ZIC5_MOUSE
ID ZIC5_MOUSE Reviewed; 622 AA.
AC Q7TQ40; Q9EQW1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Zinc finger protein ZIC 5;
DE AltName: Full=Odd paired-related protein;
DE Short=Opa-related protein;
DE AltName: Full=Zinc finger protein of the cerebellum 5;
GN Name=Zic5; Synonyms=Opr;
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], AND DEVELOPMENTAL STAGE.
RX PubMed=11044622; DOI=10.1016/s0925-4773(00)00456-1;
RA Furushima K., Murata T., Matsuo I., Aizawa S.;
RT "A new murine zinc finger gene, Opr.";
RL Mech. Dev. 98:161-164(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15136147; DOI=10.1016/j.ydbio.2004.02.017;
RA Inoue T., Hatayama M., Tohmonda T., Itohara S., Aruga J., Mikoshiba K.;
RT "Mouse Zic5 deficiency results in neural tube defects and hypoplasia of
RT cephalic neural crest derivatives.";
RL Dev. Biol. 270:146-162(2004).
RN [3]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=15465018; DOI=10.1016/j.bbrc.2004.09.052;
RA Ishiguro A., Inoue T., Mikoshiba K., Aruga J.;
RT "Molecular properties of Zic4 and Zic5 proteins: functional diversity
RT within Zic family.";
RL Biochem. Biophys. Res. Commun. 324:302-307(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-541, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Essential for neural crest development, converting cells from
CC an epidermal fate to a neural crest cell fate. Binds to DNA.
CC {ECO:0000269|PubMed:15465018}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15465018}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic ectoderm before
CC gastrulation, and gradually restricted to the anterior part from the
CC mid to late streak stage. Becomes restricted to the dorsal side of the
CC neural tube at 8 dpc. After neural tube closure, is expressed in the
CC dorsal midline of the entire neural tube and in the roof plate. Also
CC expressed in the developing limb buds. {ECO:0000269|PubMed:11044622,
CC ECO:0000269|PubMed:15136147}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibited insufficient neural tube closure
CC at the rostral end and malformation of neural-crest-derived facial
CC bones especially the mandible. After birth, mice were significantly
CC smaller than their littermates and most of them died within 2 months.
CC {ECO:0000269|PubMed:15136147}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AB042155; BAB18579.1; -; mRNA.
DR EMBL; AB114214; BAC79075.1; -; mRNA.
DR CCDS; CCDS27348.1; -.
DR RefSeq; NP_075363.1; NM_022987.3.
DR AlphaFoldDB; Q7TQ40; -.
DR SMR; Q7TQ40; -.
DR STRING; 10090.ENSMUSP00000035754; -.
DR iPTMnet; Q7TQ40; -.
DR PhosphoSitePlus; Q7TQ40; -.
DR PaxDb; Q7TQ40; -.
DR PRIDE; Q7TQ40; -.
DR ProteomicsDB; 275065; -.
DR DNASU; 65100; -.
DR GeneID; 65100; -.
DR KEGG; mmu:65100; -.
DR UCSC; uc007vbb.2; mouse.
DR CTD; 85416; -.
DR MGI; MGI:1929518; Zic5.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q7TQ40; -.
DR OrthoDB; 592023at2759; -.
DR PhylomeDB; Q7TQ40; -.
DR TreeFam; TF351425; -.
DR BioGRID-ORCS; 65100; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q7TQ40; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TQ40; protein.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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; IBA:GO_Central.
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:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0014033; P:neural crest cell differentiation; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR041643; Znf_ZIC.
DR Pfam; PF00096; zf-C2H2; 2.
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 Developmental protein; Differentiation; DNA-binding; Metal-binding;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..622
FT /note="Zinc finger protein ZIC 5"
FT /id="PRO_0000406213"
FT ZN_FING 422..444
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 450..474
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 480..504
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 510..534
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 50..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96T25"
FT CONFLICT 92
FT /note="F -> S (in Ref. 1; BAB18579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 64542 MW; E9D2B5D27DCAF640 CRC64;
MMEPPLSKRN PPALRLADLA TAQAQQLQNM TGFPVLVGPP AHSQRRAVAM HLHPRDLGTD
PGVASTALGP EHMAQASGQG PCPPSQGLPG LFQVPAPAAR SVASGTHPGA RTHPDGGGSS
GAQASAPPPP APPLPPSQSS SPPPPPPPPP ALSGYTATNS GGGSSSGKGH SRDFVLRRDL
SATAPAAAMH GAPLGGEQRS GSSSPQHPTP PPHPAGMFIS ASGTYAGRDG GGSALFPALH
DSPGAPGGHP LNGQMRLGLA AAAAAAAELY GRAEPPFAPR SGDAHYGAVA AAAAAALHGY
GAVNLNLNLA AAAAAAAAAG PGPHLQHHAP PPAPPPAPAP HPHHPHLPGA AGAFLRYMRQ
PIKRELICKW LDPEELAGPP ASADSGVKPC SKTFGTMHEL VNHVTVEHVG GPEQSSHVCF
WEDCPREGKP FKAKYKLINH IRVHTGEKPF PCPFPGCGKV FARSENLKIH KRTHTGEKPF
KCEFDGCDRK FANSSDRKKH SHVHTSDKPY YCKIRGCDKS YTHPSSLRKH MKIHCKSPPP
SPGALGYSSV GTPVGDPLSP VLDPTRSRSS TLSPQVTNLN EWYVCQASGA PSHLHTPSSN
GTTSESEDEE MYGNPEVMRT IH
