SOX9B_XENLA
ID SOX9B_XENLA Reviewed; 476 AA.
AC Q6DFF5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transcription factor Sox-9-B {ECO:0000305};
GN Name=sox9-b; Synonyms=sox9, sox9b {ECO:0000312|EMBL:AAH76783.1};
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:0000312|EMBL:BAG48176.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:BAG48176.1};
RA Yoshimoto S.;
RT "Xenopus laevis Sox9b.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAG48176.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAH76783.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {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).
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. {ECO:0000250|UniProtKB:Q04887}.
CC -!- SUBUNIT: Interacts with the sumoylation factors ube2i/ubc9 and sumo1.
CC {ECO:0000250|UniProtKB:B7ZR65}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B7ZR65,
CC ECO:0000250|UniProtKB:Q6F2E7, ECO:0000255|PROSITE-ProRule:PRU00267}.
CC Cytoplasm {ECO:0000250|UniProtKB:B7ZR65, ECO:0000250|UniProtKB:Q6F2E7}.
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:0000250|UniProtKB:B7ZR65, ECO:0000250|UniProtKB:Q6F2E7}.
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-364 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; AB439583; BAG48176.1; -; mRNA.
DR EMBL; BC076783; AAH76783.1; -; mRNA.
DR RefSeq; NP_001087942.1; NM_001094473.1.
DR AlphaFoldDB; Q6DFF5; -.
DR SMR; Q6DFF5; -.
DR DNASU; 494585; -.
DR GeneID; 494585; -.
DR KEGG; xla:494585; -.
DR CTD; 494585; -.
DR Xenbase; XB-GENE-1034775; sox9.L.
DR OrthoDB; 782373at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 494585; Expressed in internal ear and 17 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; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0043049; P:otic placode formation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR029548; SOX-9.
DR InterPro; IPR022151; Sox_N.
DR PANTHER; PTHR45803:SF1; PTHR45803:SF1; 1.
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; 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..476
FT /note="Transcription factor Sox-9-B"
FT /id="PRO_0000377416"
FT DNA_BIND 105..173
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 157..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..476
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 427..435
FT /note="9aaTAD 3"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT COMPBIAS 18..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..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 CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:B7ZR65"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:B7ZR65"
SQ SEQUENCE 476 AA; 53320 MW; 5F3B83C97613FD00 CRC64;
MNLLDPFMKM SEEQDKCLSG APSPTMSEDS AGSPCPSGSG SDTENTRPQE NTFPKGDQEM
KKETEDEKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK NKPHVKRPMN AFMVWAQAAR
RKLADQYPHL HNAELSKTLG KLWRLLNEGE KRPFVEEAER LRVQHKKDHP DYKYQPRRRK
SVKNGQSEQD DSAEQTHISP NAIFKALQAD SPHSTSSMSE VHSPGEHSGQ SQGPPTPPTT
PKTDVQPGKP DLKREGRPLQ ESGRQPPHID FRDVDIGELS SEVISTIETF DVNEFDQYLP
PNGHPGVGSA QAPYTGSYGI SSTPSATTGA GSAWMSKQQQ QPQQHSLSTI NSEQSQSQQR
THIKTEQLSP SHYSDQQQQH SPQQLNYSSF NLQHYSSSYP TITRAQYDYT EHQGSNSYYT
HASGQNSGLY SNFTYMNPSQ RPMYTPIADT TGVPSIPQTH SPQHWEQPVY TQLTRP
