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ZIC2A_XENLA
ID   ZIC2A_XENLA             Reviewed;         503 AA.
AC   Q91689; O93487; Q641A3;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Zinc finger protein ZIC 2-A;
DE   AltName: Full=Zinc finger DNA-binding protein fZic;
DE   AltName: Full=Zinc finger protein ZIC 2;
DE            Short=XlZic2;
DE            Short=xZic2;
DE   AltName: Full=Zinc finger protein of the cerebellum 2-A;
GN   Name=zic2-a; Synonyms=zic2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=9739105; DOI=10.1016/s0925-4773(98)00073-2;
RA   Nakata K., Nagai T., Aruga J., Mikoshiba K.;
RT   "Xenopus Zic family and its role in neural and neural crest development.";
RL   Mech. Dev. 75:43-51(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Neurula;
RX   PubMed=9634234; DOI=10.1038/31242;
RA   Brewster R., Lee J., Ruiz i Altaba A.;
RT   "Gli/Zic factors pattern the neural plate by defining domains of cell
RT   differentiation.";
RL   Nature 393:579-583(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 226-302, FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=16207750; DOI=10.1242/dev.02066;
RA   Houston D.W., Wylie C.;
RT   "Maternal Xenopus Zic2 negatively regulates Nodal-related gene expression
RT   during anteroposterior patterning.";
RL   Development 132:4845-4855(2005).
RN   [5]
RP   INDUCTION.
RX   PubMed=11091076; DOI=10.1016/s0925-4773(00)00480-9;
RA   Nakata K., Koyabu Y., Aruga J., Mikoshiba K.;
RT   "A novel member of the Xenopus Zic family, Zic5, mediates neural crest
RT   development.";
RL   Mech. Dev. 99:83-91(2000).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16871625; DOI=10.1002/dvdy.20906;
RA   Fujimi T.J., Mikoshiba K., Aruga J.;
RT   "Xenopus Zic4: conservation and diversification of expression profiles and
RT   protein function among the Xenopus Zic family.";
RL   Dev. Dyn. 235:3379-3386(2006).
CC   -!- FUNCTION: Transcriptional repressor that inhibits neurogenesis and
CC       induces neural and neural crest differentiation. Regulates
CC       anteroposterior patterning in early development by inhibiting
CC       expression of the nodal genes through the inhibition of vegt. Required
CC       for gastrulation movements and for proper anterior neural and axial
CC       development. May also act as a transcriptional activator. May bind to
CC       the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'.
CC       {ECO:0000269|PubMed:16207750, ECO:0000269|PubMed:9634234,
CC       ECO:0000269|PubMed:9739105}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9634234}. Cytoplasm
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in both animal and vegetal regions of the
CC       oocyte. At blastula and gastrula stages (stages 9 to 10.5), expressed
CC       throughout the ectoderm. During late gastrula to neurula stages,
CC       expression gradually diminishes in the midline region of the neural
CC       plate and increases in the anterior neural folds, and continues to be
CC       expressed in the posterior medial part of the neural plate. In early
CC       tailbud stages (stages 22-23), expressed in the dorsal forebrain,
CC       midbrain and hindbrain. Subsequently expressed in the telencephalon and
CC       diencephalon/mesencephalon boundary. In the spinal cord, expression is
CC       restricted to the dorsal most region including the roof plate. Also
CC       expressed in the somites and eye vesicles. In the eye, expression is
CC       restricted to the ciliary marginal zone of neural retina and is absent
CC       from the lens. {ECO:0000269|PubMed:16207750,
CC       ECO:0000269|PubMed:16871625, ECO:0000269|PubMed:9634234,
CC       ECO:0000269|PubMed:9739105}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Continuously expressed from the egg to the tailbud stage (stage 30)
CC       with an increase in expression at the early gastrula stage (stage 10).
CC       {ECO:0000269|PubMed:16207750, ECO:0000269|PubMed:16871625,
CC       ECO:0000269|PubMed:9739105}.
CC   -!- INDUCTION: By zic1, zic2, zic3 and zic5. {ECO:0000269|PubMed:11091076}.
CC   -!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary for
CC       transcription activation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AB009565; BAA33407.1; -; mRNA.
DR   EMBL; U57453; AAC80229.1; -; mRNA.
DR   EMBL; BC082436; AAH82436.1; -; mRNA.
DR   RefSeq; NP_001081193.1; NM_001087724.1.
DR   AlphaFoldDB; Q91689; -.
DR   SMR; Q91689; -.
DR   MaxQB; Q91689; -.
DR   DNASU; 397704; -.
DR   GeneID; 397704; -.
DR   KEGG; xla:397704; -.
DR   CTD; 397704; -.
DR   Xenbase; XB-GENE-482658; zic2.L.
DR   OrthoDB; 768287at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397704; Expressed in blastula and 10 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0014034; P:neural crest cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; ISS: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   2: Evidence at transcript level;
KW   Activator; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW   Gastrulation; Metal-binding; Neurogenesis; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..503
FT                   /note="Zinc finger protein ZIC 2-A"
FT                   /id="PRO_0000047249"
FT   ZN_FING         277..312
FT                   /note="C2H2-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         321..348
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         354..378
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         384..408
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         414..436
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          61..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        20..21
FT                   /note="Missing (in Ref. 1; BAA33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32..33
FT                   /note="Missing (in Ref. 3; AAH82436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="A -> G (in Ref. 1; BAA33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..76
FT                   /note="Missing (in Ref. 2; AAC80229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        422
FT                   /note="S -> T (in Ref. 1; BAA33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        438
FT                   /note="S -> T (in Ref. 1; BAA33407)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  53941 MW;  3F173F6648C8E806 CRC64;
     MLLDAGPQFP ALGVGTFARH HHHHHHHHAA VAAAAAAAAE MQERELSLAQ NTFVEPTHMA
     AFKLNPGGGS GGGSGGGGGG GGAGPNGGAG ASGPHDLSPP GQTSAFTSQA GYPTSALAPH
     SAYSGAAAFN SPRDFLFRGR GFAEGSAAAG GGQHGLFGPP AGSLHHHPHH HHQLSHAEHP
     QGHLLFPGIH DQHAAASQNT LGGQMRLGLP GEVFGRTEQY RQVSSPRGDP YTAAQLHNQY
     SPMNMGMNMA AHHHHHHHHH PGAFFRYMRQ PCIKQELICK WIDPEQLNNP KKSCTKTFST
     MHELVTHVSV EHVGGPEQSN HICFWEECPR EGKPFKAKYK LVNHIRVHTG EKPFPCPFPG
     CGKVFARSEN LKIHKRTHTG EKPFQCEFEG CDRRFANSSD RKKHMHVHTS DKPYLCKMCD
     KSYTHPSSLR KHMKVHESSP QGSESSPAAS SGYESSTPPG LVSPNSETQN PNLSPAAAAV
     SAVHNVSSGA SGALASNFNE WYV
 
 
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