ZIC1_MOUSE
ID ZIC1_MOUSE Reviewed; 447 AA.
AC P46684; Q6PAK5; Q80Y18;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger protein ZIC 1;
DE AltName: Full=Zinc finger protein of the cerebellum 1;
GN Name=Zic1; Synonyms=Zic;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=ICR; TISSUE=Cerebellum;
RX PubMed=7931345; DOI=10.1046/j.1471-4159.1994.63051880.x;
RA Aruga J., Yokota N., Hashimoto M., Furuichi T., Fukuda M., Mikoshiba K.;
RT "A novel zinc finger protein, zic, is involved in neurogenesis, especially
RT in the cell lineage of cerebellar granule cells.";
RL J. Neurochem. 63:1880-1890(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=11053430; DOI=10.1074/jbc.m004430200;
RA Mizugishi K., Aruga J., Nakata K., Mikoshiba K.;
RT "Molecular properties of Zic proteins as transcriptional regulators and
RT their relationship to GLI proteins.";
RL J. Biol. Chem. 276:2180-2188(2001).
RN [6]
RP FUNCTION, INTERACTION WITH GLI1; GLI2 AND GLI3, AND SUBCELLULAR LOCATION.
RX PubMed=11238441; DOI=10.1074/jbc.c000773200;
RA Koyabu Y., Nakata K., Mizugishi K., Aruga J., Mikoshiba K.;
RT "Physical and functional interactions between Zic and Gli proteins.";
RL J. Biol. Chem. 276:6889-6892(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=11944941; DOI=10.1006/dbio.2002.0598;
RA Aruga J., Tohmonda T., Homma S., Mikoshiba K.;
RT "Zic1 promotes the expansion of dorsal neural progenitors in spinal cord by
RT inhibiting neuronal differentiation.";
RL Dev. Biol. 244:329-341(2002).
RN [8]
RP FUNCTION, INTERACTION WITH MDFIC, AND SUBCELLULAR LOCATION.
RX PubMed=15207726; DOI=10.1016/j.bbrc.2004.05.158;
RA Mizugishi K., Hatayama M., Tohmonda T., Ogawa M., Inoue T., Mikoshiba K.,
RA Aruga J.;
RT "Myogenic repressor I-mfa interferes with the function of Zic family
RT proteins.";
RL Biochem. Biophys. Res. Commun. 320:233-240(2004).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19303920; DOI=10.1016/j.neuroscience.2009.02.082;
RA Dipietrantonio H.J., Dymecki S.M.;
RT "Zic1 levels regulate mossy fiber neuron position and axon laterality
RT choice in the ventral brain stem.";
RL Neuroscience 162:560-573(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20354137; DOI=10.1096/fj.09-148908;
RA Kalogeropoulos M., Varanasi S.S., Olstad O.K., Sanderson P., Gautvik V.T.,
RA Reppe S., Francis R.M., Gautvik K.M., Birch M.A., Datta H.K.;
RT "Zic1 transcription factor in bone: neural developmental protein regulates
RT mechanotransduction in osteocytes.";
RL FASEB J. 24:2893-2903(2010).
CC -!- FUNCTION: Acts as a transcriptional activator. Involved in
CC neurogenesis. Plays important roles in the early stage of organogenesis
CC of the CNS, as well as during dorsal spinal cord development and
CC maturation of the cerebellum. Involved in the spatial distribution of
CC mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a
CC role in the regulation of MF axon pathway choice. Promotes MF migration
CC towards ipsilaterally-located cerebellar territories. May have a role
CC in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1
CC and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence
CC 5'-TGGGTGGTC-3'. {ECO:0000269|PubMed:11053430,
CC ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:11944941,
CC ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:19303920,
CC ECO:0000269|PubMed:20354137, ECO:0000269|PubMed:7931345}.
CC -!- SUBUNIT: Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC
CC (via the C2H2-type domains 3, 4 and 5). Interacts with GLI1; the
CC interaction enhances transcription activation. Interacts with GLI2.
CC Interacts with GLI3; the interaction enhances transcription activation.
CC {ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:15207726}.
CC -!- INTERACTION:
CC P46684; Q8K0K3: Gli2; NbExp=2; IntAct=EBI-308006, EBI-308039;
CC P46684; P08151: GLI1; Xeno; NbExp=2; IntAct=EBI-308006, EBI-308084;
CC P46684; P10071: GLI3; Xeno; NbExp=2; IntAct=EBI-308006, EBI-308055;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes in the
CC cytoplasm in presence of MDFIC overexpression.
CC -!- TISSUE SPECIFICITY: Expressed in osteoblasts (at protein level).
CC Expressed in the CNS. A high level expression is seen in the
CC cerebellum, while a low level expression is seen in the olfactory bulb,
CC diencephalon, and brainstem. Expressed in lumbar spine and iliac crest.
CC {ECO:0000269|PubMed:19303920, ECO:0000269|PubMed:20354137,
CC ECO:0000269|PubMed:7931345}.
CC -!- DEVELOPMENTAL STAGE: Expressed in progenitor cells in the dorsal third
CC of the ventricular zone at 12.5 dpc. Expressed in newly emerging
CC pontine gray nucleus (PGN) precursor cells of the extramural migratory
CC stream (ems) between 12.5 and 14.5 dpc. Expressed in precerebellar
CC mossy fiber (MF) neurons of the PGN (located either rostromedially or
CC caudolaterally) persisted through at least P8 after birth (at protein
CC level). In the early embryonic stage, it is expressed in the dorsal
CC half of the neural tube and adjacent mesenchyme, and in the developing
CC cerebellum it is expressed persistently in the granule cell lineage
CC throughout the prenatal and postnatal periods.
CC {ECO:0000269|PubMed:11944941, ECO:0000269|PubMed:7931345}.
CC -!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for
CC transcription activation.
CC -!- DISRUPTION PHENOTYPE: Mice show a cell mass decrease of the spinal
CC dorsal horn, hypoplasia and abnormal foliation patterns in the
CC cerebellum. {ECO:0000269|PubMed:11944941}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; D32167; BAA06878.1; -; mRNA.
DR EMBL; AK136977; BAE23194.1; -; mRNA.
DR EMBL; CH466560; EDL20910.1; -; Genomic_DNA.
DR EMBL; BC050889; AAH50889.2; -; mRNA.
DR EMBL; BC060247; AAH60247.1; -; mRNA.
DR EMBL; BC063247; AAH63247.1; -; mRNA.
DR CCDS; CCDS23403.1; -.
DR PIR; I56511; I56511.
DR RefSeq; NP_033599.2; NM_009573.3.
DR RefSeq; XP_006511124.1; XM_006511061.1.
DR AlphaFoldDB; P46684; -.
DR SMR; P46684; -.
DR BioGRID; 204694; 1.
DR IntAct; P46684; 3.
DR MINT; P46684; -.
DR STRING; 10090.ENSMUSP00000034927; -.
DR iPTMnet; P46684; -.
DR PhosphoSitePlus; P46684; -.
DR MaxQB; P46684; -.
DR PaxDb; P46684; -.
DR PeptideAtlas; P46684; -.
DR PRIDE; P46684; -.
DR ProteomicsDB; 275371; -.
DR Antibodypedia; 1317; 416 antibodies from 33 providers.
DR DNASU; 22771; -.
DR Ensembl; ENSMUST00000034927; ENSMUSP00000034927; ENSMUSG00000032368.
DR Ensembl; ENSMUST00000065360; ENSMUSP00000068858; ENSMUSG00000032368.
DR GeneID; 22771; -.
DR KEGG; mmu:22771; -.
DR UCSC; uc009raf.1; mouse.
DR CTD; 7545; -.
DR MGI; MGI:106683; Zic1.
DR VEuPathDB; HostDB:ENSMUSG00000032368; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160269; -.
DR HOGENOM; CLU_002678_37_1_1; -.
DR InParanoid; P46684; -.
DR OMA; MKVHSKS; -.
DR OrthoDB; 768287at2759; -.
DR PhylomeDB; P46684; -.
DR TreeFam; TF351425; -.
DR BioGRID-ORCS; 22771; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Zic1; mouse.
DR PRO; PR:P46684; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P46684; protein.
DR Bgee; ENSMUSG00000032368; Expressed in habenula and 179 other tissues.
DR Genevisible; P46684; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0098727; P:maintenance of cell number; IGI:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IGI:MGI.
DR GO; GO:0007389; P:pattern specification process; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IPI:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; NAS:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IMP:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR041643; Znf_ZIC.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF18366; zf_ZIC; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..447
FT /note="Zinc finger protein ZIC 1"
FT /id="PRO_0000047245"
FT ZN_FING 225..260
FT /note="C2H2-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 269..296
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 302..326
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 332..356
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 375..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="A -> R (in Ref. 1; BAA06878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 48331 MW; D41F412F44C2AD3D CRC64;
MLLDAGPQYP AIGVTTFGAS RHHSAGDVAE RDVGLGINPF ADGMGAFKLN PSSHELASAG
QTAFTSQAPG YAAAAALGHH HHPGHVGSYS SAAFNSTRDF LFRNRGFGDA AAAASAQHSL
FAASAGGFGG PHGHTDAAGH LLFSGLHEQA AGHASPNVVN GQMRLGFSGD MYPRPEQYGQ
VTSPRSEHYA APQLHGYGPM NVNMAAHHGA GAFFRYMRQP IKQELICKWI EPEQLANPKK
SCNKTFSTMH ELVTHVTVEH VGGPEQSNHI CFWEECPREG KPFKAKYKLV NHIRVHTGEK
PFPCPFPGCG KVFARSENLK IHKRTHTGEK PFKCEFEGCD RRFANSSDRK KHMHVHTSDK
PYLCKMCDKS YTHPSSLRKH MKVHESSSQG SQPSPAASSG YESSTPPTIV SPTTDNPTTS
SMSPSSSAVH HTAGHSALSS NFNEWYV
