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SOX2_CHICK
ID   SOX2_CHICK              Reviewed;         315 AA.
AC   P48430; Q54A48;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Transcription factor SOX-2;
DE            Short=cSox2;
DE   AltName: Full=delta EF2a;
GN   Name=SOX2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=7748786; DOI=10.1016/0925-4773(94)00299-3;
RA   Uwanogho D., Rex M., Cartwright E.J., Pearl G., Healy C., Scotting P.J.,
RA   Sharpe P.T.;
RT   "Embryonic expression of the chicken Sox2, Sox3 and Sox11 genes suggests an
RT   interactive role in neuronal development.";
RL   Mech. Dev. 49:23-36(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=White leghorn; TISSUE=Brain;
RX   PubMed=7628452; DOI=10.1002/j.1460-2075.1995.tb07357.x;
RA   Kamachi Y., Sockanathan S., Liu Q., Breitman M., Lovell-Badge R.,
RA   Kondoh H.;
RT   "Involvement of SOX proteins in lens-specific activation of crystallin
RT   genes.";
RL   EMBO J. 14:3510-3519(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=12689590; DOI=10.1016/s1534-5807(03)00088-1;
RA   Uchikawa M., Ishida Y., Takemoto T., Kamachi Y., Kondoh H.;
RT   "Functional analysis of chicken Sox2 enhancers highlights an array of
RT   diverse regulatory elements that are conserved in mammals.";
RL   Dev. Cell 4:509-519(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=14517545; DOI=10.1038/nn1131;
RA   Bylund M., Andersson E., Novitch B.G., Muhr J.;
RT   "Vertebrate neurogenesis is counteracted by Sox1-3 activity.";
RL   Nat. Neurosci. 6:1162-1168(2003).
CC   -!- FUNCTION: Transcriptional activator (PubMed:7628452). Binds to the
CC       consensus DNA sequence 5'-TCATTGTTGTTG-3' (PubMed:7628452). In
CC       cooperation with other transcription factors, binds to the promoter
CC       sequence of the crystallin gene to activate transcription in the lens
CC       (PubMed:7628452). Downstream SRRT target that mediates the promotion of
CC       neural stem cell self-renewal (By similarity). Keeps neural cells
CC       undifferentiated by counteracting the activity of proneural proteins
CC       and suppresses neuronal differentiation (PubMed:14517545). May function
CC       as a switch in neuronal development (PubMed:7748786).
CC       {ECO:0000250|UniProtKB:P48432, ECO:0000269|PubMed:14517545,
CC       ECO:0000269|PubMed:7628452, ECO:0000269|PubMed:7748786}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:7628452}.
CC   -!- TISSUE SPECIFICITY: First expressed in the embryonic neural plate
CC       shortly before closure and expression continues in the neural tube.
CC       From stage 16 onwards, expressed throughout the CNS including the
CC       brain, with expression predominant in the undifferentiated cells of the
CC       neural epithelium. Also expressed at a low level in the retina and the
CC       gut epithelium. Highly expressed in the lens placode at stage 13 and in
CC       the lens at stage 17. {ECO:0000269|PubMed:7628452,
CC       ECO:0000269|PubMed:7748786}.
CC   -!- DEVELOPMENTAL STAGE: Expression is maximal at stages 24-31, then begins
CC       to decline. Expression is low by stage 37 and is absent by stage 39.
CC       Does not appear to be expressed in adults.
CC       {ECO:0000269|PubMed:7748786}.
CC   -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC       number of yeast and animal transcription factors.
CC       {ECO:0000250|UniProtKB:P41225}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA09168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U12532; AAB09662.1; -; mRNA.
DR   EMBL; D50603; BAA09168.1; ALT_INIT; mRNA.
DR   EMBL; AB092842; BAC67545.1; -; Genomic_DNA.
DR   PIR; I50706; I50706.
DR   RefSeq; NP_990519.2; NM_205188.2.
DR   AlphaFoldDB; P48430; -.
DR   BMRB; P48430; -.
DR   SMR; P48430; -.
DR   STRING; 9031.ENSGALP00000014363; -.
DR   PaxDb; P48430; -.
DR   GeneID; 396105; -.
DR   KEGG; gga:396105; -.
DR   CTD; 6657; -.
DR   VEuPathDB; HostDB:geneid_396105; -.
DR   eggNOG; KOG0527; Eukaryota.
DR   HOGENOM; CLU_021123_0_0_1; -.
DR   InParanoid; P48430; -.
DR   OrthoDB; 1161594at2759; -.
DR   PhylomeDB; P48430; -.
DR   TreeFam; TF351735; -.
DR   PRO; PR:P48430; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0030900; P:forebrain development; IBA:GO_Central.
DR   GO; GO:0048839; P:inner ear development; IBA:GO_Central.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:AgBase.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR032643; SOX-2.
DR   InterPro; IPR022097; SOX_fam.
DR   PANTHER; PTHR10270:SF231; PTHR10270:SF231; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12336; SOXp; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..315
FT                   /note="Transcription factor SOX-2"
FT                   /id="PRO_0000048718"
FT   DNA_BIND        39..107
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           270..278
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P41225"
FT   COMPBIAS        10..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   315 AA;  34511 MW;  6EDC91E00F5E9335 CRC64;
     MYNMMETELK PPAPQQTSGG GTGNSNSAAN NQKNSPDRVK RPMNAFMVWS RGQRRKMAQE
     NPKMHNSEIS KRLGAEWKLL SEAEKRPFID EAKRLRALHM KEHPDYKYRP RRKTKTLMKK
     DKYTLPGGLL APGTNTMTTG VGVGATLGAG VNQRMDSYAH MNGWTNGGYG MMQEQLGYPQ
     HPGLNAHNAA QMQPMHRYDV SALQYNSMTS SQTYMNGSPT YSMSYSQQGT PGMALGSMGS
     VVKTESSSSP PVVTSSSHSR APCQAGDLRD MISMYLPGAE VPEPAAPSRL HMSQHYQSAP
     VPGTAINGTL PLSHM
 
 
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