WT1_XENTR
ID WT1_XENTR Reviewed; 413 AA.
AC B5DE03;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Wilms tumor protein homolog {ECO:0000250|UniProtKB:P22561};
GN Name=wt1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI68476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI68476.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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}.
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 -!- 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; BC168476; AAI68476.1; -; mRNA.
DR RefSeq; NP_001135625.1; NM_001142153.1.
DR AlphaFoldDB; B5DE03; -.
DR BMRB; B5DE03; -.
DR SMR; B5DE03; -.
DR Ensembl; ENSXETT00000101007; ENSXETP00000083701; ENSXETG00000040519.
DR GeneID; 100216184; -.
DR KEGG; xtr:100216184; -.
DR CTD; 7490; -.
DR Xenbase; XB-GENE-484999; wt1.
DR InParanoid; B5DE03; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000040519; Expressed in testis and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..413
FT /note="Wilms tumor protein homolog"
FT /id="PRO_0000391389"
FT ZN_FING 290..314
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 320..344
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 350..372
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..402
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 334..348
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT REGION 360..368
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT MOTIF 218..226
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT SITE 388
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT SITE 394
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19544"
SQ SEQUENCE 413 AA; 46461 MW; CF62CB23A13C58A8 CRC64;
MGSDVRDMNA LLPPVSTLSG NSSCSMPVSS SGQWAPVLDF PPGAPYSSLP PHSFIKQEPT
WNPDPHEDQC LSAFTVHFSG QFTGTAGACR YGAFGAPTPS QATTGQARMF PNSPYLSNCL
DNQQGMRNQG YSAVAFDGTP SYGHTPSHHT AQFTNHSFKH EDPMGQQTSL GEQQYSVPPP
VYGCHTPTDS CTGSQALLLR TPYNSDNLYQ MTSQLECMTW NQMNLGSSLK SHGTSYENDS
HSTPMLYSCG GQYRIHTHGV FRGIQDVRRV PGVTPAIVRS STEANEKRPF MCAYPGCNKR
YFKLSHLQMH SRKHTGEKPY QCDFKDCERR FSRSDQLKRH QRRHTGIKPF QCKTCQRKFS
RSDHLKTHTR THTGEKPFSC RWPSCQKKFA RSDELVRHHN MHQRNMTKLQ LAL
