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SOX1_XENLA
ID   SOX1_XENLA              Reviewed;         393 AA.
AC   Q2PG84; A2TED2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Transcription factor Sox-1 {ECO:0000250|UniProtKB:Q6DGL6};
DE            Short=XlSox1 {ECO:0000303|PubMed:17056008};
DE            Short=xSox1 {ECO:0000303|Ref.2};
DE   AltName: Full=SRY (sex determining region Y)-box 1;
GN   Name=sox1 {ECO:0000312|EMBL:BAE72677.1};
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:0000305, ECO:0000312|EMBL:BAE72677.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   TISSUE=Tail bud {ECO:0000269|PubMed:17056008};
RX   PubMed=17056008; DOI=10.1016/j.bbrc.2006.10.040;
RA   Nitta K.R., Takahashi S., Haramoto Y., Fukuda M., Onuma Y., Asashima M.;
RT   "Expression of Sox1 during Xenopus early embryogenesis.";
RL   Biochem. Biophys. Res. Commun. 351:287-293(2006).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:ABS83011.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryonic head {ECO:0000269|Ref.2};
RA   Ma L., Zhao S.-H., Kong Q.-H., Mao B.-Y.;
RT   "Temporal and spatial expression patterns of Sox1 gene in Xenopus laevis
RT   embryo.";
RL   Dong Wu Xue Yan Jiu 28:403-408(2007).
RN   [3] {ECO:0000312|EMBL:ABM92338.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhang C., Grammer T.C., Basta T., Tai P., Espinosa J.M., Klymkowsky M.W.;
RT   "Sox3 acts through multiple regulatory targets to suppress Nodal signaling
RT   during Xenopus germ-layer specification.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:ABM92338.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAI69643.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional activator (By similarity). Participates in
CC       neural induction. {ECO:0000250|UniProtKB:Q6DGL6,
CC       ECO:0000269|PubMed:17056008}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48430,
CC       ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- TISSUE SPECIFICITY: Expressed in the animal hemisphere at early
CC       cleavage stages and in the presumptive ectoderm in the late blastula
CC       embryo. At gastrula stage (stage 10.5), expressed weakly in the
CC       anterior ectoderm distant from the blastopore. At neural plate stages
CC       (stage 13), expression appears in the anterior neural plate. At neural
CC       fold stage (stage 20), strongly expressed in the anterior of the neural
CC       tube. At stages 23 and 25, expression increases in the presumptive
CC       brain and appears in the optic vesicle. At tail bud stages, strongly
CC       expressed in the brain, eye and weakly in the spinal cord. In the tail
CC       bud brain, strongly expressed in the dorsal region. In the eye,
CC       expressed in strong in the dorsal roof of the brain vesicles.
CC       {ECO:0000269|PubMed:17056008, ECO:0000269|Ref.2}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed in unfertilized eggs and at blastula stages. Expression
CC       remains relatively high until late gastrula stage (stage 11) but
CC       becomes weaker at early neurula stages (stages 12 to 15). Expressed
CC       strongly at stages 18, 20 and 30. {ECO:0000269|PubMed:17056008,
CC       ECO:0000269|Ref.2}.
CC   -!- INDUCTION: By bmp-antagonism. {ECO:0000269|PubMed:17056008}.
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: Unlike Ref.2, PubMed:17056008 doesn't detect maternal
CC       expression. {ECO:0000305}.
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DR   EMBL; AB219572; BAE72677.1; -; mRNA.
DR   EMBL; EF672727; ABS83011.1; -; mRNA.
DR   EMBL; EF192051; ABM92338.1; -; mRNA.
DR   EMBL; BC169643; AAI69643.1; -; mRNA.
DR   RefSeq; NP_001089143.1; NM_001095674.1.
DR   AlphaFoldDB; Q2PG84; -.
DR   SMR; Q2PG84; -.
DR   GeneID; 734174; -.
DR   KEGG; xla:734174; -.
DR   CTD; 734174; -.
DR   Xenbase; XB-GENE-1018276; sox1.S.
DR   OrthoDB; 1600890at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 734174; Expressed in brain and 5 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR031268; SOX-1.
DR   InterPro; IPR022097; SOX_fam.
DR   PANTHER; PTHR10270:SF40; PTHR10270:SF40; 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   2: Evidence at transcript level;
KW   Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..393
FT                   /note="Transcription factor Sox-1"
FT                   /id="PRO_0000378063"
FT   DNA_BIND        34..102
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           338..346
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P41225"
FT   COMPBIAS        13..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..234
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        366
FT                   /note="A -> AAA (in Ref. 2; ABM92338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  41059 MW;  920F6D0AE47F96A6 CRC64;
     MYSMMMETDL HSPGVQPPNN TGQGGGNKAS QDRVKRPMNA FMVWSRGQRR KMAQENPKMH
     NSEISKRLGA EWKVMSEAEK RPFIDEAKRL RALHMKEHPD YKYRPRRKTK TLLKKDKYSL
     AGGLLHAAGG GHMGVGLSPG GGGGGCGGAG GMVVQRMESP GSGASTGGYA HMNGWANGAY
     PGSVAAAAAA AMMQEAQLAY SQQQQQHPGS GGHHPHHHPH HPHHHPHHHP HHNPTSHPTP
     PQPMHRYDMS ALQYSPLPGA QTYMSASPSS YGALSYSSSQ QQHQGSPSSA AVAAAAAAAS
     SGALGVLGSL VKSEPSVSPP VSGGGSHNRP PCPGDLREMI SMYLPGGGEA GDPAAAAAAA
     AAAAAATSRL HSLPQHYQGT GTGITSTMPL THI
 
 
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