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 25-MAY-2022, entry version 117. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 submandibular gland and 249 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 //