ID SOX9_XENTR Reviewed; 482 AA.
AC Q6F2E7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Transcription factor Sox-9 {ECO:0000305};
DE Short=Xt-sox9 {ECO:0000303|PubMed:18816826};
GN Name=sox9 {ECO:0000303|PubMed:18692165};
GN ORFNames=TNeu111f21.1 {ECO:0000303|Ref.2};
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:AAT72000.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qin S., Dors M., Johnson E., Bloom S., Hood L., Rowen L.;
RT "Sequence of Xenopus tropicalis development genes.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAT72000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ82635.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PUTATIVE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18692165; DOI=10.1016/j.bone.2008.07.005;
RA Miura S., Hanaoka K., Togashi S.;
RT "Skeletogenesis in Xenopus tropicalis: characteristic bone development in
RT an anuran amphibian.";
RL Bone 43:901-909(2008).
RN [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=18850318; DOI=10.1007/s10577-008-1257-z;
RA Uno Y., Nishida C., Yoshimoto S., Ito M., Oshima Y., Yokoyama S.,
RA Nakamura M., Matsuda Y.;
RT "Diversity in the origins of sex chromosomes in anurans inferred from
RT comparative mapping of sexual differentiation genes for three species of
RT the Raninae and Xenopodinae.";
RL Chromosome Res. 16:999-1011(2008).
RN [5] {ECO:0000305}
RP PUTATIVE FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18816826; DOI=10.1002/dvdy.21692;
RA El Jamil A., Kanhoush R., Magre S., Boizet-Bonhoure B., Penrad-Mobayed M.;
RT "Sex-specific expression of SOX9 during gonadogenesis in the amphibian
RT Xenopus tropicalis.";
RL Dev. Dyn. 237:2996-3005(2008).
CC -!- FUNCTION: Transcription factor that plays a key role in chondrocytes
CC differentiation and skeletal development. Specifically binds the 5'-
CC ACAAAG-3' DNA motif present in enhancers and super-enhancers and
CC promotes expression of genes important for chondrogenesis, including
CC COL2A1. Plays a central role in successive steps of chondrocyte
CC differentiation. Absolutely required for precartilaginous condensation,
CC the first step in chondrogenesis during which skeletal progenitors
CC differentiate into prechondrocytes. Together with SOX5 and SOX6,
CC required for overt chondrogenesis when condensed prechondrocytes
CC differentiate into early stage chondrocytes, the second step in
CC chondrogenesis. Later, required to direct hypertrophic maturation and
CC block osteoblast differentiation of growth plate chondrocytes:
CC maintains chondrocyte columnar proliferation, delays prehypertrophy and
CC then prevents osteoblastic differentiation of chondrocytes. Also
CC required for chondrocyte hypertrophy, both indirectly, by keeping the
CC lineage fate of chondrocytes, and directly, by remaining present in
CC upper hypertrophic cells. Low lipid levels are the main nutritional
CC determinant for chondrogenic commitment of skeletal progenitor cells:
CC when lipids levels are low, FOXO transcription factors promote
CC expression of SOX9, which induces chondrogenic commitment and
CC suppresses fatty acid oxidation. In addition to cartilage development,
CC also acts as a regulator of proliferation and differentiation in
CC epithelial stem/progenitor cells (By similarity). Unlikely to play a
CC role in sex determination but may function during testicular and
CC ovarian differentiation (PubMed:18692165, PubMed:18816826).
CC {ECO:0000250|UniProtKB:Q04887, ECO:0000269|PubMed:18692165,
CC ECO:0000269|PubMed:18816826}.
CC -!- SUBUNIT: Interacts with the sumoylation factors ube2i/ubc9 and sumo1.
CC {ECO:0000250|UniProtKB:B7ZR65}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:18816826}. Cytoplasm {ECO:0000269|PubMed:18816826}.
CC Note=Restricted to the nucleus of Sertoli-like cells in the testis, but
CC localizes to the cytoplasm of previtellogenic oocytes in the ovary
CC before being translocated into the nucleus of vitellogenic oocytes.
CC {ECO:0000269|PubMed:18816826}.
CC -!- TISSUE SPECIFICITY: Expressed in both male and female gonads from after
CC metamorphosis through to adult stages. In the testis, expression is
CC restricted to the supporting Sertoli-like cells. Conversely in the
CC ovary, expression is localized to primary oocytes (at protein level).
CC In developing limbs, expressed before chrondrocytes form (stage 52
CC tadpoles) and throughout the cartilaginous anlagen until stage 56,
CC after which expression ceases in the enlarged cells of the diaphysis.
CC At later stages, expression continues in the chondrocytes of the
CC epiphysis and metaphysis, and weak expression is seen in most of the
CC diaphysis. {ECO:0000269|PubMed:18692165, ECO:0000269|PubMed:18816826}.
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:P48436}.
CC -!- PTM: Sumoylated. Lys-370 is the major site of sumoylation, although
CC sumoylation at Lys-61 also occurs. Sumoylation plays a key role in
CC regulating formation of the neural crest and otic placode (By
CC similarity). {ECO:0000250|UniProtKB:B7ZR65}.
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DR EMBL; AC148478; AAT72000.1; -; Genomic_DNA.
DR EMBL; CR855424; CAJ82635.1; -; mRNA.
DR RefSeq; NP_001016853.1; NM_001016853.2.
DR AlphaFoldDB; Q6F2E7; -.
DR SMR; Q6F2E7; -.
DR STRING; 8364.ENSXETP00000025787; -.
DR Ensembl; ENSXETT00000087663; ENSXETP00000093444; ENSXETG00000035507.
DR GeneID; 549607; -.
DR KEGG; xtr:549607; -.
DR AGR; Xenbase:XB-GENE-1034769; -.
DR CTD; 6662; -.
DR Xenbase; XB-GENE-1034769; sox9.
DR InParanoid; Q6F2E7; -.
DR OMA; QSSNSYY; -.
DR OrthoDB; 2902801at2759; -.
DR Reactome; R-XTR-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-XTR-8878166; Transcriptional regulation by RUNX2.
DR Proteomes; UP000008143; Chromosome 10.
DR Bgee; ENSXETG00000035507; Expressed in neurula embryo and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IEP:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0043049; P:otic placode formation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
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:SF1; TRANSCRIPTION FACTOR SOX-9; 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 Activator; Chondrogenesis; Cytoplasm; Developmental protein;
KW Differentiation; DNA-binding; Gonadal differentiation; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..482
FT /note="Transcription factor Sox-9"
FT /id="PRO_0000377417"
FT DNA_BIND 105..173
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..103
FT /note="Dimerization (DIM)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 63..103
FT /note="PQA"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 160..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..308
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 295..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..482
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 448..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 276..285
FT /note="9aaTAD 1"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 291..299
FT /note="9aaTAD 2"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 433..441
FT /note="9aaTAD 3"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT COMPBIAS 18..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:B7ZR65"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:B7ZR65"
SQ SEQUENCE 482 AA; 53985 MW; 718E12FF777342EC CRC64;
MNLLDPFMKM TEEQDKCMSG APSPTMSEDS AGSPCPSGSG SDTENTRPQE NTFPKGDPEL
KKETEDEKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK SKPHVKRPMN AFMVWAQAAR
RKLADQYPHL HNAELSKTLG KLWRLLNEGE KRPFVEEAER LRIQHKKDHP DYKYQPRRRK
SVKNGQSEQE DGAEQTHISP NAIFKALQAD SPHSASSMSE VHSPGEHSGQ SQGPPTPPTT
PKTDVQPGKP DLKREGRPLQ ESGRQPPHID FRDVDIGELS SEVISTIETF DVNEFDQYLP
PNGHPGVGST QAPYTGSYGI NSTPSATPGA GPAWMSKQQQ QQQQQPQPPQ HSLSTINSEQ
SQSQQRTHIK TEQLSPSHYS DQQQQHSPQQ LNYSSFNLQH YSSSYPTITR AQYDYTEHQG
SNSYYSHASG QNSGLYSNFS YMNPSQRPMY TPIADTTGVP SIPQTHSPQH WEQPVYTQLT
RP
//
