN_FING 345..370
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..406
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..436
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 442..466
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..496
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 80..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..506
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MNGRSCGMNLHRTSRTPQGPGLLGGQHIPPIRAHAGTPCSSSCASTP
FT SPSIGSLANSLHLKMSSGAGMAPQSNMAASPIHLPALSPRRQLLANGKPQFQVTPAGVM
FT AAPHTIKPKQQEFGDPFSPNPEKGALGFGPQCKSIGKGSCNNLVVTSSPM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012281"
FT VAR_SEQ 508..516
FT /note="RSSTELHPD -> TNICASSHW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012282"
FT VAR_SEQ 517..780
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012283"
FT CONFLICT 274
FT /note="L -> P (in Ref. 2; BAC35623)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="L -> I (in Ref. 2; BAC35623)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 83882 MW; 9A15F8FBC1775787 CRC64;
MMVQRLGPIS PPASQVSTAC KQISPSLPRA VNAANLNRPP SDTRSVILQE SLVSTTLSLT
ESQSALSVKQ EWSQSYRAFP SLSSSHSSQN GTDLGDLLSL PPGTPVSGNS VSNSLPPYLF
GMENSHSPYP SPRHSATRAH STRSKKRALS LSPLSDGIGI DFNTIIRTSP TSLVAYINGP
RASPANLSPQ SEVYGHFLGV RGSCIPQSCA VASGQKGILV ASGGHTLPGY GEDGTLEYER
MQQLEHGGLQ PGPVNNMVLQ PGLPGQDGQT ANMLKTERLE EFPASALDLP SALPLPLPPP
QGPPPPYHAH PHLHHPELLP HTQSLSLAQT GLEEDGEMED SGGKHCCRWI DCSALYDQQE
ELVRHIEKVH IDQRKGEDFT CFWTGCPRRY KPFNARYKLL IHMRVHSGEK PNKCTFEGCK
KAFSRLENLK IHLRSHTGEK PYLCQHPGCQ KAFSNSSDRA KHQRTHLDTK PYACQIPGCT
KRYTDPSSLR KHVKAHSSRE QQARKKLRSS TELHPDLLTD CLAVQPLQPA TSPGDAADHT
VGHSPGPGPG PGPGAELYSA PIFASNHSTR SGTAAGAGPP PHPVSHPSPG HNVQGSPHNP
SSQLPPLTAV DAGAERFAPP TPSPHHISPG RVPAPPSLLQ RAQAPHSQQP PGSLLKPYQP
ETNSSFQPNG IHVHGFYGQL QTFCPPHYPD SQRTVPPSGS CSMVPSFEDC LVPTSMGQAG
FDVFHRAFST HSGITVYDLP SASSSLFGES LRSGPEDPTF LQLSAVDRCP SQLSSVYTEG
