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Wilms tumor protein homolog

 WT1_RAT                 Reviewed;         448 AA.
P49952;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Wilms tumor protein homolog;
Name=Wt1; Synonyms=Wt-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=1330293;
Sharma P.M., Yang X., Bowman M., Roberts V., Sukumar S.;
"Molecular cloning of rat Wilms' tumor complementary DNA and a study
of messenger RNA expression in the urogenital system and the brain.";
Cancer Res. 52:6407-6412(1992).
[2]
RNA EDITING OF POSITION 280.
PubMed=7926762; DOI=10.1101/gad.8.6.720;
Sharma P.M., Bowman M., Madden S.L., Rauscher F.J. III, Sukumar S.;
"RNA editing in the Wilms' tumor susceptibility gene, WT1.";
Genes Dev. 8:720-731(1994).
-!- FUNCTION: Transcription factor that plays an important role in
cellular development and cell survival. Recognizes and binds to
the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of
numerous target genes, including EPO. Plays an essential role for
development of the urogenital system. It has a tumor suppressor as
well as an oncogenic role in tumor formation. Function may be
isoform-specific: isoforms lacking the KTS motif may act as
transcription factors. Isoforms containing the KTS motif may bind
mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has
lower affinity for DNA, and can bind RNA.
{ECO:0000250|UniProtKB:P19544}.
-!- SUBUNIT: Interacts with ZNF224 via the zinc-finger region.
Interacts with WTAP, AMER1 and SRY. Homodimer. Interacts with
WTIP. Interacts with actively translating polysomes. Detected in
nuclear ribonucleoprotein (mRNP) particles. Interacts with U2AF2.
Interacts with HNRNPU via the zinc-finger region. Interacts with
CITED2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleoplasm
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
{ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus speckle
{ECO:0000250}. Note=Shuttles between nucleus and cytoplasm.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P49952-1; Sequence=Displayed;
Name=2;
IsoId=P49952-2; Sequence=VSP_006872, VSP_006873;
Name=3;
IsoId=P49952-3; Sequence=VSP_006872;
Name=4;
IsoId=P49952-4; Sequence=VSP_006873;
-!- TISSUE SPECIFICITY: Kidney.
-!- DEVELOPMENTAL STAGE: Expressed during kidney development.
-!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3'
via its C2H2-type zinc fingers. Starting from the N-terminus, the
second zinc finger binds to the 3'-GCG motif, the middle zinc
finger interacts with the central TGG motif, and the C-terminal
zinc finger binds to the 5'-GCG motif. Binds double-stranded
target DNA, irrespective of the cytosine methylation status. Has
reduced affinity for target DNA where the cytosines have been
oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-
carboxylcytosine. {ECO:0000250|UniProtKB:P19544}.
-!- RNA EDITING: Modified_positions=280 {ECO:0000269|PubMed:7926762};
Note=Partially edited.;
-!- MISCELLANEOUS: Presence of the KTS motif hinders interactions
between DNA and zinc-finger 4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; X69716; CAA49373.1; -; mRNA.
PIR; S33926; S33926.
RefSeq; NP_113722.2; NM_031534.2.
UniGene; Rn.92531; -.
ProteinModelPortal; P49952; -.
SMR; P49952; -.
BioGrid; 246993; 1.
STRING; 10116.ENSRNOP00000060038; -.
PaxDb; P49952; -.
PRIDE; P49952; -.
GeneID; 24883; -.
KEGG; rno:24883; -.
UCSC; RGD:3974; rat. [P49952-1]
CTD; 7490; -.
RGD; 3974; Wt1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000230937; -.
HOVERGEN; HBG006960; -.
InParanoid; P49952; -.
KO; K09234; -.
PhylomeDB; P49952; -.
PRO; PR:P49952; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0035802; P:adrenal cortex formation; ISS:UniProtKB.
GO; GO:0030325; P:adrenal gland development; ISS:UniProtKB.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISS:UniProtKB.
GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0032835; P:glomerulus development; ISS:UniProtKB.
GO; GO:0008406; P:gonad development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0030539; P:male genitalia development; ISS:UniProtKB.
GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2000195; P:negative regulation of female gonad development; ISS:UniProtKB.
GO; GO:0072302; P:negative regulation of metanephric glomerular mesangial cell proliferation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
GO; GO:2000020; P:positive regulation of male gonad development; ISS:UniProtKB.
GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072166; P:posterior mesonephric tubule development; ISS:UniProtKB.
GO; GO:0003156; P:regulation of animal organ formation; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
GO; GO:0007530; P:sex determination; ISS:UniProtKB.
GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
GO; GO:0009888; P:tissue development; ISS:UniProtKB.
GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
GO; GO:0061032; P:visceral serous pericardium development; ISS:UniProtKB.
Gene3D; 2.40.155.10; -; 1.
InterPro; IPR009017; GFP.
InterPro; IPR017987; Wilms_tumour.
InterPro; IPR000976; Wilms_tumour_N.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF02165; WT1; 1.
PRINTS; PR00049; WILMSTUMOUR.
SMART; SM00355; ZnF_C2H2; 4.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
RNA editing; RNA-binding; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 448 Wilms tumor protein homolog.
/FTId=PRO_0000047134.
ZN_FING 322 346 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 352 376 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 382 404 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 413 437 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 366 380 Important for interaction with target
DNA. {ECO:0000250}.
REGION 392 400 Important for interaction with target
DNA. {ECO:0000250}.
MOTIF 407 409 KTS motif. {ECO:0000250}.
COMPBIAS 27 82 Pro-rich.
SITE 423 423 Important for interaction with target
DNA. {ECO:0000250}.
SITE 429 429 Important for interaction with target
DNA. {ECO:0000250}.
CROSSLNK 72 72 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 176 176 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 443 443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P19544}.
VAR_SEQ 249 265 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:1330293}.
/FTId=VSP_006872.
VAR_SEQ 407 409 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:1330293}.
/FTId=VSP_006873.
VARIANT 280 280 L -> P (in RNA edited version).
SEQUENCE 448 AA; 49193 MW; 329AC9AC1FF73F76 CRC64;
MGSDVRDLNA LLPAVSSLGG GGGCGLPVSG ARQWAPVLDF APPGASAYGS LGGPAPPPAP
PPPPPPPHSF IKQEPSWGGA EPHEEQCLSA FTLHFSGQFT GTAGACRYGP FGPPPPSQAS
SGQARMFPNA PYLPSCLESQ PSIRNQGYST VTFDGAPSYG HTPSHHAAQF PNHSFKHEDP
MGQQGSLGEQ QYSVPPPVYG CHTPTDSCTG SQALLLRTPY SSDNLYQMTS QLECMTWNQM
NLGATLKGMA AGSSSSVKWT EGQSNHGTGY ESENHTTPIL CGAQYRIHTH GVFRGIQDVR
RVSGVAPTLV RSASETSEKR PFMCAYPGCN KRYFKLSHLQ MHSRKHTGEK PYQCDFKDCE
RRFSRSDQLK RHQRRHTGVK PFQCKTCQRK FSRSDHLKTH TRTHTGKTSE KPFSCRWHSC
QKKFARSDEL VRHHNMHQRN MTKLHVAL


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