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ID3B_XENLA
ID   ID3B_XENLA              Reviewed;         118 AA.
AC   Q7SZ28; Q91418;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=DNA-binding protein inhibitor ID-3-B;
DE   AltName: Full=Inhibitor of DNA binding 3-B;
DE            Short=XIdIIa {ECO:0000312|EMBL:AAD14295.1};
DE   AltName: Full=Inhibitor of differentiation 3-B;
GN   Name=id3-b; Synonyms=id3;
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] {ECO:0000312|EMBL:AAH54166.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAH54166.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAD14295.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-118.
RC   TISSUE=Neurula {ECO:0000269|PubMed:7619724};
RX   PubMed=7619724; DOI=10.1016/0925-4773(94)00329-l;
RA   Zhang H., Reynaud S., Kloc M., Etkin L.D., Spohr G.;
RT   "Id gene activity during Xenopus embryogenesis.";
RL   Mech. Dev. 50:119-130(1995).
CC   -!- FUNCTION: Transcriptional regulator (lacking a basic DNA binding
CC       domain) which negatively regulates the basic helix-loop-helix (bHLH)
CC       transcription factors by forming heterodimers and inhibiting their DNA
CC       binding and transcriptional activity. Influences cell fate decisions in
CC       the embryo by sequestering and blocking the activity of the bHLH
CC       transcription factors that control these decisions. Inhibits the
CC       binding of myogenic bHLH-containing complexes to E-box DNA, thereby
CC       preventing activation of muscle-specific target genes. Also inhibits
CC       the activity of neurogenic factor neurod1/neuroD. Plays a role in cell
CC       cycle progression and survival of neural crest progenitors; binding to
CC       either hes4-B/hairy2b or stat3 blocks the formation of transcription
CC       factor complexes and the repressor function of hes4-B/hairy2B, to allow
CC       neural crest progenitors to differentiate. May play a role in the
CC       regulation of the circadian rhythm (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer (By similarity). Heterodimer with other HLH
CC       proteins. Interacts (via HLH domain) with the bHLH protein hes4/hairy2
CC       (via Orange domain). Interacts with stat3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q91399}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02535,
CC       ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR   EMBL; BC054166; AAH54166.1; -; mRNA.
DR   EMBL; S79040; AAD14295.1; -; mRNA.
DR   PIR; I51318; I51318.
DR   RefSeq; NP_001079757.1; NM_001086288.1.
DR   AlphaFoldDB; Q7SZ28; -.
DR   SMR; Q7SZ28; -.
DR   DNASU; 379447; -.
DR   GeneID; 379447; -.
DR   KEGG; xla:379447; -.
DR   CTD; 379447; -.
DR   Xenbase; XB-GENE-866418; id3.S.
DR   OMA; GDARVCH; -.
DR   OrthoDB; 1624054at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 379447; Expressed in gastrula and 18 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; PTHR11723; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   3: Inferred from homology;
KW   Biological rhythms; Developmental protein; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..118
FT                   /note="DNA-binding protein inhibitor ID-3-B"
FT                   /id="PRO_0000390725"
FT   DOMAIN          32..84
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   CONFLICT        66
FT                   /note="S -> A (in Ref. 2; AAD14295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="E -> S (in Ref. 2; AAD14295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="L -> R (in Ref. 2; AAD14295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="D -> Y (in Ref. 2; AAD14295)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   118 AA;  12886 MW;  99B102ACB2E63D54 CRC64;
     MKAISPVRSM SSCYQAVCCL SEQSLSIARG SSLKGAGIDE TMGLLYDMNG CYSKLKELVP
     GIPQGSKLSQ VEILQHVIDY IFDLQIVLGE DQQQNSILNL QKSDFSELAT QGDARVCH
 
 
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