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SOX10_XENTR
ID   SOX10_XENTR             Reviewed;         436 AA.
AC   A4IIJ8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Transcription factor Sox-10 {ECO:0000312|EMBL:AAI36048.1};
DE   AltName: Full=SRY (sex determining region Y)-box 10;
GN   Name=sox10 {ECO:0000312|EMBL:AAI36048.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI36048.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI36048.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8AXX8}.
CC   -!- SUBUNIT: Interacts with the sumoylation factors ube2i/ubc9 and sumo1.
CC       {ECO:0000250|UniProtKB:Q8AXX8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P56693}. Nucleus
CC       {ECO:0000250|UniProtKB:P56693}.
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:0000250|UniProtKB:Q8AXX8}.
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DR   EMBL; BC136047; AAI36048.1; -; mRNA.
DR   RefSeq; NP_001093691.1; NM_001100221.1.
DR   RefSeq; XP_012815859.1; XM_012960405.2.
DR   AlphaFoldDB; A4IIJ8; -.
DR   SMR; A4IIJ8; -.
DR   PaxDb; A4IIJ8; -.
DR   DNASU; 100101700; -.
DR   Ensembl; ENSXETT00000013902; ENSXETP00000013902; ENSXETG00000006348.
DR   GeneID; 100101700; -.
DR   KEGG; xtr:100101700; -.
DR   CTD; 6663; -.
DR   Xenbase; XB-GENE-480304; sox10.
DR   eggNOG; KOG0527; Eukaryota.
DR   HOGENOM; CLU_031800_0_0_1; -.
DR   InParanoid; A4IIJ8; -.
DR   OMA; HTTGQSH; -.
DR   OrthoDB; 782373at2759; -.
DR   PhylomeDB; A4IIJ8; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000006348; Expressed in neural crest and 16 other 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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0030318; P:melanocyte differentiation; ISS:UniProtKB.
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:0014029; P:neural crest formation; ISS:UniProtKB.
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   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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   Cytoplasm; Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Wnt signaling pathway.
FT   CHAIN           1..436
FT                   /note="Transcription factor Sox-10"
FT                   /id="PRO_0000376862"
FT   DNA_BIND        90..158
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..88
FT                   /note="Dimerization (DIM)"
FT                   /evidence="ECO:0000250|UniProtKB:P56693"
FT   REGION          145..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..295
FT                   /note="Transactivation domain (TAM)"
FT                   /evidence="ECO:0000250|UniProtKB:P56693"
FT   REGION          322..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..436
FT                   /note="Transactivation domain (TAC)"
FT                   /evidence="ECO:0000250|UniProtKB:P56693"
FT   REGION          413..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        44
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AXX8"
FT   CROSSLNK        331
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8AXX8"
SQ   SEQUENCE   436 AA;  47852 MW;  7F20DA1A8EB598A1 CRC64;
     MSDDQSLSEV EMSPVGSEDP SLTPDPLPPH AHSSPDDDEE TKVKKEQDSE DERFPVCIRE
     AVSQVLSGYD WTLVPMPVRV NGGSKSKPHV KRPMNAFMVW AQAARRKLAD QYPHLHNAEL
     SKTLGKLWRL LNENDKRPFI EEAERLRMQH KKDHPDYKYQ PRRRKNGKPN PGEGDGSSEA
     EGGAASIQAH YKNSHLDHRH GSPMSDGNSE HSAGQSHGPP TPPTTPKTEL QAGKSDGKRD
     GSRSLGEGGK PHIDFGNVDI GEISHDVMAN METFDVNEFD QYLPPNGHAG HPSHIGGYTS
     SYGLSGALAA GPSAWALAKQ HPQTDSKAQV KTESSSTSHY TEQPSTSQLT YTSLGLPHYG
     SAFPSISRPQ FDYADHQPSS SYYSHSSQAS SLYSAFSYMG PPQRPLYTAI SDSPSVAQSH
     SPTHWEQPVY TTLSRP
 
 
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