ID   SOX7_HUMAN              Reviewed;         388 AA.
AC   Q9BT81; B4DKV0; Q53YD0;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Transcription factor SOX-7;
GN   Name=SOX7;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Fetal thymus;
RX   PubMed=11691915; DOI=10.1093/nar/29.21.4274;
RA   Takash W., Canizares J., Bonneaud N., Poulat F., Mattei M.-G., Jay P.,
RA   Berta P.;
RT   "SOX7 transcription factor: sequence, chromosomal localisation, expression,
RT   transactivation and interference with Wnt signalling.";
RL   Nucleic Acids Res. 29:4274-4283(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lung, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [6]
RP   FUNCTION, INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18819930; DOI=10.1158/1541-7786.mcr-07-2175;
RA   Guo L., Zhong D., Lau S., Liu X., Dong X.Y., Sun X., Yang V.W.,
RA   Vertino P.M., Moreno C.S., Varma V., Dong J.T., Zhou W.;
RT   "Sox7 Is an independent checkpoint for beta-catenin function in prostate
RT   and colon epithelial cells.";
RL   Mol. Cancer Res. 6:1421-1430(2008).
CC   -!- FUNCTION: Binds to and activates the CDH5 promoter, hence plays a role
CC       in the transcriptional regulation of genes expressed in the hemogenic
CC       endothelium and blocks further differentiation into blood precursors
CC       (By similarity). May be required for the survival of both hematopoietic
CC       and endothelial precursors during specification (By similarity).
CC       Competes with GATA4 for binding and activation of the FGF3 promoter (By
CC       similarity). Represses Wnt/beta-catenin-stimulated transcription,
CC       probably by targeting CTNNB1 to proteasomal degradation. Binds the DNA
CC       sequence 5'-AACAAT-3'. {ECO:0000250, ECO:0000269|PubMed:18819930}.
CC   -!- SUBUNIT: Interacts with CTNNB1/beta-catenin; this interaction may lead
CC       to the proteasomal degradation of active CTNNB1 and thus inhibition of
CC       Wnt/beta-catenin-stimulated transcription.
CC       {ECO:0000269|PubMed:18819930}.
CC   -!- INTERACTION:
CC       Q9BT81; Q92870-2: APBB2; NbExp=3; IntAct=EBI-7239117, EBI-21535880;
CC       Q9BT81; O76003: GLRX3; NbExp=3; IntAct=EBI-7239117, EBI-374781;
CC       Q9BT81; P42858: HTT; NbExp=15; IntAct=EBI-7239117, EBI-466029;
CC       Q9BT81; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-7239117, EBI-4395514;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC       Cytoplasm {ECO:0000269|PubMed:18819930}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BT81-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BT81-2; Sequence=VSP_056667;
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues.
CC       Present both in mesenchymal and epithelial cells in some adult tissues,
CC       including colon. Tends to be down-regulated in prostate adenocarcinomas
CC       and colorectal tumors due to promoter hypermethylation.
CC       {ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:18819930}.
CC   -!- DEVELOPMENTAL STAGE: In 8 week-old embryo, expressed in brain, tongue,
CC       heart, liver, lung and vertebrae. {ECO:0000269|PubMed:11691915}.
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DR   EMBL; AJ409320; CAC84226.1; -; mRNA.
DR   EMBL; BT006693; AAP35339.1; -; mRNA.
DR   EMBL; AK055556; BAB70955.1; -; mRNA.
DR   EMBL; AK296724; BAG59312.1; -; mRNA.
DR   EMBL; AC011008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC105001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC071947; AAH71947.1; -; mRNA.
DR   CCDS; CCDS5977.1; -. [Q9BT81-1]
DR   RefSeq; NP_113627.1; NM_031439.3. [Q9BT81-1]
DR   AlphaFoldDB; Q9BT81; -.
DR   SMR; Q9BT81; -.
DR   BioGRID; 123691; 7.
DR   IntAct; Q9BT81; 80.
DR   MINT; Q9BT81; -.
DR   STRING; 9606.ENSP00000301921; -.
DR   iPTMnet; Q9BT81; -.
DR   PhosphoSitePlus; Q9BT81; -.
DR   BioMuta; SOX7; -.
DR   DMDM; 20532272; -.
DR   EPD; Q9BT81; -.
DR   jPOST; Q9BT81; -.
DR   MassIVE; Q9BT81; -.
DR   MaxQB; Q9BT81; -.
DR   PaxDb; 9606-ENSP00000301921; -.
DR   PeptideAtlas; Q9BT81; -.
DR   ProteomicsDB; 4490; -.
DR   ProteomicsDB; 78959; -. [Q9BT81-1]
DR   Antibodypedia; 1821; 254 antibodies from 30 providers.
DR   DNASU; 83595; -.
DR   Ensembl; ENST00000304501.2; ENSP00000301921.1; ENSG00000171056.8. [Q9BT81-1]
DR   Ensembl; ENST00000646538.2; ENSP00000495029.1; ENSG00000285438.2. [Q9BT81-1]
DR   GeneID; 83595; -.
DR   KEGG; hsa:83595; -.
DR   MANE-Select; ENST00000304501.2; ENSP00000301921.1; NM_031439.4; NP_113627.1.
DR   UCSC; uc003wtf.5; human. [Q9BT81-1]
DR   AGR; HGNC:18196; -.
DR   CTD; 83595; -.
DR   DisGeNET; 83595; -.
DR   GeneCards; SOX7; -.
DR   HGNC; HGNC:18196; SOX7.
DR   HPA; ENSG00000171056; Tissue enhanced (vagina).
DR   MIM; 612202; gene.
DR   neXtProt; NX_Q9BT81; -.
DR   OpenTargets; ENSG00000171056; -.
DR   OpenTargets; ENSG00000258724; -.
DR   PharmGKB; PA38307; -.
DR   VEuPathDB; HostDB:ENSG00000171056; -.
DR   eggNOG; KOG0527; Eukaryota.
DR   GeneTree; ENSGT00940000161092; -.
DR   HOGENOM; CLU_044994_0_0_1; -.
DR   InParanoid; Q9BT81; -.
DR   OMA; HRTPVDK; -.
DR   OrthoDB; 2902801at2759; -.
DR   PhylomeDB; Q9BT81; -.
DR   TreeFam; TF321918; -.
DR   PathwayCommons; Q9BT81; -.
DR   Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   SignaLink; Q9BT81; -.
DR   SIGNOR; Q9BT81; -.
DR   BioGRID-ORCS; 83595; 20 hits in 1168 CRISPR screens.
DR   ChiTaRS; SOX7; human.
DR   GenomeRNAi; 83595; -.
DR   Pharos; Q9BT81; Tbio.
DR   PRO; PR:Q9BT81; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9BT81; Protein.
DR   Bgee; ENSG00000171056; Expressed in lower esophagus mucosa and 98 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0001706; P:endoderm formation; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd22046; HMG-box_SoxF_SOX7; 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; IPR033392; Sox7/17/18_central.
DR   InterPro; IPR021934; Sox_C.
DR   PANTHER; PTHR10270; SOX TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR10270:SF210; TRANSCRIPTION FACTOR SOX-7; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12067; Sox17_18_mid; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS51516; SOX_C; 1.
DR   Genevisible; Q9BT81; HS.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..388
FT                   /note="Transcription factor SOX-7"
FT                   /id="PRO_0000048731"
FT   DOMAIN          268..388
FT                   /note="Sox C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00849"
FT   DNA_BIND        45..113
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          20..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..79
FT                   /note="MASLLGAYPWPEGLECPALDAELSDGQSPPAVPRPPGDKGSESRIRRPMNAF
FT                   MVWAKDERKRLAVQNPDLHNAELSKML -> MSMLAERRRKQKWAVDPQNTAWSNDDSK
FT                   FGQRMLEKMGWSKGKGLGAQEQGATDHIKVQVKNNHLGLGATINNEDNWIAHQDDFNQL
FT                   LAELNTCHGQETTDSSDKKEKKSFSLEEKSKISKNRVHYMKFTK (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056667"
SQ   SEQUENCE   388 AA;  42197 MW;  DBA0EFE440DC2A74 CRC64;
     MASLLGAYPW PEGLECPALD AELSDGQSPP AVPRPPGDKG SESRIRRPMN AFMVWAKDER
     KRLAVQNPDL HNAELSKMLG KSWKALTLSQ KRPYVDEAER LRLQHMQDYP NYKYRPRRKK
     QAKRLCKRVD PGFLLSSLSR DQNALPEKRS GSRGALGEKE DRGEYSPGTA LPSLRGCYHE
     GPAGGGGGGT PSSVDTYPYG LPTPPEMSPL DVLEPEQTFF SSPCQEEHGH PRRIPHLPGH
     PYSPEYAPSP LHCSHPLGSL ALGQSPGVSM MSPVPGCPPS PAYYSPATYH PLHSNLQAHL
     GQLSPPPEHP GFDALDQLSQ VELLGDMDRN EFDQYLNTPG HPDSATGAMA LSGHVPVSQV
     TPTGPTETSL ISVLADATAT YYNSYSVS
//