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Zinc finger protein ZIC 2 (Zinc finger protein of the cerebellum 2)

 ZIC2_MOUSE              Reviewed;         530 AA.
Q62520;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 2.
22-NOV-2017, entry version 139.
RecName: Full=Zinc finger protein ZIC 2;
AltName: Full=Zinc finger protein of the cerebellum 2;
Name=Zic2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cerebellum;
PubMed=8557628; DOI=10.1074/jbc.271.2.1043;
Aruga J., Nagai T., Tokuyama T., Hayashizaki Y., Okazaki Y.,
Chapman V.M., Mikoshiba K.;
"The mouse zic gene family. Homologues of the Drosophila pair-rule
gene odd-paired.";
J. Biol. Chem. 271:1043-1047(1996).
[2]
SEQUENCE REVISION TO 488-512.
Aruga J.;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=10677508; DOI=10.1073/pnas.97.4.1618;
Nagai T., Aruga J., Minowa O., Sugimoto T., Ohno Y., Noda T.,
Mikoshiba K.;
"Zic2 regulates the kinetics of neurulation.";
Proc. Natl. Acad. Sci. U.S.A. 97:1618-1623(2000).
[4]
FUNCTION, AND DNA-BINDING.
PubMed=11053430; DOI=10.1074/jbc.M004430200;
Mizugishi K., Aruga J., Nakata K., Mikoshiba K.;
"Molecular properties of Zic proteins as transcriptional regulators
and their relationship to GLI proteins.";
J. Biol. Chem. 276:2180-2188(2001).
[5]
SUBCELLULAR LOCATION, AND INTERACTION WITH GLI1 AND GLI2.
PubMed=11238441; DOI=10.1074/jbc.C000773200;
Koyabu Y., Nakata K., Mizugishi K., Aruga J., Mikoshiba K.;
"Physical and functional interactions between Zic and Gli proteins.";
J. Biol. Chem. 276:6889-6892(2001).
[6]
FUNCTION.
PubMed=11756505;
Aruga J., Inoue T., Hoshino J., Mikoshiba K.;
"Zic2 controls cerebellar development in cooperation with Zic1.";
J. Neurosci. 22:218-225(2002).
[7]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=13678579; DOI=10.1016/S0092-8674(03)00684-6;
Herrera E., Brown L., Aruga J., Rachel R.A., Dolen G., Mikoshiba K.,
Brown S., Mason C.A.;
"Zic2 patterns binocular vision by specifying the uncrossed retinal
projection.";
Cell 114:545-557(2003).
[8]
FUNCTION, AND INTERACTION WITH MDFIC.
PubMed=15207726; DOI=10.1016/j.bbrc.2004.05.158;
Mizugishi K., Hatayama M., Tohmonda T., Ogawa M., Inoue T.,
Mikoshiba K., Aruga J.;
"Myogenic repressor I-mfa interferes with the function of Zic family
proteins.";
Biochem. Biophys. Res. Commun. 320:233-240(2004).
[9]
FUNCTION, INTERACTION WITH MDFIC, SUBCELLULAR LOCATION, AND
DNA-BINDING.
PubMed=15465018; DOI=10.1016/j.bbrc.2004.09.052;
Ishiguro A., Inoue T., Mikoshiba K., Aruga J.;
"Molecular properties of Zic4 and Zic5 proteins: functional diversity
within Zic family.";
Biochem. Biophys. Res. Commun. 324:302-307(2004).
[10]
FUNCTION.
PubMed=18417618; DOI=10.1242/dev.020693;
Garcia-Frigola C., Carreres M.I., Vegar C., Mason C., Herrera E.;
"Zic2 promotes axonal divergence at the optic chiasm midline by EphB1-
dependent and -independent mechanisms.";
Development 135:1833-1841(2008).
[11]
INTERACTION WITH DHX9, PHOSPHORYLATION AT SER-192 AND SER-200,
DNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-192 AND
SER-200.
PubMed=18068128; DOI=10.1016/j.febslet.2007.11.080;
Ishiguro A., Aruga J.;
"Functional role of Zic2 phosphorylation in transcriptional
regulation.";
FEBS Lett. 582:154-158(2008).
[12]
INTERACTION WITH RNF180, AND UBIQUITINATION.
PubMed=18363970; DOI=10.1111/j.1365-2443.2008.01169.x;
Ogawa M., Mizugishi K., Ishiguro A., Koyabu Y., Imai Y., Takahashi R.,
Mikoshiba K., Aruga J.;
"Rines/RNF180, a novel RING finger gene-encoded product, is a
membrane-bound ubiquitin ligase.";
Genes Cells 13:397-409(2008).
[13]
FUNCTION.
PubMed=18524895; DOI=10.1523/JNEUROSCI.0632-08.2008;
Lee R., Petros T.J., Mason C.A.;
"Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2
through inducing expression of the guidance receptor EphB1.";
J. Neurosci. 28:5910-5919(2008).
[14]
FUNCTION, ASSOCIATION WITH DNA, AND DEVELOPMENTAL STAGE.
PubMed=20676059; DOI=10.1038/emboj.2010.172;
Garcia-Frigola C., Herrera E.;
"Zic2 regulates the expression of Sert to modulate eye-specific
refinement at the visual targets.";
EMBO J. 29:3170-3183(2010).
-!- FUNCTION: Acts as a transcriptional activator or repressor. Plays
important roles in the early stage of organogenesis of the CNS.
Activates the transcription of the serotonin transporter SERT in
uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine
eye-specific projections in primary visual targets. Its
transcriptional activity is repressed by MDFIC. Involved in the
formation of the ipsilateral retinal projection at the optic
chiasm midline. Drives the expression of EPHB1 on ipsilaterally
projecting growth cones. Binds to the minimal GLI-consensus
sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter
region from ventrotemporal retinal segments of retinal embryos.
{ECO:0000269|PubMed:10677508, ECO:0000269|PubMed:11053430,
ECO:0000269|PubMed:11756505, ECO:0000269|PubMed:13678579,
ECO:0000269|PubMed:15207726, ECO:0000269|PubMed:15465018,
ECO:0000269|PubMed:18417618, ECO:0000269|PubMed:18524895,
ECO:0000269|PubMed:20676059}.
-!- SUBUNIT: Interacts with RNF180 (PubMed:18363970). Interacts (via
the C2H2-type domains 3, 4 and 5) with MDFIC (via the C2H2-type
domains 3, 4 and 5); the interaction reduces its transcriptional
activity (PubMed:15207726, PubMed:15465018). Interacts (via C2H2-
type domain 3) with DHX9 (PubMed:18068128). Interacts with GLI1
and GLI2 (PubMed:11238441). {ECO:0000250|UniProtKB:O95409,
ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:15207726,
ECO:0000269|PubMed:15465018, ECO:0000269|PubMed:18068128,
ECO:0000269|PubMed:18363970}.
-!- INTERACTION:
P10071:GLI3 (xeno); NbExp=2; IntAct=EBI-308076, EBI-308055;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes in the
cytoplasm in presence of MDFIC overexpression. Both phosphorylated
and unphosphorylated forms are localized in the nucleus.
-!- TISSUE SPECIFICITY: CNS. A high level expression is seen in the
cerebellum.
-!- DEVELOPMENTAL STAGE: Expressed in the ipsilateral retinal ganglion
cells (iRGCs) of the peripheral ventrotemporal (VT) neural retina,
during the outgrowth of the uncrossed retinal projection between
16.5 and 18.5 dpc (at protein level). Expression is down-regulated
as RGCs extend toward chiasmatic midline at the optic chiasm.
{ECO:0000269|PubMed:13678579, ECO:0000269|PubMed:20676059}.
-!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary
for transcription activation.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:18068128}.
-!- PTM: Ubiquitinated by RNF180, leading to its degradation.
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show impaired dorsal forebrain
development and insufficient closure of the posterior neuropore.
Mice survive with holoprosencephaly (HPE) and spina bifida.
{ECO:0000269|PubMed:10677508}.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D70848; BAA11115.2; -; mRNA.
UniGene; Mm.308936; -.
ProteinModelPortal; Q62520; -.
SMR; Q62520; -.
IntAct; Q62520; 4.
MINT; MINT-189917; -.
STRING; 10090.ENSMUSP00000075283; -.
iPTMnet; Q62520; -.
PhosphoSitePlus; Q62520; -.
PaxDb; Q62520; -.
PRIDE; Q62520; -.
MGI; MGI:106679; Zic2.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000232057; -.
HOVERGEN; HBG007135; -.
InParanoid; Q62520; -.
PhylomeDB; Q62520; -.
PRO; PR:Q62520; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ZIC2; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0007417; P:central nervous system development; IGI:MGI.
GO; GO:0044782; P:cilium organization; IMP:MGI.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:1900224; P:positive regulation of nodal signaling pathway involved in determination of lateral mesoderm left/right asymmetry; IMP:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; DNA-binding; Isopeptide bond; Metal-binding;
Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 530 Zinc finger protein ZIC 2.
/FTId=PRO_0000047248.
ZN_FING 256 291 C2H2-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 300 327 C2H2-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 333 357 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 363 387 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 393 415 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 100 255 Necessary for interaction with MDFIC and
transcriptional activation or repression.
COMPBIAS 20 23 Poly-His.
COMPBIAS 25 33 Poly-Ala.
COMPBIAS 89 97 Poly-Ala.
COMPBIAS 227 231 Poly-Ala.
COMPBIAS 232 239 Poly-His.
COMPBIAS 456 470 Poly-Ala.
COMPBIAS 492 506 Poly-Gly.
MOD_RES 192 192 Phosphoserine.
{ECO:0000269|PubMed:18068128}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000269|PubMed:18068128}.
CROSSLNK 253 253 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95409}.
MUTAGEN 192 192 S->A: Still phosphorylated.
{ECO:0000269|PubMed:18068128}.
MUTAGEN 200 200 S->A: Absence of phosphorylation.
Inhibits interaction with DHX9. Does not
affect DNA-binding affinity or
subcellular localization. Inhibits
strongly transcriptional activation.
{ECO:0000269|PubMed:18068128}.
SEQUENCE 530 AA; 54954 MW; BE8B476E81B1E40B CRC64;
MLLDAGPQFP AIGVGSFARH HHHSAAAAAA AAAEMQDREL SLAAAQNGFV DSAAAHMGAF
KLNPGAHELS PGQSSAFTSQ GPGAYPGSAA AAAAAAALGP HAAHVGSYSG PPFNSTRDFL
FRSRGFGDSA PGGGQHGLFG PGAGGLHHAH SDAQGHLLFP GLPPEQHGPH ASQNVLNGQM
RLGLPGEVFG RSEQYRQVAS PRTDPYSAAQ LHNQYGPMNM NMGMNMAAAA AHHHHHHHHP
GAFFRYMRQQ CIKQELICKW IDPEQLSNPK KSCNKTFSTM HELVTHVSVE HVGGPEQSNH
VCFWEECPRE GKPFKAKYKL VNHIRVHTGE KPFPCPFPGC GKVFARSENL KIHKRTHTGE
KPFQCEFEGC DRRFANSSDR KKHMHVHTSD KPYLCKMCDK SYTHPSSLRK HMKVHESSPQ
GSESSPAASS GYESSTPPGL VSPSAEPQSS SNLSPAAAAA AAAAAAAAAA VSAVHRGAGS
GSSGSGGGSA AGSGGGGGGA GGGGGGSSGG GSGTTGGHSG LSSNFNEWYV


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