ID SOX10_MOUSE Reviewed; 466 AA. AC Q04888; O08518; O09141; O54856; P70416; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 27-MAR-2024, entry version 196. DE RecName: Full=Transcription factor SOX-10; DE AltName: Full=Protein SOX-21; DE AltName: Full=Transcription factor SOX-M; GN Name=Sox10; Synonyms=Sox-10, Sox21; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE. RC STRAIN=C57BL/6J; RX PubMed=9425902; DOI=10.1038/ng0198-60; RA Southard-Smith E.M., Kos L., Pavan W.J.; RT "Sox10 mutation disrupts neural crest development in Dom Hirschsprung mouse RT model."; RL Nat. Genet. 18:60-64(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. RC STRAIN=C57BL/6J; RX PubMed=9560246; DOI=10.1073/pnas.95.9.5161; RA Herbarth B., Pingault V., Bondurand N., Kuhlbrodt K., Hermans-Borgmeyer I., RA Puliti A., Lemort N., Goossens M., Wegner M.; RT "Mutation of the Sry-related Sox10 gene in Dominant megacolon, a mouse RT model for human Hirschsprung disease."; RL Proc. Natl. Acad. Sci. U.S.A. 95:5161-5165(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9760192; DOI=10.1007/s004390050793; RA Pusch C., Hustert E., Pfeifer D., Sudbeck P., Kist R., Roe B., Wang Z., RA Balling R., Blin N., Scherer G.; RT "The SOX10/Sox10 gene from human and mouse: sequence, expression, and RT transactivation by the encoded HMG domain transcription factor."; RL Hum. Genet. 103:115-123(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/HeN; RX PubMed=9027483; DOI=10.1006/geno.1996.4483; RA Tani M., Shindo-Okada N., Hashimoto Y., Shiroishi T., Takenoshita S., RA Nagamachi Y., Yokota J.; RT "Isolation of a novel Sry-related gene that is expressed in high-metastatic RT K-1735 murine melanoma cells."; RL Genomics 39:30-37(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Salivary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-167. RX PubMed=8441686; DOI=10.1093/nar/21.3.744; RA Wright E.M., Snopek B., Koopman P.; RT "Seven new members of the Sox gene family expressed during mouse RT development."; RL Nucleic Acids Res. 21:744-744(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 114-167. RC STRAIN=Swiss Webster; TISSUE=Embryonic tooth; RX PubMed=8921394; DOI=10.1006/geno.1996.0548; RA Stock D.W., Buchanan A.V., Zhao Z., Weiss K.M.; RT "Numerous members of the Sox family of HMG box-containing genes are RT expressed in developing mouse teeth."; RL Genomics 37:234-237(1996). RN [8] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ARMCX3. RX PubMed=19304657; DOI=10.1074/jbc.m901177200; RA Mou Z., Tapper A.R., Gardner P.D.; RT "The armadillo repeat-containing protein, ARMCX3, physically and RT functionally interacts with the developmental regulatory factor Sox10."; RL J. Biol. Chem. 284:13629-13640(2009). RN [9] RP FUNCTION. RX PubMed=24204311; DOI=10.1371/journal.pgen.1003907; RA Hornig J., Froeb F., Vogl M.R., Hermans-Borgmeyer I., Tamm E.R., Wegner M.; RT "The transcription factors Sox10 and Myrf define an essential regulatory RT network module in differentiating oligodendrocytes."; RL PLoS Genet. 9:E1003907-E1003907(2013). RN [10] RP FUNCTION, AND SUBUNIT. RX PubMed=27532821; DOI=10.1002/glia.23044; RA Muth K.N., Piefke S., Weider M., Sock E., Hermans-Borgmeyer I., Wegner M., RA Kuespert M.; RT "The dual-specificity phosphatase Dusp15 is regulated by Sox10 and Myrf in RT myelinating oligodendrocytes."; RL Glia 64:2120-2132(2016). RN [11] RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=26525805; DOI=10.1111/jnc.13414; RA Baroti T., Schillinger A., Wegner M., Stolt C.C.; RT "Sox13 functionally complements the related Sox5 and Sox6 as important RT developmental modulators in mouse spinal cord oligodendrocytes."; RL J. Neurochem. 136:316-328(2016). CC -!- FUNCTION: Transcription factor that plays a central role in developing CC and mature glia (PubMed:24204311, PubMed:27532821). Specifically CC activates expression of myelin genes, during oligodendrocyte (OL) CC maturation, such as DUSP15 and MYRF, thereby playing a central role in CC oligodendrocyte maturation and CNS myelination (PubMed:24204311, CC PubMed:27532821). Once induced, MYRF cooperates with SOX10 to implement CC the myelination program (PubMed:24204311). Transcriptional activator of CC MITF, acting synergistically with PAX3 (By similarity). Transcriptional CC activator of MBP, via binding to the gene promoter (By similarity). CC {ECO:0000250|UniProtKB:O55170, ECO:0000250|UniProtKB:P56693, CC ECO:0000269|PubMed:24204311, ECO:0000269|PubMed:27532821}. CC -!- SUBUNIT: Monomer (PubMed:27532821). Interacts with Armcx3 at the CC mitochondrial outer membrane surface (PubMed:19304657). Interacts with CC PAX3 (By similarity). {ECO:0000250|UniProtKB:P56693, CC ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:27532821}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19304657}. Nucleus CC {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:9560246}. CC Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic CC side {ECO:0000269|PubMed:19304657}. CC -!- TISSUE SPECIFICITY: Expressed in oligodendroglia of the spinal tube (at CC protein level). {ECO:0000269|PubMed:26525805}. CC -!- DEVELOPMENTAL STAGE: Expressed in the motor neuron progenitor domain of CC the spinal tube from 11.5 dpc to postnatal day 6. CC {ECO:0000269|PubMed:26525805}. 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 -!- DISRUPTION PHENOTYPE: Defects in Sox10 are the cause of the mouse CC mutant dominant megacolon (dom). While dom/+ heterozygous mice display CC regional deficiencies of neural crest-derived enteric ganglia in the CC distal colon, dom/dom homozygous animals are embryonic lethal. CC {ECO:0000269|PubMed:9425902, ECO:0000269|PubMed:9560246}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB49282.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAB99738.1; Type=Erroneous initiation; Evidence={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; AF017182; AAB99738.1; ALT_INIT; mRNA. DR EMBL; AF047043; AAC24564.1; -; mRNA. DR EMBL; U66141; AAB49282.1; ALT_FRAME; mRNA. DR EMBL; BC018551; AAH18551.1; -; mRNA. DR EMBL; BC023356; AAH23356.1; -; mRNA. DR EMBL; BC025171; AAH25171.1; -; mRNA. DR EMBL; Z18959; CAA79484.1; -; mRNA. DR EMBL; U70441; AAC52859.1; -; mRNA. DR CCDS; CCDS49668.1; -. DR PIR; S30242; S30242. DR RefSeq; NP_035567.1; NM_011437.1. DR AlphaFoldDB; Q04888; -. DR SMR; Q04888; -. DR BioGRID; 203397; 2. DR STRING; 10090.ENSMUSP00000155574; -. DR iPTMnet; Q04888; -. DR PhosphoSitePlus; Q04888; -. DR MaxQB; Q04888; -. DR PaxDb; 10090-ENSMUSP00000039466; -. DR PeptideAtlas; Q04888; -. DR ProteomicsDB; 257378; -. DR Antibodypedia; 3774; 1203 antibodies from 48 providers. DR Ensembl; ENSMUST00000040019.5; ENSMUSP00000039466.5; ENSMUSG00000033006.11. DR Ensembl; ENSMUST00000230532.2; ENSMUSP00000155574.2; ENSMUSG00000033006.11. DR GeneID; 20665; -. DR KEGG; mmu:20665; -. DR UCSC; uc007wsu.2; mouse. DR AGR; MGI:98358; -. DR MGI; MGI:98358; Sox10. DR VEuPathDB; HostDB:ENSMUSG00000033006; -. DR eggNOG; KOG0527; Eukaryota. DR GeneTree; ENSGT00940000158046; -. DR HOGENOM; CLU_031800_0_0_1; -. DR InParanoid; Q04888; -. DR OMA; ATIQAHY; -. DR OrthoDB; 2902801at2759; -. DR PhylomeDB; Q04888; -. DR BioGRID-ORCS; 20665; 7 hits in 77 CRISPR screens. DR ChiTaRS; Sox10; mouse. DR PRO; PR:Q04888; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q04888; Protein. DR Bgee; ENSMUSG00000033006; Expressed in vestibular membrane of cochlear duct and 223 other cell types or tissues. DR ExpressionAtlas; Q04888; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISS:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI. DR GO; GO:0030154; P:cell differentiation; IMP:MGI. DR GO; GO:0048469; P:cell maturation; IMP:MGI. DR GO; GO:0071393; P:cellular response to progesterone stimulus; IEA:Ensembl. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB. DR GO; GO:0048589; P:developmental growth; IMP:MGI. DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI. DR GO; GO:0048484; P:enteric nervous system development; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0032808; P:lacrimal gland development; IMP:MGI. DR GO; GO:0030318; P:melanocyte differentiation; IMP:MGI. DR GO; GO:0061138; P:morphogenesis of a branching epithelium; IMP:MGI. DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB. DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:UniProtKB. DR GO; GO:0007422; P:peripheral nervous system development; IGI:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0014015; P:positive regulation of gliogenesis; IMP:UniProtKB. DR GO; GO:0031643; P:positive regulation of myelination; ISO:MGI. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; ISO:MGI. 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. DR Genevisible; Q04888; MM. PE 1: Evidence at protein level; KW Activator; Cytoplasm; DNA-binding; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..466 FT /note="Transcription factor SOX-10" FT /id="PRO_0000048747" FT DNA_BIND 104..172 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 62..102 FT /note="Dimerization (DIM)" FT /evidence="ECO:0000250|UniProtKB:P56693" FT REGION 160..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 213..275 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 228..310 FT /note="Transactivation domain (TAM)" FT /evidence="ECO:0000250|UniProtKB:P56693" FT REGION 344..375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 353..466 FT /note="Transactivation domain (TAC)" FT /evidence="ECO:0000250|UniProtKB:P56693" FT REGION 433..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..67 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..184 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..266 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..375 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..466 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P56693" FT VARIANT 11 FT /note="E -> V" FT CONFLICT 41 FT /note="G -> V (in Ref. 4; AAB49282)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="R -> P (in Ref. 6; CAA79484)" FT /evidence="ECO:0000305" FT CONFLICT 357 FT /note="K -> E (in Ref. 4; AAB49282)" FT /evidence="ECO:0000305" SQ SEQUENCE 466 AA; 49949 MW; 84862547F039E71F CRC64; MAEEQDLSEV ELSPVGSEEP RCLSPGSAPS LGPDGGGGGS GLRASPGPGE LGKVKKEQQD GEADDDKFPV CIREAVSQVL SGYDWTLVPM PVRVNGASKS KPHVKRPMNA FMVWAQAARR KLADQYPHLH NAELSKTLGK LWRLLNESDK RPFIEEAERL RMQHKKDHPD YKYQPRRRKN GKAAQGEAEC PGGEAEQGGA AAIQAHYKSA HLDHRHPEEG SPMSDGNPEH PSGQSHGPPT PPTTPKTELQ SGKADPKRDG RSLGEGGKPH IDFGNVDIGE ISHEVMSNME TFDVTELDQY LPPNGHPGHV GSYSAAGYGL GSALAVASGH SAWISKPPGV ALPTVSPPGV DAKAQVKTET TGPQGPPHYT DQPSTSQIAY TSLSLPHYGS AFPSISRPQF DYSDHQPSGP YYGHAGQASG LYSAFSYMGP SQRPLYTAIS DPSPSGPQSH SPTHWEQPVY TTLSRP //