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WT1B_XENLA
ID   WT1B_XENLA              Reviewed;         407 AA.
AC   P79958;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Wilms tumor protein homolog B;
DE            Short=XWT1b {ECO:0000303|PubMed:16818449};
DE            Short=XeWT1 {ECO:0000303|PubMed:8917094};
GN   Name=wt1-b; Synonyms=wt1 {ECO:0000312|EMBL:BAA11522.1};
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:0000305, ECO:0000312|EMBL:BAA11522.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis {ECO:0000312|EMBL:BAA11522.1};
RX   PubMed=8917094; DOI=10.1016/0378-1119(96)00143-6;
RA   Semba K., Saito-Ueno R., Takayama G., Kondo M.;
RT   "cDNA cloning and its pronephros-specific expression of the Wilms' tumor
RT   suppressor gene, WT1, from Xenopus laevis.";
RL   Gene 175:167-172(1996).
RN   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16818449; DOI=10.1242/dev.02458;
RA   Taelman V., Van Campenhout C., Soelter M., Pieler T., Bellefroid E.J.;
RT   "The Notch-effector HRT1 gene plays a role in glomerular development and
RT   patterning of the Xenopus pronephros anlagen.";
RL   Development 133:2961-2971(2006).
CC   -!- FUNCTION: Transcription factor required for development of the vascular
CC       component of the pronephric kidney, the glomus; may repress tubule-
CC       specific gene expression in the portion of the pronephros fated to form
CC       the glomus (PubMed:16818449). Recognizes and binds to the DNA sequence
CC       5'-GCG(T/G)GGGCG-3' (By similarity). Inhibits Wnt-signaling during
CC       embryonic development (By similarity). {ECO:0000250|UniProtKB:B7ZSG3,
CC       ECO:0000250|UniProtKB:P19544, ECO:0000269|PubMed:16818449}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P22561}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P22561}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:P22561}. Note=Shuttles between nucleus and
CC       cytoplasm. {ECO:0000250|UniProtKB:P22561}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pronephric anlage from stage 23 to
CC       30. Also expressed in the adult kidney (mesonephros) and in testis.
CC       {ECO:0000269|PubMed:8917094}.
CC   -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC       its C2H2-type zinc fingers. Starting from the N-terminus, the second
CC       zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts
CC       with the central TGG motif, and the C-terminal zinc finger binds to the
CC       5'-GCG motif. Binds double-stranded target DNA, irrespective of the
CC       cytosine methylation status. Has reduced affinity for target DNA where
CC       the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-
CC       formylcytosine or 5-carboxylcytosine. {ECO:0000250|UniProtKB:P19544}.
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:P19544}.
CC   -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC       {ECO:0000255}.
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DR   EMBL; D82051; BAA11522.1; -; mRNA.
DR   PIR; JC5046; JC5046.
DR   RefSeq; NP_001079336.1; NM_001085867.1.
DR   AlphaFoldDB; P79958; -.
DR   BMRB; P79958; -.
DR   SMR; P79958; -.
DR   GeneID; 378664; -.
DR   KEGG; xla:378664; -.
DR   CTD; 378664; -.
DR   Xenbase; XB-GENE-6252376; wt1.L.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 378664; Expressed in kidney and 6 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
DR   GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0072013; P:glomus development; IMP:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; IEP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR017987; Wilms_tumour.
DR   InterPro; IPR000976; Wilms_tumour_N.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23235:SF49; PTHR23235:SF49; 1.
DR   Pfam; PF02165; WT1; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; RNA editing;
KW   RNA-binding; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway; Zinc; Zinc-finger.
FT   CHAIN           1..407
FT                   /note="Wilms tumor protein homolog B"
FT                   /id="PRO_0000391388"
FT   ZN_FING         284..308
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         314..338
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         344..366
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         372..396
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          328..342
FT                   /note="Important for interaction with target DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   REGION          354..362
FT                   /note="Important for interaction with target DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   MOTIF           213..221
FT                   /note="9aaTAD"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   SITE            382
FT                   /note="Important for interaction with target DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   SITE            388
FT                   /note="Important for interaction with target DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   CROSSLNK        55
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
FT   CROSSLNK        158
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250|UniProtKB:P19544"
SQ   SEQUENCE   407 AA;  45983 MW;  E2554C658005870C CRC64;
     MGSDVRDMNL LPPVSSLSGN SSCNMPVSNS SQWAPVLDFP PGAPYSSLTP HSFIKQEPTW
     NPDPHEDQCL SAFTVHFSGQ FTGTAGACRY GPFGAPTPSQ ATTGQARMFP NAPYLSNCLD
     NQQSMRNQGY SAVAFDGTPS YGHTPSHHTA QFTNHSFKHE DPISQQTSLG EQQYSVPPPV
     YGCHTPTDTC TGSQALLLRT PYNSDNLYQM ECMTWNQMNL GSSLKSHGTT YENDSHSAPM
     LYSCGGQYRI HTHGVFRGIQ DVRRVPGVTP AIVRSTEANE KRPFMCAYPG CNKRYFKLSH
     LQMHSRKHTG EKPYQCDFKD CERRFSRSDQ LKRHQRRHTG VKPFQCKTCQ RKFSRSDHLK
     THTRTHTGEK PFSCRWPSCQ KKFARSDELV RHHNMHQRNM TKLQLAL
 
 
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