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   27-MAR-2024, entry version 127.
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   GlyGen; A2A884; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; A2A884; -.
DR   PhosphoSitePlus; A2A884; -.
DR   EPD; A2A884; -.
DR   jPOST; A2A884; -.
DR   MaxQB; A2A884; -.
DR   PaxDb; 10090-ENSMUSP00000101914; -.
DR   PeptideAtlas; A2A884; -.
DR   ProteomicsDB; 275143; -.
DR   Pumba; A2A884; -.
DR   Antibodypedia; 32189; 42 antibodies from 9 providers.
DR   DNASU; 16656; -.
DR   Ensembl; ENSMUST00000106307.9; ENSMUSP00000101914.3; ENSMUSG00000028634.18.
DR   Ensembl; ENSMUST00000166542.3; ENSMUSP00000130249.3; ENSMUSG00000028634.18.
DR   GeneID; 16656; -.
DR   KEGG; mmu:16656; -.
DR   UCSC; uc008una.1; mouse.
DR   AGR; MGI:106589; -.
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; EDRGPPN; -.
DR   OrthoDB; 3353821at2759; -.
DR   PhylomeDB; A2A884; -.
DR   TreeFam; TF331837; -.
DR   BioGRID-ORCS; 16656; 3 hits in 78 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 210 other cell types or tissues.
DR   ExpressionAtlas; A2A884; baseline and differential.
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 DNA-templated transcription; 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   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   InterPro; IPR034729; ZF_CCHC_HIVEP.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45944; SCHNURRI, ISOFORM F; 1.
DR   PANTHER; PTHR45944:SF5; TRANSCRIPTION FACTOR HIVEP3; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; A2A884; MM.
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
//