ZEP3_MOUSE
ID ZEP3_MOUSE Reviewed; 2348 AA.
AC A2A884; A2MZW0; Q69ZG6; Q6SNP9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcription factor HIVEP3;
DE AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3 homolog;
DE AltName: Full=KB-binding and recognition component;
DE AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
DE AltName: Full=Kappa-binding protein 1;
DE Short=KBP-1;
DE AltName: Full=Recombinant component;
DE AltName: Full=Schnurri-3;
DE AltName: Full=Zinc finger protein ZAS3;
GN Name=Hivep3; Synonyms=KBP1, Kiaa1555, Krc, Rc, shn3, Zas3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-2341, DOMAIN, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8812474; DOI=10.1006/geno.1996.0380;
RA Wu L.-C., Liu Y., Strandtmann J., Mak C.-H., Lee B., Li Z., Yu C.Y.;
RT "The mouse DNA binding protein Rc for the kappa B motif of transcription
RT and for the V(D)J recombination signal sequences contains composite DNA-
RT protein interaction domains and belongs to a new family of large
RT transcriptional proteins.";
RL Genomics 35:415-424(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1281-2348.
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1497-2295, FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DOMAIN, AND REPEAT.
RX PubMed=8255760; DOI=10.1093/nar/21.22.5067;
RA Wu L.-C., Mak C.-H., Dear N., Boehm T., Foroni L., Rabbitts T.H.;
RT "Molecular cloning of a zinc finger protein which binds to the heptamer of
RT the signal sequence for V(D)J recombination.";
RL Nucleic Acids Res. 21:5067-5073(1993).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=9862992; DOI=10.1093/nar/27.2.643;
RA Bachmeyer C., Mak C.H., Yu C.Y., Wu L.-C.;
RT "Regulation by phosphorylation of the zinc finger protein KRC that binds
RT the kappaB motif and V(D)J recombination signal sequences.";
RL Nucleic Acids Res. 27:643-648(1999).
RN [6]
RP FUNCTION.
RX PubMed=11035930; DOI=10.1006/excr.2000.5029;
RA Allen C.E., Wu L.-C.;
RT "Downregulation of KRC induces proliferation, anchorage independence, and
RT mitotic cell death in HeLa cells.";
RL Exp. Cell Res. 260:346-356(2000).
RN [7]
RP FUNCTION.
RX PubMed=10625627; DOI=10.1074/jbc.275.2.913;
RA Hjelmsoe I., Allen C.E., Cohn M.A., Tulchinsky E.M., Wu L.-C.;
RT "The kappaB and V(D)J recombination signal sequence binding protein KRC
RT regulates transcription of the mouse metastasis-associated gene
RT S100A4/mts1.";
RL J. Biol. Chem. 275:913-920(2000).
RN [8]
RP FUNCTION, AND DOMAIN ZAS.
RX PubMed=12193271; DOI=10.1186/1471-2172-3-10;
RA Allen C.E., Mak C.-H., Wu L.-C.;
RT "The kappa B transcriptional enhancer motif and signal sequences of V(D)J
RT recombination are targets for the zinc finger protein HIVEP3/KRC: a site
RT selection amplification binding study.";
RL BMC Immunol. 3:10-10(2002).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TRAF1 AND TRAF2, AND
RP REGION.
RX PubMed=11804591; DOI=10.1016/s1097-2765(01)00434-8;
RA Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
RT "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-
RT driven responses and interacts with TRAF2.";
RL Mol. Cell 9:121-131(2002).
RN [10]
RP FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12001065; DOI=10.1002/gene.10084;
RA Hicar M.D., Robinson M.L., Wu L.-C.;
RT "Embryonic expression and regulation of the large zinc finger protein
RT KRC.";
RL Genesis 33:8-20(2002).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14530385; DOI=10.1073/pnas.2133048100;
RA Hong J.W., Allen C.E., Wu L.-C.;
RT "Inhibition of NF-kappaB by ZAS3, a zinc-finger protein that also binds to
RT the kappaB motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12301-12306(2003).
RN [12]
RP FUNCTION, INTERACTION WITH JUN, AND INDUCTION.
RX PubMed=14707112; DOI=10.1084/jem.20030421;
RA Oukka M., Wein M.N., Glimcher L.H.;
RT "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T
RT cells.";
RL J. Exp. Med. 199:15-24(2004).
RN [13]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=15627499; DOI=10.1016/j.bbaexp.2004.10.004;
RA Hong J.-W., Wu L.-C.;
RT "Structural characterization of the gene encoding the large zinc finger
RT protein ZAS3: implication to the origin of multiple promoters in eukaryotic
RT genes.";
RL Biochim. Biophys. Acta 1681:74-87(2005).
RN [14]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH RUNX2 AND
RP WWP1.
RX PubMed=16728642; DOI=10.1126/science.1126313;
RA Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
RA Glimcher L.H.;
RT "Regulation of adult bone mass by the zinc finger adapter protein Schnurri-
RT 3.";
RL Science 312:1223-1227(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays a role of transcription factor; binds to recognition
CC signal sequences (Rss heptamer) for somatic recombination of
CC immunoglobulin and T-cell receptor gene segments; Binds also to the
CC kappa-B motif of gene such as S100A4, involved in cell progression and
CC differentiation. Kappa-B motif is a gene regulatory element found in
CC promoters and enhancers of genes involved in immunity, inflammation,
CC and growth and that responds to viral antigens, mitogens, and
CC cytokines. Involvement of HIVEP3 in cell growth is strengthened by the
CC fact that its down-regulation promotes cell cycle progression with
CC ultimate formation of multinucleated giant cells. Strongly inhibits
CC TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor
CC NF-kappa-B by several mechanisms: as transcription factor, by competing
CC for Kappa-B motif and by repressing transcription in the nucleus;
CC through a non transcriptional process, by inhibiting nuclear
CC translocation of RELA by association with TRAF2, an adapter molecule in
CC the tumor necrosis factor signaling, which blocks the formation of IKK
CC complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-
CC mediated and c-Jun N-terminal kinase/JNK-mediated responses that
CC include apoptosis and pro-inflammatory cytokine gene expression.
CC Positively regulates the expression of IL2 in T-cell. Essential
CC regulator of adult bone formation. {ECO:0000269|PubMed:10625627,
CC ECO:0000269|PubMed:11035930, ECO:0000269|PubMed:11804591,
CC ECO:0000269|PubMed:12001065, ECO:0000269|PubMed:12193271,
CC ECO:0000269|PubMed:14530385, ECO:0000269|PubMed:14707112,
CC ECO:0000269|PubMed:8255760, ECO:0000269|PubMed:8812474}.
CC -!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a
CC multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1.
CC {ECO:0000269|PubMed:11804591, ECO:0000269|PubMed:14707112,
CC ECO:0000269|PubMed:16728642}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804591}. Nucleus
CC {ECO:0000269|PubMed:11804591}.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages, lymphocytes, brain,
CC thymus, spleen and bone marrow. Expressed in osteoblasts, whole bone
CC and, to a lesser extent, in osteoclasts. {ECO:0000269|PubMed:14530385,
CC ECO:0000269|PubMed:16728642, ECO:0000269|PubMed:8255760,
CC ECO:0000269|PubMed:8812474}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the thymus with increasing level,
CC approximately 4-fold, from 15.5 dpc to 16.5 dpc, constant level from
CC 16.5 dpc to birth, then decrease to a low level by P30. Expressed at
CC 13.5 dpc in the dorsal root ganglia of the peripheral nervous system
CC and the trigeminal ganglion of the metencephalon and at relatively low
CC levels in the cerebral cortex; no significant expression was observed
CC prior to 13.5 dpc. Expressed in the spinal cord at 19 dpc, but weakly
CC detected in the lung and the liver. {ECO:0000269|PubMed:12001065,
CC ECO:0000269|PubMed:8255760}.
CC -!- INDUCTION: Upon CD3/CD28 stimulation in CD4 T-cells. Induced by LPS in
CC pre-B-cells. {ECO:0000269|PubMed:12001065,
CC ECO:0000269|PubMed:14707112}.
CC -!- DOMAIN: ZAS2 domain binds DNA as dimers, tetramers, and multiple of
CC tetramers and readily forms highly ordered DNA-protein structures.
CC {ECO:0000269|PubMed:12193271, ECO:0000269|PubMed:8255760,
CC ECO:0000269|PubMed:8812474}.
CC -!- PTM: Phosphorylated on threonine and serine residues. Phosphorylation
CC by cyclin-dependent kinase CDK1 decreases HIVEP3 DNA binding affinity,
CC and by epidermal growth factor receptor kinase increases its DNA
CC binding affinity. {ECO:0000269|PubMed:9862992}.
CC -!- DISRUPTION PHENOTYPE: Mice display adult-onset osteosclerosis with
CC increased bone mass due to increased osteoblast activity; the
CC osteoblasts contain elevated levels of Runx2.
CC {ECO:0000269|PubMed:16728642}.
CC -!- MISCELLANEOUS: Hivep3 gene expression is probably controlled by a
CC combination of differential promoter usage, alternative splicing, and
CC possible intergenic splicing.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA40039.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAR88090.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL607142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY454345; AAR88090.1; ALT_FRAME; mRNA.
DR EMBL; AK173200; BAD32478.1; -; mRNA.
DR EMBL; L07911; AAA40039.1; ALT_SEQ; mRNA.
DR CCDS; CCDS38863.1; -.
DR PIR; S41479; S41479.
DR PIR; T42717; T42717.
DR RefSeq; NP_034787.2; NM_010657.3.
DR RefSeq; XP_006502878.1; XM_006502815.2.
DR RefSeq; XP_006502879.1; XM_006502816.2.
DR RefSeq; XP_006502880.1; XM_006502817.2.
DR RefSeq; XP_011238754.1; XM_011240452.1.
DR RefSeq; XP_011238755.1; XM_011240453.1.
DR AlphaFoldDB; A2A884; -.
DR SMR; A2A884; -.
DR BioGRID; 201013; 1.
DR IntAct; A2A884; 1.
DR MINT; A2A884; -.
DR STRING; 10090.ENSMUSP00000101914; -.
DR iPTMnet; A2A884; -.
DR PhosphoSitePlus; A2A884; -.
DR EPD; A2A884; -.
DR jPOST; A2A884; -.
DR MaxQB; A2A884; -.
DR PaxDb; A2A884; -.
DR PeptideAtlas; A2A884; -.
DR PRIDE; A2A884; -.
DR ProteomicsDB; 275143; -.
DR Antibodypedia; 32189; 28 antibodies from 8 providers.
DR DNASU; 16656; -.
DR Ensembl; ENSMUST00000106307; ENSMUSP00000101914; ENSMUSG00000028634.
DR Ensembl; ENSMUST00000166542; ENSMUSP00000130249; ENSMUSG00000028634.
DR GeneID; 16656; -.
DR KEGG; mmu:16656; -.
DR UCSC; uc008una.1; mouse.
DR CTD; 59269; -.
DR MGI; MGI:106589; Hivep3.
DR VEuPathDB; HostDB:ENSMUSG00000028634; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157218; -.
DR HOGENOM; CLU_000719_1_0_1; -.
DR InParanoid; A2A884; -.
DR OMA; QEKTGQP; -.
DR OrthoDB; 212048at2759; -.
DR PhylomeDB; A2A884; -.
DR TreeFam; TF331837; -.
DR BioGRID-ORCS; 16656; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Hivep3; mouse.
DR PRO; PR:A2A884; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A884; protein.
DR Bgee; ENSMUSG00000028634; Expressed in gastrula and 206 other tissues.
DR ExpressionAtlas; A2A884; baseline and differential.
DR Genevisible; A2A884; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion 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:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR InterPro; IPR034729; ZF_CCHC_HIVEP.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2348
FT /note="Transcription factor HIVEP3"
FT /id="PRO_0000331628"
FT REPEAT 1897..1900
FT /note="1"
FT /evidence="ECO:0000269|PubMed:8255760"
FT REPEAT 1927..1930
FT /note="2"
FT /evidence="ECO:0000269|PubMed:8255760"
FT REPEAT 1933..1936
FT /note="3"
FT /evidence="ECO:0000269|PubMed:8255760"
FT REPEAT 1961..1964
FT /note="4"
FT /evidence="ECO:0000269|PubMed:8255760"
FT REPEAT 2024..2027
FT /note="5"
FT /evidence="ECO:0000269|PubMed:8255760"
FT ZN_FING 185..207
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..235
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 633..663
FT /note="CCHC HIVEP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01154"
FT ZN_FING 1720..1742
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1748..1772
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..235
FT /note="ZAS1"
FT REGION 204..1055
FT /note="No DNA binding activity or transactivation activity,
FT but complete prevention of TRAF-dependent NF-Kappa-B
FT activation; associates with TRAF2 and JUN"
FT REGION 239..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..280
FT /note="Acidic 1"
FT REGION 475..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..865
FT /note="Acidic 2"
FT REGION 1229..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1772
FT /note="ZAS2"
FT REGION 1783..1841
FT /note="Acidic 3"
FT REGION 1786..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2009..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2148
FT /note="5 X 4 AA tandem repeats of [ST]-P-X-[RK]"
FT REGION 2184..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2284..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1409..1433
FT /evidence="ECO:0000255"
FT MOTIF 885..891
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1842
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1938..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 131
FT /note="L -> S (in Ref. 2; AAR88090)"
FT /evidence="ECO:0000305"
FT CONFLICT 583..584
FT /note="QP -> HA (in Ref. 2; AAR88090)"
FT /evidence="ECO:0000305"
FT CONFLICT 721..722
FT /note="GS -> AC (in Ref. 2; AAR88090)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="S -> T (in Ref. 2; AAR88090)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="E -> Q (in Ref. 2; AAR88090)"
FT /evidence="ECO:0000305"
FT CONFLICT 1507
FT /note="K -> F (in Ref. 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1660
FT /note="L -> V (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1880
FT /note="Q -> E (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1944
FT /note="L -> V (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1994
FT /note="L -> P (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 1998
FT /note="C -> R (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 2014
FT /note="R -> P (in Ref. 4; AAA40039)"
FT /evidence="ECO:0000305"
FT CONFLICT 2105
FT /note="A -> G (in Ref. 2; AAR88090 and 4; AAA40039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2348 AA; 253413 MW; E226133774AD50C8 CRC64;
MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT QELLATQPFS
GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP GKPEHLLEGS TWQLVDPMRP
GPSGSFVAPG LHPQSQLLPS HASILPPEEL PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ
KPGKYICQYC SRPCAKPSVL QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK
AGLASGSSSE MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL
SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT HTIKQKLALR
LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP NTNAKSYAEI IFGKCGRIGQ
RTSMLASTST QPLLPLSSED KPSLVPLSVP RTQVIEHITK LITINEAVVD TSEIDSVKPR
RSSLTRRSSV ESPKSSLYRD SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA
CTISTHHHTF RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG
PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN YEAHKKYYCS
ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT PLRKRRKEKS LGDEEEPPAF
GSPGPSETAH NRPLGSTKSP AEASKSAPSL EGPTSFQPRT PKPGAGSEPG KERRTMSKEI
SVIQHTSSFE KSDPPEQPSG LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI
LVTEEPDRPD TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG
ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS KTLGSHMLTV
PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL SPTGPSLAVP AAPPPPAAPP
ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE SSEEPAASKP STKSSVPQIS VGTTQGGPSG
GKSQMQDRPP LGSSPPYTEA LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM
AGLLSSPYSM PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC
PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST EYSSDIQLPP
VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS YGSAMYTTLS QILVTQSPGS
PASTALTKYE EPSSKSMTVC EADVYEAEPG PSSISKEQNR GYQTPYLRVP ERKGTSLSSE
GILSLEGCSS TASGSKRVLS PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT
STEDRKKTEK PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE
YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL QEGTDSKKVL
QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS LYNPNLPGVS TKAALSLLRS
KQKVSKETYT MATAPHPEAG RLVPSNSRKP RMTEVHLPSL VSPESQKDPA RVEKEEKQGK
AEEGTPTSKR GEPARVKIFE GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR
THTDVRPYVC KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE
GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA PPCLPPTLQE
NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR GTQGLPRLGL APLEKDMSSA
PSPKATSPRR PWSPSKEAGS RPSLTRKHSL TKNDSSPQQC SPAREAQASV TSTPGPQMGP
GRDLGPHLCG SPRLELSCLT PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT
VLPGKWALAG PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP
SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP IGGIQMVQAR
PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP TESPSASVSP VAKVSKFTLS
SELEEERTGR GPGRPPDWEP HRAEAPPGPM GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL
ANLKASSFPP LDRSSSMDCL AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP
KGSGPPSI
