WT1_MOUSE
ID WT1_MOUSE Reviewed; 449 AA.
AC P22561; A2A402;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Wilms tumor protein homolog;
GN Name=Wt1; Synonyms=Wt-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=1671709; DOI=10.1128/mcb.11.3.1707-1712.1991;
RA Buckler A.J., Pelletier J., Haber D.A., Glaser T., Housman D.E.;
RT "Isolation, characterization, and expression of the murine Wilms' tumor
RT gene (WT1) during kidney development.";
RL Mol. Cell. Biol. 11:1707-1712(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP ALTERNATIVE INITIATION, AND ALTERNATIVE SPLICING (ISOFORMS 5 AND 6).
RX PubMed=8621495; DOI=10.1074/jbc.271.15.8646;
RA Bruening W., Pelletier J.;
RT "A non-AUG translational initiation event generates novel WT1 isoforms.";
RL J. Biol. Chem. 271:8646-8654(1996).
RN [4]
RP INTERACTION WITH U2AF2.
RX PubMed=9784496; DOI=10.1101/gad.12.20.3217;
RA Davies R.C., Calvio C., Bratt E., Larsson S.H., Lamond A.I., Hastie N.D.;
RT "WT1 interacts with the splicing factor U2AF65 in an isoform-dependent
RT manner and can be incorporated into spliceosomes.";
RL Genes Dev. 12:3217-3225(1998).
RN [5]
RP SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH POLYSOMES.
RX PubMed=14681305; DOI=10.1093/hmg/ddh040;
RA Niksic M., Slight J., Sanford J.R., Caceres J.F., Hastie N.D.;
RT "The Wilms' tumour protein (WT1) shuttles between nucleus and cytoplasm and
RT is present in functional polysomes.";
RL Hum. Mol. Genet. 13:463-471(2004).
RN [6]
RP INTERACTION WITH WTIP.
RX PubMed=14736876; DOI=10.1074/jbc.m314155200;
RA Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
RA Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S., Mundel P.,
RA Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
RT "A WT1 co-regulator controls podocyte phenotype by shuttling between
RT adhesion structures and nucleus.";
RL J. Biol. Chem. 279:14398-14408(2004).
RN [7]
RP FUNCTION.
RX PubMed=17167543; DOI=10.1139/o06-065;
RA Morrison A.A., Venables J.P., Dellaire G., Ladomery M.R.;
RT "The Wilms tumour suppressor protein WT1 (+KTS isoform) binds alpha-actinin
RT 1 mRNA via its zinc-finger domain.";
RL Biochem. Cell Biol. 84:789-798(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16467207; DOI=10.1182/blood-2005-07-2889;
RA Dame C., Kirschner K.M., Bartz K.V., Wallach T., Hussels C.S., Scholz H.;
RT "Wilms tumor suppressor, Wt1, is a transcriptional activator of the
RT erythropoietin gene.";
RL Blood 107:4282-4290(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16920711; DOI=10.1074/jbc.m602668200;
RA Kirschner K.M., Wagner N., Wagner K.-D., Wellmann S., Scholz H.;
RT "The Wilms tumor suppressor Wt1 promotes cell adhesion through
RT transcriptional activation of the alpha4integrin gene.";
RL J. Biol. Chem. 281:31930-31939(2006).
RN [10]
RP FUNCTION, INTERACTION WITH CITED2, AND DEVELOPMENTAL STAGE.
RX PubMed=17537799; DOI=10.1242/dev.004390;
RA Val P., Martinez-Barbera J.P., Swain A.;
RT "Adrenal development is initiated by Cited2 and Wt1 through modulation of
RT Sf-1 dosage.";
RL Development 134:2349-2358(2007).
RN [11]
RP INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
RX PubMed=16924231; DOI=10.1038/sj.onc.1209922;
RA Spraggon L., Dudnakova T., Slight J., Lustig-Yariv O., Cotterell J.,
RA Hastie N., Miles C.;
RT "hnRNP-U directly interacts with WT1 and modulates WT1 transcriptional
RT activation.";
RL Oncogene 26:1484-1491(2007).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=19457926; DOI=10.1093/hmg/ddp237;
RA Buaas F.W., Val P., Swain A.;
RT "The transcription co-factor CITED2 functions during sex determination and
RT early gonad development.";
RL Hum. Mol. Genet. 18:2989-3001(2009).
CC -!- FUNCTION: Transcription factor that plays an important role in cellular
CC development and cell survival (PubMed:16467207, PubMed:16920711,
CC PubMed:17537799). Recognizes and binds to the DNA sequence 5'-
CC GCG(T/G)GGGCG-3' (By similarity). Regulates the expression of numerous
CC target genes, including EPO (PubMed:16467207). Plays an essential role
CC for development of the urogenital system. It has a tumor suppressor as
CC well as an oncogenic role in tumor formation. Function may be isoform-
CC specific: isoforms lacking the KTS motif may act as transcription
CC factors. Isoforms containing the KTS motif may bind mRNA and play a
CC role in mRNA metabolism or splicing (PubMed:17167543). Isoform 1 has
CC lower affinity for DNA, and can bind RNA.
CC {ECO:0000250|UniProtKB:P19544, ECO:0000269|PubMed:16467207,
CC ECO:0000269|PubMed:16920711, ECO:0000269|PubMed:17167543,
CC ECO:0000269|PubMed:17537799}.
CC -!- SUBUNIT: Interacts with ZNF224 via the zinc-finger region. Interacts
CC with WTAP, AMER1 and SRY. Interacts with RBM4 (By similarity).
CC Homodimer. Interacts with WTIP. Interacts with actively translating
CC polysomes. Detected in nuclear ribonucleoprotein (mRNP) particles.
CC Interacts with U2AF2. Interacts with HNRNPU via the zinc-finger region.
CC Isoform 1 and isoform 3 interacts with CITED2. {ECO:0000250,
CC ECO:0000269|PubMed:14681305, ECO:0000269|PubMed:14736876,
CC ECO:0000269|PubMed:16924231, ECO:0000269|PubMed:17537799,
CC ECO:0000269|PubMed:9784496}.
CC -!- INTERACTION:
CC P22561; Q4JK59: Tet2; NbExp=2; IntAct=EBI-8327829, EBI-4291768;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleoplasm.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14681305}. Nucleus,
CC nucleolus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:14681305}.
CC Nucleus speckle. Note=Shuttles between nucleus and cytoplasm.
CC {ECO:0000269|PubMed:14681305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=6;
CC Name=1;
CC IsoId=P22561-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22561-2; Sequence=VSP_006868, VSP_006869;
CC Name=3;
CC IsoId=P22561-3; Sequence=VSP_006868;
CC Name=4;
CC IsoId=P22561-4; Sequence=VSP_006869;
CC Name=5;
CC IsoId=P22561-5; Sequence=VSP_037585;
CC Name=6;
CC IsoId=P22561-6; Sequence=VSP_037585, VSP_006868;
CC -!- TISSUE SPECIFICITY: Detected in neurons of the embryonic dorsal root
CC ganglion and in Sertoli cells of the adult testis (at protein level).
CC Detected in kidney. {ECO:0000269|PubMed:16467207}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the coelomic epithelium and within
CC some mesonephric tubules of the genital ridge at 10 dpc. Expressed
CC during kidney development. {ECO:0000269|PubMed:17537799,
CC ECO:0000269|PubMed:19457926}.
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 -!- RNA EDITING: Modified_positions=281 {ECO:0000250}; Note=Partially
CC edited. {ECO:0000250};
CC -!- MISCELLANEOUS: Presence of the KTS motif hinders interactions between
CC DNA and zinc-finger 4. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Detected in nucleus speckle, may bind mRNA.
CC -!- MISCELLANEOUS: [Isoform 4]: Detected in nucleoplasm, probably functions
CC as transcription factor. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative initiation of
CC isoform 1. Extended N-terminus. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative initiation of
CC isoform 1. Extended N-terminus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC 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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DR EMBL; M55512; AAA40573.1; -; mRNA.
DR EMBL; AL512584; CAM18169.2; -; Genomic_DNA.
DR CCDS; CCDS16496.2; -. [P22561-5]
DR PIR; A39692; A39692.
DR AlphaFoldDB; P22561; -.
DR BMRB; P22561; -.
DR SMR; P22561; -.
DR IntAct; P22561; 1.
DR STRING; 10090.ENSMUSP00000117891; -.
DR PhosphoSitePlus; P22561; -.
DR PaxDb; P22561; -.
DR PRIDE; P22561; -.
DR ProteomicsDB; 299699; -. [P22561-1]
DR ProteomicsDB; 299700; -. [P22561-2]
DR ProteomicsDB; 299701; -. [P22561-3]
DR ProteomicsDB; 299702; -. [P22561-4]
DR ProteomicsDB; 299703; -. [P22561-5]
DR ProteomicsDB; 299704; -. [P22561-6]
DR DNASU; 22431; -.
DR MGI; MGI:98968; Wt1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P22561; -.
DR PhylomeDB; P22561; -.
DR PRO; PR:P22561; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P22561; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0035802; P:adrenal cortex formation; IMP:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; IMP:BHF-UCL.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; ISS:UniProtKB.
DR GO; GO:0060976; P:coronary vasculature development; TAS:DFLAT.
DR GO; GO:0060539; P:diaphragm development; IMP:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0032836; P:glomerular basement membrane development; ISO:MGI.
DR GO; GO:0032835; P:glomerulus development; IMP:UniProtKB.
DR GO; GO:0008406; P:gonad development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0030539; P:male genitalia development; IMP:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:1900200; P:mesenchymal cell apoptotic process involved in metanephros development; IMP:MGI.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:UniProtKB.
DR GO; GO:0001823; P:mesonephros development; IMP:MGI.
DR GO; GO:0072278; P:metanephric comma-shaped body morphogenesis; IEP:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; IMP:UniProtKB.
DR GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IMP:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000195; P:negative regulation of female gonad development; IMP:UniProtKB.
DR GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; IMP:MGI.
DR GO; GO:0072302; P:negative regulation of metanephric glomerular mesangial cell proliferation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0072015; P:podocyte development; IEP:UniProtKB.
DR GO; GO:0072112; P:podocyte differentiation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1905643; P:positive regulation of DNA methylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0060421; P:positive regulation of heart growth; IMP:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; IMP:UniProtKB.
DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; IMP:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072166; P:posterior mesonephric tubule development; IMP:UniProtKB.
DR GO; GO:0003156; P:regulation of animal organ formation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0007530; P:sex determination; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; IMP:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR GO; GO:0061032; P:visceral serous pericardium development; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW RNA editing; RNA-binding; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..449
FT /note="Wilms tumor protein homolog"
FT /id="PRO_0000047132"
FT ZN_FING 323..347
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..377
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..438
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 49..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..381
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250"
FT REGION 393..401
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250"
FT MOTIF 236..244
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT MOTIF 408..410
FT /note="KTS motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 424
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250"
FT SITE 430
FT /note="Important for interaction with target DNA"
FT /evidence="ECO:0000250"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19544"
FT VAR_SEQ 1
FT /note="M -> MDFLLSQEPASTCVPEPASQHTLRREPGCVQQPEQPGDRGPRSAWAK
FT SSAENPQDRRSGEPSASEPHLM (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_037585"
FT VAR_SEQ 250..266
FT /note="Missing (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1671709"
FT /id="VSP_006868"
FT VAR_SEQ 408..410
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:1671709"
FT /id="VSP_006869"
FT VARIANT 281
FT /note="L -> P (in RNA edited version)"
FT CONFLICT 33
FT /note="R -> A (in Ref. 2; CAM18169)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="I -> T (in Ref. 2; CAM18169)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..447
FT /note="HV -> QL (in Ref. 2; CAM18169)"
FT /evidence="ECO:0000305"
SQ 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
