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Wilms tumor protein homolog

 WT1_MOUSE               Reviewed;         449 AA.
P22561; A2A402;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
22-NOV-2017, entry version 164.
RecName: Full=Wilms tumor protein homolog;
Name=Wt1; Synonyms=Wt-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
PubMed=1671709; DOI=10.1128/MCB.11.3.1707;
Buckler A.J., Pelletier J., Haber D.A., Glaser T., Housman D.E.;
"Isolation, characterization, and expression of the murine Wilms'
tumor gene (WT1) during kidney development.";
Mol. Cell. Biol. 11:1707-1712(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
ALTERNATIVE INITIATION, AND ALTERNATIVE SPLICING (ISOFORMS 5 AND 6).
PubMed=8621495; DOI=10.1074/jbc.271.15.8646;
Bruening W., Pelletier J.;
"A non-AUG translational initiation event generates novel WT1
isoforms.";
J. Biol. Chem. 271:8646-8654(1996).
[4]
INTERACTION WITH U2AF2.
PubMed=9784496; DOI=10.1101/gad.12.20.3217;
Davies R.C., Calvio C., Bratt E., Larsson S.H., Lamond A.I.,
Hastie N.D.;
"WT1 interacts with the splicing factor U2AF65 in an isoform-dependent
manner and can be incorporated into spliceosomes.";
Genes Dev. 12:3217-3225(1998).
[5]
SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH POLYSOMES.
PubMed=14681305; DOI=10.1093/hmg/ddh040;
Niksic M., Slight J., Sanford J.R., Caceres J.F., Hastie N.D.;
"The Wilms' tumour protein (WT1) shuttles between nucleus and
cytoplasm and is present in functional polysomes.";
Hum. Mol. Genet. 13:463-471(2004).
[6]
INTERACTION WITH WTIP.
PubMed=14736876; DOI=10.1074/jbc.M314155200;
Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S.,
Mundel P., Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
"A WT1 co-regulator controls podocyte phenotype by shuttling between
adhesion structures and nucleus.";
J. Biol. Chem. 279:14398-14408(2004).
[7]
FUNCTION.
PubMed=17167543; DOI=10.1139/o06-065;
Morrison A.A., Venables J.P., Dellaire G., Ladomery M.R.;
"The Wilms tumour suppressor protein WT1 (+KTS isoform) binds alpha-
actinin 1 mRNA via its zinc-finger domain.";
Biochem. Cell Biol. 84:789-798(2006).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16467207; DOI=10.1182/blood-2005-07-2889;
Dame C., Kirschner K.M., Bartz K.V., Wallach T., Hussels C.S.,
Scholz H.;
"Wilms tumor suppressor, Wt1, is a transcriptional activator of the
erythropoietin gene.";
Blood 107:4282-4290(2006).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16920711; DOI=10.1074/jbc.M602668200;
Kirschner K.M., Wagner N., Wagner K.-D., Wellmann S., Scholz H.;
"The Wilms tumor suppressor Wt1 promotes cell adhesion through
transcriptional activation of the alpha4integrin gene.";
J. Biol. Chem. 281:31930-31939(2006).
[10]
FUNCTION, INTERACTION WITH CITED2, AND DEVELOPMENTAL STAGE.
PubMed=17537799; DOI=10.1242/dev.004390;
Val P., Martinez-Barbera J.P., Swain A.;
"Adrenal development is initiated by Cited2 and Wt1 through modulation
of Sf-1 dosage.";
Development 134:2349-2358(2007).
[11]
INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
PubMed=16924231; DOI=10.1038/sj.onc.1209922;
Spraggon L., Dudnakova T., Slight J., Lustig-Yariv O., Cotterell J.,
Hastie N., Miles C.;
"hnRNP-U directly interacts with WT1 and modulates WT1 transcriptional
activation.";
Oncogene 26:1484-1491(2007).
[12]
DEVELOPMENTAL STAGE.
PubMed=19457926; DOI=10.1093/hmg/ddp237;
Buaas F.W., Val P., Swain A.;
"The transcription co-factor CITED2 functions during sex determination
and early gonad development.";
Hum. Mol. Genet. 18:2989-3001(2009).
-!- FUNCTION: Transcription factor that plays an important role in
cellular development and cell survival (PubMed:16467207,
PubMed:16920711, PubMed:17537799). Recognizes and binds to the DNA
sequence 5'-GCG(T/G)GGGCG-3' (By similarity). Regulates the
expression of numerous target genes, including EPO
(PubMed:16467207). 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 (PubMed:17167543). Isoform 1
has lower affinity for DNA, and can bind RNA.
{ECO:0000250|UniProtKB:P19544, ECO:0000269|PubMed:16467207,
ECO:0000269|PubMed:16920711, ECO:0000269|PubMed:17167543,
ECO:0000269|PubMed:17537799}.
-!- SUBUNIT: Interacts with ZNF224 via the zinc-finger region.
Interacts with WTAP, AMER1 and SRY. Interacts with RBM4 (By
similarity). 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. Isoform 1 and
isoform 3 interacts with CITED2. {ECO:0000250,
ECO:0000269|PubMed:14681305, ECO:0000269|PubMed:14736876,
ECO:0000269|PubMed:16924231, ECO:0000269|PubMed:17537799,
ECO:0000269|PubMed:9784496}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleoplasm.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681305}.
Nucleus, nucleolus {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:14681305}. Nucleus speckle. Note=Shuttles
between nucleus and cytoplasm. {ECO:0000269|PubMed:14681305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=6;
Name=1;
IsoId=P22561-1; Sequence=Displayed;
Note=Detected in nucleus speckle, may bind mRNA.;
Name=2;
IsoId=P22561-2; Sequence=VSP_006868, VSP_006869;
Name=3;
IsoId=P22561-3; Sequence=VSP_006868;
Name=4;
IsoId=P22561-4; Sequence=VSP_006869;
Note=Detected in nucleoplasm, probably functions as
transcription factor.;
Name=5;
IsoId=P22561-5; Sequence=VSP_037585;
Note=Produced by alternative initiation of isoform 1. Extended
N-terminus.;
Name=6;
IsoId=P22561-6; Sequence=VSP_037585, VSP_006868;
Note=Produced by alternative initiation of isoform 1. Extended
N-terminus.;
-!- TISSUE SPECIFICITY: Detected in neurons of the embryonic dorsal
root ganglion and in Sertoli cells of the adult testis (at protein
level). Detected in kidney. {ECO:0000269|PubMed:16467207}.
-!- DEVELOPMENTAL STAGE: Expressed in the coelomic epithelium and
within some mesonephric tubules of the genital ridge at 10 dpc.
Expressed during kidney development. {ECO:0000269|PubMed:17537799,
ECO:0000269|PubMed:19457926}.
-!- 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=281 {ECO:0000250}; Note=Partially
edited. {ECO:0000250};
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M55512; AAA40573.1; -; mRNA.
EMBL; AL512584; CAM18169.2; -; Genomic_DNA.
CCDS; CCDS16496.2; -. [P22561-5]
PIR; A39692; A39692.
UniGene; Mm.389339; -.
ProteinModelPortal; P22561; -.
SMR; P22561; -.
IntAct; P22561; 1.
MINT; MINT-243493; -.
STRING; 10090.ENSMUSP00000117891; -.
PhosphoSitePlus; P22561; -.
PaxDb; P22561; -.
PRIDE; P22561; -.
DNASU; 22431; -.
MGI; MGI:98968; Wt1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
HOGENOM; HOG000230937; -.
HOVERGEN; HBG006960; -.
InParanoid; P22561; -.
PhylomeDB; P22561; -.
PRO; PR:P22561; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_WT1; -.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
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:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
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; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA: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; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0035802; P:adrenal cortex formation; IMP:UniProtKB.
GO; GO:0030325; P:adrenal gland development; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
GO; GO:0043010; P:camera-type eye development; IMP:MGI.
GO; GO:0060923; P:cardiac muscle cell fate commitment; IMP:BHF-UCL.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISS:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; TAS:DFLAT.
GO; GO:0060539; P:diaphragm development; IMP:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0032836; P:glomerular basement membrane development; ISO:MGI.
GO; GO:0072015; P:glomerular visceral epithelial cell development; IEP:UniProtKB.
GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; IDA:UniProtKB.
GO; GO:0032835; P:glomerulus development; IMP:UniProtKB.
GO; GO:0008406; P:gonad development; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0001822; P:kidney development; IMP:UniProtKB.
GO; GO:0030539; P:male genitalia development; IMP:UniProtKB.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:UniProtKB.
GO; GO:0001823; P:mesonephros development; IMP:MGI.
GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEP:UniProtKB.
GO; GO:0072075; P:metanephric mesenchyme development; IMP:UniProtKB.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IMP:UniProtKB.
GO; GO:0001656; P:metanephros development; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:2000195; P:negative regulation of female gonad development; IMP:UniProtKB.
GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; IMP:MGI.
GO; GO:0072302; P:negative regulation of metanephric glomerular mesangial cell proliferation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA: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; IMP:UniProtKB.
GO; GO:2000020; P:positive regulation of male gonad development; IMP:UniProtKB.
GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072166; P:posterior mesonephric tubule development; IMP:UniProtKB.
GO; GO:0003156; P:regulation of animal organ formation; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
GO; GO:0007530; P:sex determination; IMP:MGI.
GO; GO:0007338; P:single fertilization; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0007356; P:thorax and anterior abdomen determination; IMP:UniProtKB.
GO; GO:0009888; P:tissue development; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
GO; GO:0061032; P:visceral serous pericardium development; IMP:UniProtKB.
InterPro; IPR017987; Wilms_tumour.
InterPro; IPR000976; Wilms_tumour_N.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF02165; WT1; 2.
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.
1: Evidence at protein level;
Alternative initiation; 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 1 449 Wilms tumor protein homolog.
/FTId=PRO_0000047132.
ZN_FING 323 347 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 353 377 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 383 405 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 414 438 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 367 381 Important for interaction with target
DNA. {ECO:0000250}.
REGION 393 401 Important for interaction with target
DNA. {ECO:0000250}.
MOTIF 408 410 KTS motif. {ECO:0000250}.
COMPBIAS 28 83 Pro-rich.
SITE 424 424 Important for interaction with target
DNA. {ECO:0000250}.
SITE 430 430 Important for interaction with target
DNA. {ECO:0000250}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P19544}.
VAR_SEQ 1 1 M -> MDFLLSQEPASTCVPEPASQHTLRREPGCVQQPEQP
GDRGPRSAWAKSSAENPQDRRSGEPSASEPHLM (in
isoform 5 and isoform 6). {ECO:0000305}.
/FTId=VSP_037585.
VAR_SEQ 250 266 Missing (in isoform 2, isoform 3 and
isoform 6). {ECO:0000303|PubMed:1671709}.
/FTId=VSP_006868.
VAR_SEQ 408 410 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:1671709}.
/FTId=VSP_006869.
VARIANT 281 281 L -> P (in RNA edited version).
CONFLICT 33 33 R -> A (in Ref. 2; CAM18169).
{ECO:0000305}.
CONFLICT 269 269 I -> T (in Ref. 2; CAM18169).
{ECO:0000305}.
CONFLICT 446 447 HV -> QL (in Ref. 2; CAM18169).
{ECO:0000305}.
SEQUENCE 449 AA; 49246 MW; 962381E9C8D7A380 CRC64;
MGSDVRDLNA LLPAVSSLGG GGGGCGLPVS GARQWAPVLD FAPPGASAYG SLGGPAPPPA
PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTLHFSGQF TGTAGACRYG PFGPPPPSQA
SSGQARMFPN APYLPSCLES QPTIRNQGYS TVTFDGAPSY GHTPSHHAAQ FPNHSFKHED
PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ
MNLGATLKGM AAGSSSSVKW TEGQSNHGIG YESENHTAPI LCGAQYRIHT HGVFRGIQDV
RRVSGVAPTL VRSASETSEK RPFMCAYPGC NKRYFKLSHL QMHSRKHTGE KPYQCDFKDC
ERRFSRSDQL KRHQRRHTGV KPFQCKTCQR KFSRSDHLKT HTRTHTGKTS EKPFSCRWHS
CQKKFARSDE LVRHHNMHQR NMTKLHVAL


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