SOX10_PIG
ID SOX10_PIG Reviewed; 469 AA.
AC A5A763;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Transcription factor SOX-10;
GN Name=SOX10;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okumura N., Matsumoto T., Hamasima N., Uenishi H., Ogawa T., Komatsuda A.,
RA Fukudome N., Ide H., Suzuki A., Kojima C., Awata T.;
RT "Sequences and genetic variations of forty-four porcine coat color related
RT genes.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that plays a central role in developing
CC and mature glia (By similarity). Specifically activates expression of
CC myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15
CC and MYRF, thereby playing a central role in oligodendrocyte maturation
CC and CNS myelination (By similarity). Once induced, MYRF cooperates with
CC SOX10 to implement the myelination program (By similarity).
CC Transcriptional activator of MITF, acting synergistically with PAX3 (By
CC similarity). Transcriptional activator of MBP, via binding to the gene
CC promoter (By similarity). {ECO:0000250|UniProtKB:O55170,
CC ECO:0000250|UniProtKB:P56693, ECO:0000250|UniProtKB:Q04888}.
CC -!- SUBUNIT: Monomer. Interacts with ARMCX3 at the mitochondrial outer
CC membrane surface. Interacts with PAX3 (By similarity).
CC {ECO:0000250|UniProtKB:P56693, ECO:0000250|UniProtKB:Q04888}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q04888}. Nucleus
CC {ECO:0000250|UniProtKB:Q04888}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q04888}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q04888}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q04888}.
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}.
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DR EMBL; AB271933; BAF62308.1; -; mRNA.
DR RefSeq; NP_001093403.1; NM_001099933.1.
DR AlphaFoldDB; A5A763; -.
DR SMR; A5A763; -.
DR STRING; 9823.ENSSSCP00000000119; -.
DR PaxDb; A5A763; -.
DR Ensembl; ENSSSCT00025040171; ENSSSCP00025017094; ENSSSCG00025029557.
DR Ensembl; ENSSSCT00030004996; ENSSSCP00030001992; ENSSSCG00030003836.
DR Ensembl; ENSSSCT00035012680; ENSSSCP00035004282; ENSSSCG00035010141.
DR Ensembl; ENSSSCT00045001176; ENSSSCP00045000656; ENSSSCG00045000796.
DR Ensembl; ENSSSCT00050090075; ENSSSCP00050038684; ENSSSCG00050066118.
DR Ensembl; ENSSSCT00055032672; ENSSSCP00055026025; ENSSSCG00055016514.
DR Ensembl; ENSSSCT00060046278; ENSSSCP00060019813; ENSSSCG00060034119.
DR Ensembl; ENSSSCT00065040966; ENSSSCP00065017359; ENSSSCG00065030336.
DR Ensembl; ENSSSCT00070049730; ENSSSCP00070041986; ENSSSCG00070024810.
DR GeneID; 414903; -.
DR KEGG; ssc:414903; -.
DR CTD; 6663; -.
DR eggNOG; KOG0527; Eukaryota.
DR InParanoid; A5A763; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 5.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR GO; GO:0048484; P:enteric nervous system development; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR022151; Sox_N.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12444; Sox_N; 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; Cytoplasm; DNA-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..469
FT /note="Transcription factor SOX-10"
FT /id="PRO_0000296389"
FT DNA_BIND 107..175
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..105
FT /note="Dimerization (DIM)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 163..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..313
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 356..469
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000250|UniProtKB:P56693"
FT REGION 357..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56693"
SQ SEQUENCE 469 AA; 50044 MW; 2AD509205EB57DEE CRC64;
MAEEQDLSEV ELSPVGSEEP RCLSPGSAPS LGPDGGGGGG GGSGLRASPG PGELGKVKKE
QQDGEADDDK FPVCIREAVS QVLSGYDWTL VPMPVRVNGA SKSKPHVKRP MNAFMVWAQA
ARRKLADQYP HLHNAELSKT LGKLWRLLNE SDKRPFIEEA ERLRMQHKKD HPDYKYQPRR
RKNGKAAQGE SECPGGEAEQ GGAAAIQAHY KSAHLDHRHP GEGSPMSDGN PEHPSGQSHG
PPTPPTTPKT ELQSGKADPK RDGRSMGEGG KPHIDFGNVD IGEISHEVMS NMETFDVAEL
DQYLPPNGHP GHVGSYSAAG YGLGSALAVA SGHSAWISKP PGVALPTVSP PGVDAKAQVK
TETAGPQGPS HYSDQPSTSQ IAYTSLSLPH YGSAFPSISR PQFDYSDHQP SGPYYGHSGQ
TSGLYSAFSY MGPSQRPLYT AISDPSPSGP QSHSPTHWEQ PVYTTLSRP
