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
