ID SOX10_XENLA Reviewed; 446 AA.
AC Q8AXX8; B7ZR69;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Transcription factor Sox-10 {ECO:0000312|EMBL:AAN62483.1};
DE AltName: Full=SRY (sex determining region Y)-box 10;
GN Name=sox10;
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:AAN62483.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Neurula {ECO:0000269|PubMed:12812785};
RX PubMed=12812785; DOI=10.1016/s0012-1606(03)00161-1;
RA Aoki Y., Saint-Germain N., Gyda M., Magner-Fink E., Lee Y.-H., Credidio C.,
RA Saint-Jeannet J.-P.;
RT "Sox10 regulates the development of neural crest-derived melanocytes in
RT Xenopus.";
RL Dev. Biol. 259:19-33(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO13216.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Tail bud {ECO:0000269|PubMed:12885557};
RX PubMed=12885557; DOI=10.1016/s0012-1606(03)00247-1;
RA Honore S.M., Aybar M.J., Mayor R.;
RT "Sox10 is required for the early development of the prospective neural
RT crest in Xenopus embryos.";
RL Dev. Biol. 260:79-96(2003).
RN [3] {ECO:0000312|EMBL:AAI70062.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI70062.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UBE2I AND SMO1, SUMOYLATION AT LYS-52 AND
RP LYS-341, AND MUTAGENESIS OF LYS-52 AND LYS-341.
RX PubMed=16256735; DOI=10.1016/j.devcel.2005.09.016;
RA Taylor K.M., Labonne C.;
RT "SoxE factors function equivalently during neural crest and inner ear
RT development and their activity is regulated by SUMOylation.";
RL Dev. Cell 9:593-603(2005).
RN [5] {ECO:0000305}
RP INDUCTION.
RX PubMed=16943273; DOI=10.1242/dev.02558;
RA O'Donnell M., Hong C.-S., Huang X., Delnicki R.J., Saint-Jeannet J.-P.;
RT "Functional analysis of Sox8 during neural crest development in Xenopus.";
RL Development 133:3817-3826(2006).
CC -!- FUNCTION: Acts early in neural crest formation, functioning redundantly
CC with the other group E Sox factors sox8 and sox9 to induce neural crest
CC progenitors. Acts downstream of wnt-signaling at the neural plate
CC border. Involved in the specification of neural crest progenitors fated
CC to form the pigment cell lineage. {ECO:0000269|PubMed:12812785,
CC ECO:0000269|PubMed:12885557, ECO:0000269|PubMed:16256735}.
CC -!- SUBUNIT: Interacts with the sumoylation factors ube2i/ubc9 and sumo1.
CC {ECO:0000269|PubMed:16256735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P56693}. Nucleus
CC {ECO:0000250|UniProtKB:P56693}.
CC -!- TISSUE SPECIFICITY: First expressed at stages 13/14 at the lateral
CC edges of the neural plate, in the neural crest forming region. By stage
CC 22, neural crest cells migrate in the cranial region and strong
CC expression is seen in the crest cells that populate the branchial
CC arches as well as those migrating in the frontonasal region. Also
CC strongly expressed in the trunk neural crest. Expression in the otic
CC vesicle begins around stage 25 and persists until at least stage 40. At
CC stage 30, expression is down-regulated in the cranial neural crest of
CC the pharyngeal arches but persists in the trunk neural crest, in the
CC otic vesicle and in discrete domains adjacent to the hindbrain. At
CC stage 40, expression is restricted to the otic vesicle, differentiated
CC pigment cells, and in several cranial ganglia.
CC {ECO:0000269|PubMed:12812785, ECO:0000269|PubMed:12885557}.
CC -!- INDUCTION: By sox8, sox9 and snai1/snail, wnt-signaling and fgf-
CC signaling in the neural crest-forming region.
CC {ECO:0000269|PubMed:12812785, ECO:0000269|PubMed:12885557,
CC ECO:0000269|PubMed:16943273}.
CC -!- DOMAIN: The transactivation domains TAM and TAC (for transactivation
CC domain in the middle and at the C-terminus, respectively) are required
CC to contact transcriptional coactivators and basal transcriptional
CC machinery components and thereby induce gene transactivation.
CC {ECO:0000250|UniProtKB:P48436}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:16256735}.
CC -!- DISRUPTION PHENOTYPE: Loss of neural crest precursors. Also an increase
CC in apoptosis and a decrease in cell proliferation in the neural fold.
CC {ECO:0000269|PubMed:12885557}.
CC -!- CAUTION: Although PubMed:12812785 report induction by snai2/slug,
CC PubMed:12885557 report that sox10 lies in between snai1/snail and
CC snai2/slug in the complex sequence of inductive events required for
CC neural crest formation. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY149116; AAN62483.1; -; mRNA.
DR EMBL; AY157667; AAO13216.1; -; mRNA.
DR EMBL; BC170062; AAI70062.1; -; mRNA.
DR RefSeq; NP_001082358.1; NM_001088889.1.
DR RefSeq; XP_018112033.1; XM_018256544.1.
DR AlphaFoldDB; Q8AXX8; -.
DR SMR; Q8AXX8; -.
DR GeneID; 398422; -.
DR KEGG; xla:398422; -.
DR AGR; Xenbase:XB-GENE-865362; -.
DR CTD; 398422; -.
DR Xenbase; XB-GENE-865362; sox10.L.
DR OMA; HYKGTHL; -.
DR OrthoDB; 2902801at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 398422; Expressed in internal ear and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; 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:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd22031; HMG-box_SoxE; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR022151; Sox_N.
DR PANTHER; PTHR45803; SOX100B; 1.
DR PANTHER; PTHR45803:SF6; TRANSCRIPTION FACTOR SOX-10; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12444; Sox_N; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..446
FT /note="Transcription factor Sox-10"
FT /id="PRO_0000376861"
FT DNA_BIND 98..166
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..96
FT /note="Dimerization (DIM)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 153..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..303
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 337..446
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 421..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:16256735"
FT CROSSLNK 341
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:16256735"
FT MUTAGEN 52
FT /note="K->R: Eliminates one of two sumoylated products.
FT Abolishes interaction with sumoylation factors."
FT /evidence="ECO:0000269|PubMed:16256735"
FT MUTAGEN 341
FT /note="K->R: Eliminates one of two sumoylated products."
FT /evidence="ECO:0000269|PubMed:16256735"
FT CONFLICT 36
FT /note="D -> DDD (in Ref. 3; AAI70062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49098 MW; B7F13C68F2854443 CRC64;
MSDDQSLSEV EMSPVGSEDP SLTPDPLPPH AHSSPDDDDD DDEEEEEETK VKKEQDSEDE
RFPVCIREAV SQVLNGYDWT LVPMPVRVNG GSKSKPHVKR PMNAFMVWAQ AARRKLADQY
PHLHNAELSK TLGKLWRLLN ENDKRPFIEE AERLRMQHKK DHPDYKYQPR RRKNGKPSPG
EGDGSSEAEG GAASIQAHYK NSHLDHRHGS PMSDGNSEHS TGQSHGPPTP PTTPKTELQA
GKSDGKRDGS HALREGGKPQ IDFGNVDIGE ISHDVMSNME TFDVNEFDQY LPPNGHAGHP
SHIGGYTSSY GLTGALAAGP SAWALAKQHS QTVADSKAQV KTESSSTSHY TEQPSTSQLT
YTSLGLPHYG SAFPSISRPQ FDYADHQPSS SYYSHSAQAS SLYSAFSYMG PPQRPLYTAI
SDPPSVAQSH SPTHWEQPVY TTLSRP
//
