SOX30_HUMAN
ID SOX30_HUMAN Reviewed; 753 AA.
AC O94993; O94995; Q8IYX6;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcription factor SOX-30;
GN Name=SOX30;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC TISSUE=Testis;
RX PubMed=10359848; DOI=10.1093/nar/27.12.2503;
RA Osaki E., Nishina Y., Inazawa J., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Ohsugi M., Tezuka T., Yoshida M., Semba K.;
RT "Identification of a novel Sry-related gene and its germ cell-specific
RT expression.";
RL Nucleic Acids Res. 27:2503-2510(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-429.
RC TISSUE=Brain;
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 [3]
RP FUNCTION, INTERACTION WITH CTNNB1, AND SUBCELLULAR LOCATION.
RX PubMed=29739711; DOI=10.1016/j.ebiom.2018.04.026;
RA Han F., Liu W.B., Shi X.Y., Yang J.T., Zhang X., Li Z.M., Jiang X., Yin L.,
RA Li J.J., Huang C.S., Cao J., Liu J.Y.;
RT "SOX30 Inhibits Tumor Metastasis through Attenuating Wnt-Signaling via
RT Transcriptional and Posttranslational Regulation of beta-Catenin in Lung
RT Cancer.";
RL EBioMedicine 31:253-266(2018).
CC -!- FUNCTION: Acts as both a transcriptional activator and repressor
CC (PubMed:10359848, PubMed:29739711). Binds to the DNA sequence 5'-ACAAT-
CC 3' and shows a preference for guanine residues surrounding this core
CC motif (PubMed:10359848). Binds to its own promoter and activates its
CC own transcription (By similarity). Required to activate the expression
CC of postmeiotic genes involved in spermiogenesis (By similarity). Binds
CC to the promoter region of CTNNB1 and represses its transcription which
CC leads to inhibition of Wnt signaling (PubMed:29739711). Also inhibits
CC Wnt signaling by binding to the CTNNB1 protein, preventing interaction
CC of CTNNB1 with TCF7L2/TCF4 (PubMed:29739711).
CC {ECO:0000250|UniProtKB:Q8CGW4, ECO:0000269|PubMed:10359848,
CC ECO:0000269|PubMed:29739711}.
CC -!- SUBUNIT: Interacts with CTNNB1, competitively inhibiting CTNNB1-
CC TCF7L2/TCF4 interaction. {ECO:0000269|PubMed:29739711}.
CC -!- INTERACTION:
CC O94993; O43865: AHCYL1; NbExp=3; IntAct=EBI-742973, EBI-2371423;
CC O94993; Q8IYR0: CFAP206; NbExp=4; IntAct=EBI-742973, EBI-749051;
CC O94993; Q14192: FHL2; NbExp=3; IntAct=EBI-742973, EBI-701903;
CC O94993; Q01543: FLI1; NbExp=3; IntAct=EBI-742973, EBI-2271018;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10359848,
CC ECO:0000269|PubMed:29739711}. Cytoplasm {ECO:0000269|PubMed:29739711}.
CC Note=Enriched at the chromocenter. {ECO:0000250|UniProtKB:Q8CGW4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94993-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94993-2; Sequence=VSP_002205, VSP_002206;
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; AB022083; BAA37146.1; -; mRNA.
DR EMBL; AB022441; BAA37149.1; -; mRNA.
DR EMBL; BC033492; AAH33492.2; -; mRNA.
DR CCDS; CCDS4339.1; -. [O94993-1]
DR CCDS; CCDS4340.1; -. [O94993-2]
DR RefSeq; NP_001295094.1; NM_001308165.1.
DR RefSeq; NP_008948.1; NM_007017.2. [O94993-2]
DR RefSeq; NP_848511.1; NM_178424.1. [O94993-1]
DR PDB; 7JJK; X-ray; 1.40 A; A=335-423.
DR PDBsum; 7JJK; -.
DR AlphaFoldDB; O94993; -.
DR SMR; O94993; -.
DR BioGRID; 116247; 19.
DR IntAct; O94993; 15.
DR MINT; O94993; -.
DR STRING; 9606.ENSP00000265007; -.
DR iPTMnet; O94993; -.
DR PhosphoSitePlus; O94993; -.
DR BioMuta; SOX30; -.
DR MassIVE; O94993; -.
DR PaxDb; O94993; -.
DR PeptideAtlas; O94993; -.
DR PRIDE; O94993; -.
DR ProteomicsDB; 50621; -. [O94993-1]
DR ProteomicsDB; 50622; -. [O94993-2]
DR Antibodypedia; 1746; 224 antibodies from 29 providers.
DR DNASU; 11063; -.
DR Ensembl; ENST00000265007.11; ENSP00000265007.6; ENSG00000039600.11. [O94993-1]
DR Ensembl; ENST00000311371.9; ENSP00000309343.5; ENSG00000039600.11. [O94993-2]
DR GeneID; 11063; -.
DR KEGG; hsa:11063; -.
DR MANE-Select; ENST00000265007.11; ENSP00000265007.6; NM_178424.2; NP_848511.1.
DR UCSC; uc003lxb.1; human. [O94993-1]
DR CTD; 11063; -.
DR DisGeNET; 11063; -.
DR GeneCards; SOX30; -.
DR HGNC; HGNC:30635; SOX30.
DR HPA; ENSG00000039600; Tissue enriched (testis).
DR MIM; 606698; gene.
DR neXtProt; NX_O94993; -.
DR OpenTargets; ENSG00000039600; -.
DR PharmGKB; PA134876614; -.
DR VEuPathDB; HostDB:ENSG00000039600; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000161042; -.
DR HOGENOM; CLU_543964_0_0_1; -.
DR InParanoid; O94993; -.
DR OMA; PFREYPD; -.
DR OrthoDB; 369754at2759; -.
DR PhylomeDB; O94993; -.
DR TreeFam; TF336594; -.
DR PathwayCommons; O94993; -.
DR SignaLink; O94993; -.
DR BioGRID-ORCS; 11063; 20 hits in 1090 CRISPR screens.
DR ChiTaRS; SOX30; human.
DR GenomeRNAi; 11063; -.
DR Pharos; O94993; Tbio.
DR PRO; PR:O94993; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O94993; protein.
DR Bgee; ENSG00000039600; Expressed in left testis and 87 other tissues.
DR ExpressionAtlas; O94993; baseline and differential.
DR Genevisible; O94993; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0010369; C:chromocenter; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0120211; P:proacrosomal vesicle fusion; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0031960; P:response to corticosteroid; IEP:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..753
FT /note="Transcription factor SOX-30"
FT /id="PRO_0000048773"
FT DNA_BIND 337..405
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 463..501
FT /note="GETSPAIQLPTPAVQSPSPVTLFQPSVSSAAQVAVQDPS -> VHALTVGLP
FT LAMEIFRVQCQNALVIMKTGTQNMRVSFQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10359848"
FT /id="VSP_002205"
FT VAR_SEQ 502..753
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10359848"
FT /id="VSP_002206"
FT VARIANT 429
FT /note="Q -> K (in dbSNP:rs12188040)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_049563"
FT VARIANT 749
FT /note="V -> M (in dbSNP:rs889057)"
FT /id="VAR_024485"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:7JJK"
FT HELIX 364..377
FT /evidence="ECO:0007829|PDB:7JJK"
FT HELIX 380..398
FT /evidence="ECO:0007829|PDB:7JJK"
SQ SEQUENCE 753 AA; 81854 MW; E9BF1409EE7FE81D CRC64;
MERARPEPPP QPRPLRPAPP PLPVEGTSFW AAAMEPPPSS PTLSAAASAT LASSCGEAVA
SGLQPAVRRL LQVKPEQVLL LPQPQAQNEE AAASSAQARL LQFRPDLRLL QPPTASDGAT
SRPELHPVQP LALHVKAKKQ KLGPSLDQSV GPRGAVETGP RASRVVKLEG PGPALGYFRG
DEKGKLEAEE VMRDSMQGGA GKSPAAIREG VIKTEEPERL LEDCRLGAEP ASNGLVHGSA
EVILAPTSGA FGPHQQDLRI PLTLHTVPPG ARIQFQGAPP SELIRLTKVP LTPVPTKMQS
LLEPSVKIET KDVPLTVLPS DAGIPDTPFS KDRNGHVKRP MNAFMVWARI HRPALAKANP
AANNAEISVQ LGLEWNKLSE EQKKPYYDEA QKIKEKHREE FPGWVYQPRP GKRKRFPLSV
SNVFSGTTQN IISTNPTTVY PYRSPTYSVV IPSLQNPITH PVGETSPAIQ LPTPAVQSPS
PVTLFQPSVS SAAQVAVQDP SLPVYPALPP QRFTGPSQTD THQLHSEATH TVKQPTPVSL
ESANRISSSA STAHARFATS TIQPPREYSS VSPCPRSAPI PQASPIPHPH VYQPPPLGHP
ATLFGTPPRF SFHHPYFLPG PHYFPSSTCP YSRPPFGYGN FPSSMPECLS YYEDRYPKHE
GIFSTLNRDY SFRDYSSECT HSENSRSCEN MNGTSYYNSH SHSGEENLNP VPQLDIGTLE
NVFTAPTSTP SSIQQVNVTD SDEEEEEKVL RDL
