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Nuclear receptor corepressor 2 (N-CoR2) (Silencing mediator of retinoic acid and thyroid hormone receptor) (SMRT) (SMRTe) (T3 receptor-associating factor) (TRAC) (Thyroid-, retinoic-acid-receptor-associated corepressor)

 NCOR2_MOUSE             Reviewed;        2472 AA.
Q9WU42; E9Q9V0; Q9WU43; Q9WUC1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
10-OCT-2018, entry version 170.
RecName: Full=Nuclear receptor corepressor 2;
Short=N-CoR2;
AltName: Full=Silencing mediator of retinoic acid and thyroid hormone receptor;
Short=SMRT;
Short=SMRTe;
AltName: Full=T3 receptor-associating factor;
Short=TRAC;
AltName: Full=Thyroid-, retinoic-acid-receptor-associated corepressor;
Name=Ncor2; Synonyms=Smrt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Brain, and Spleen;
PubMed=10077563; DOI=10.1073/pnas.96.6.2639;
Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M.;
"Unique forms of human and mouse nuclear receptor corepressor SMRT.";
Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Embryo;
PubMed=10097068; DOI=10.1073/pnas.96.7.3519;
Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D.;
"SMRTe, a silencing mediator for retinoid and thyroid hormone
receptors-extended isoform that is more related to the nuclear
receptor corepressor.";
Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
INTERACTION WITH C1D.
PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G.,
Lazar M.A.;
"Cloning and characterization of a corepressor and potential component
of the nuclear hormone receptor repression complex.";
Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
[5]
INTERACTION WITH HDAC7.
PubMed=10640276;
Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
"Isolation of a novel histone deacetylase reveals that class I and
class II deacetylases promote SMRT-mediated repression.";
Genes Dev. 14:55-66(2000).
[6]
INTERACTION WITH CBFA2T3.
PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
Downing J.R., Meyers S., Hiebert S.W.;
"ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
with multiple histone deacetylases and binds mSin3A through its
oligomerization domain.";
Mol. Cell. Biol. 21:6470-6483(2001).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-2215, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
FUNCTION, AND INTERACTION WITH NR4A2.
PubMed=19144721; DOI=10.1242/dev.029769;
Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L.,
Burbach J.P., Smidt M.P.;
"Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
through release of SMRT-mediated repression.";
Development 136:531-540(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-549;
SER-550; SER-747; SER-750; THR-1350; SER-1565; SER-1749; SER-2004;
SER-2012; SER-2015; SER-2016; SER-2018; THR-2020; SER-2181 AND
SER-2215, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1983, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
INTERACTION WITH MECP2.
PubMed=23770565; DOI=10.1038/nn.3434;
Lyst M.J., Ekiert R., Ebert D.H., Merusi C., Nowak J., Selfridge J.,
Guy J., Kastan N.R., Robinson N.D., de Lima Alves F., Rappsilber J.,
Greenberg M.E., Bird A.;
"Rett syndrome mutations abolish the interaction of MeCP2 with the
NCoR/SMRT co-repressor.";
Nat. Neurosci. 16:898-902(2013).
[13]
DNA-BINDING, AND INTERACTION WITH BCL6.
PubMed=23455674; DOI=10.1038/ni.2543;
Huang C., Hatzi K., Melnick A.;
"Lineage-specific functions of Bcl-6 in immunity and inflammation are
mediated by distinct biochemical mechanisms.";
Nat. Immunol. 14:380-388(2013).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-18 AND ARG-1854, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Transcriptional corepressor. Mediates the
transcriptional repression activity of some nuclear receptors by
promoting chromatin condensation, thus preventing access of the
basal transcription. Isoform 1 and isoform 5 have different
affinities for different nuclear receptors. Involved in the
regulation BCL6-dependent of the germinal center (GC) reactions,
mainly through the control of the GC B-cells proliferation and
survival. Recruited by ZBTB7A to the androgen response
elements/ARE on target genes, negatively regulates androgen
receptor signaling and androgen-induced cell proliferation.
{ECO:0000250|UniProtKB:Q9Y618, ECO:0000269|PubMed:19144721}.
-!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B
and histone deacetylases HDAC1 and HDAC2. This complex associates
with the thyroid (TR) and the retinoid acid receptors (RAR) in the
absence of ligand, and may stabilize their interaction with TFIIB.
Interacts directly with RARA in the absence of ligand; the
interaction represses RARA activity. Interacts (isoform SMRT) with
HDAC10. Interacts with MINT. Component of the N-Cor repressor
complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R,
CORO2A and GPS2. Interacts with CBFA2T3 and ATXN1L. Interacts with
RARB; the interaction is weak and does not repress RARB
transactivational activity. Interacts with HDAC7 and C1D.
Interacts with NR4A2; this interaction increases in the absence of
PITX3. Interacts with BCL6 (via the BTB domain), required for BCL6
transcriptional repressor activity on a subset of target genes.
Forms ternary complexes with BCOR and BCL6 on target gene
promoters but, on enhancer elements, interacts with BCL6 and HDAC3
to repress proximal gene expression. May interact with DEAF1.
Interacts with RXRA. Interacts with MECP2. Interacts with ZBTB7A
(By similarity). Interacts with AR (By similarity).
{ECO:0000250|UniProtKB:Q9Y618, ECO:0000269|PubMed:10640276,
ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:19144721,
ECO:0000269|PubMed:23455674, ECO:0000269|PubMed:23770565,
ECO:0000269|PubMed:9405624}.
-!- INTERACTION:
P51608:MECP2 (xeno); NbExp=4; IntAct=EBI-6673326, EBI-1189067;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=Q9WU42-1; Sequence=Displayed;
Name=Beta;
IsoId=Q9WU42-2; Sequence=VSP_003414;
-!- TISSUE SPECIFICITY: Ubiquitous. Also widely expressed in early
embryos.
-!- DOMAIN: The N-terminal region contains repression functions that
are divided into three independent repression domains (RD1, RD2
and RD3). The C-terminal region contains the nuclear receptor-
interacting domains that are divided in two separate interaction
domains (ID1 and ID2).
-!- DOMAIN: The two interaction domains (ID) contain a conserved
sequence referred to as the CORNR box. This motif is required and
sufficient to permit binding to unligated TR and RARS. Sequences
flanking the CORNR box determine nuclear hormone receptor
specificity.
-!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors
family. {ECO:0000305}.
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EMBL; AF113001; AAD20944.1; -; mRNA.
EMBL; AF113002; AAD20945.1; -; mRNA.
EMBL; AF125671; AAD22972.1; -; mRNA.
EMBL; AC132118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC139377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS57382.1; -. [Q9WU42-2]
RefSeq; NP_001240833.1; NM_001253904.1.
RefSeq; NP_001240834.1; NM_001253905.1. [Q9WU42-2]
RefSeq; XP_011239133.1; XM_011240831.2. [Q9WU42-1]
UniGene; Mm.278646; -.
ProteinModelPortal; Q9WU42; -.
SMR; Q9WU42; -.
BioGrid; 203350; 12.
CORUM; Q9WU42; -.
DIP; DIP-42595N; -.
IntAct; Q9WU42; 7.
MINT; Q9WU42; -.
STRING; 10090.ENSMUSP00000083250; -.
iPTMnet; Q9WU42; -.
PhosphoSitePlus; Q9WU42; -.
EPD; Q9WU42; -.
PaxDb; Q9WU42; -.
PeptideAtlas; Q9WU42; -.
PRIDE; Q9WU42; -.
Ensembl; ENSMUST00000111394; ENSMUSP00000107025; ENSMUSG00000029478. [Q9WU42-2]
Ensembl; ENSMUST00000111398; ENSMUSP00000107029; ENSMUSG00000029478. [Q9WU42-1]
GeneID; 20602; -.
KEGG; mmu:20602; -.
UCSC; uc008zra.2; mouse. [Q9WU42-2]
CTD; 9612; -.
MGI; MGI:1337080; Ncor2.
eggNOG; KOG1878; Eukaryota.
eggNOG; ENOG410YDXP; LUCA.
GeneTree; ENSGT00840000129748; -.
HOGENOM; HOG000113746; -.
HOVERGEN; HBG052587; -.
InParanoid; Q9WU42; -.
KO; K06065; -.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-3214815; HDACs deacetylate histones.
Reactome; R-MMU-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
ChiTaRS; Ncor2; mouse.
PRO; PR:Q9WU42; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029478; Expressed in 291 organ(s), highest expression level in olfactory bulb.
CleanEx; MM_NCOR2; -.
ExpressionAtlas; Q9WU42; baseline and differential.
Genevisible; Q9WU42; MM.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
GO; GO:0016604; C:nuclear body; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0005112; F:Notch binding; ISO:MGI.
GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0042974; F:retinoic acid receptor binding; ISO:MGI.
GO; GO:0046965; F:retinoid X receptor binding; ISO:MGI.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:MGI.
GO; GO:0072365; P:regulation of cellular ketone metabolic process by negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0021537; P:telencephalon development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060509; P:type I pneumocyte differentiation; IMP:MGI.
GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
CDD; cd00167; SANT; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR031557; N-CoR_GPS2_interact.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
Pfam; PF15784; GPS2_interact; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF46689; SSF46689; 2.
PROSITE; PS51293; SANT; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Repressor; Transcription; Transcription regulation.
CHAIN 1 2472 Nuclear receptor corepressor 2.
/FTId=PRO_0000055623.
DOMAIN 427 478 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 606 657 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 254 312 Interaction with SIN3A/B. {ECO:0000250}.
REGION 2086 2090 Required for interaction with RARA in the
absence of its ligand. {ECO:0000250}.
COILED 165 207 {ECO:0000255}.
COILED 492 560 {ECO:0000255}.
COILED 658 682 {ECO:0000255}.
MOTIF 2094 2098 CORNR box of ID1.
MOTIF 2296 2300 CORNR box of ID2.
COMPBIAS 494 507 Poly-Gln.
COMPBIAS 775 804 Pro-rich.
COMPBIAS 989 999 Pro-rich.
COMPBIAS 1351 1357 Pro-rich.
COMPBIAS 1615 1619 Poly-Ala.
COMPBIAS 2434 2437 Poly-Pro.
MOD_RES 18 18 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 493 493 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 549 549 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 550 550 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 747 747 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 878 878 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 938 938 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 945 945 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 958 958 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1181 1181 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1209 1209 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1220 1220 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1350 1350 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1449 1449 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1509 1509 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1565 1565 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1624 1624 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1746 1746 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1749 1749 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1819 1819 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1854 1854 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1920 1920 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1963 1963 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 1983 1983 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2004 2004 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2012 2012 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2015 2015 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2016 2016 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2018 2018 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2020 2020 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2035 2035 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 2161 2161 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
MOD_RES 2181 2181 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 2215 2215 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2371 2371 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y618}.
VAR_SEQ 36 254 Missing (in isoform Beta).
{ECO:0000303|PubMed:10077563}.
/FTId=VSP_003414.
CONFLICT 176 176 M -> RL (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 396 402 PPMLYDA -> RHVVRR (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 555 555 D -> H (in Ref. 1; AAD20944).
{ECO:0000305}.
CONFLICT 756 756 T -> M (in Ref. 1; AAD20944).
{ECO:0000305}.
CONFLICT 785 785 V -> A (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 806 846 PSPAAPPATVDKDEQEAPAAPAPQTEDAKEQKSEAEEIDVG
-> HHLPHPRLLWTRMNKKPRLLQLPRQRMPRSRSLRPRRS
MWE (in Ref. 1; AAD20944/AAD20945).
{ECO:0000305}.
CONFLICT 856 856 E -> K (in Ref. 1; AAD20945).
{ECO:0000305}.
CONFLICT 859 859 E -> K (in Ref. 1; AAD20945).
{ECO:0000305}.
CONFLICT 867 867 E -> K (in Ref. 1; AAD20945).
{ECO:0000305}.
CONFLICT 895 895 E -> K (in Ref. 1; AAD20945).
{ECO:0000305}.
CONFLICT 916 916 S -> F (in Ref. 1; AAD20944).
{ECO:0000305}.
CONFLICT 975 975 I -> IQ (in Ref. 1; AAD20944).
{ECO:0000305}.
CONFLICT 1046 1063 PKLPTEPPRWSSGLPFPI -> QSYRLSPHAGHRLPSH
(in Ref. 2; AAD22972). {ECO:0000305}.
CONFLICT 1073 1080 PHAADPSA -> TRADPL (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1133 1133 Missing (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1149 1149 Missing (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1157 1157 G -> E (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1172 1201 GSATSGSITKGLPSTRAADGPSYRGSITHG -> APPPVEA
SPRASQYPGCRRPQLQRLYHPR (in Ref. 2;
AAD22972). {ECO:0000305}.
CONFLICT 1696 1696 A -> S (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1855 1857 Missing (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1909 1909 P -> A (in Ref. 1; AAD20944/AAD20945).
{ECO:0000305}.
CONFLICT 1913 1913 A -> G (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1923 1923 A -> G (in Ref. 1; AAD20944/AAD20945).
{ECO:0000305}.
CONFLICT 1956 1956 N -> S (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 1968 1968 A -> G (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 2195 2196 TA -> AV (in Ref. 2; AAD22972).
{ECO:0000305}.
CONFLICT 2213 2214 SK -> LE (in Ref. 1; AAD20944).
{ECO:0000305}.
CONFLICT 2224 2224 A -> T (in Ref. 1; AAD20944).
{ECO:0000305}.
SEQUENCE 2472 AA; 269807 MW; 8068020DF0AAB9B7 CRC64;
MSGSTQPVAQ TWRAAEPRYP PHGISYPVQI ARSHTDVGLL EYQHHPRDYT SHLSPGSIIQ
PQRRRPSLLS EFQPGSERSQ ELHLRPESRT FLPELGKPDI EFTESKRPRL ELLPDTLLRP
SPLLATGQPS GSEDLTKDRS LAGKLEPVSP PSPPHADPEL ELAPSRLSKE ELIQNMDRVD
REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA
AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQRFCQ
RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG
LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMDDPM
KVYKDRQVTN MWSEQERDTF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK
SLVRRSYRRR GKSQQQQQQQ QQQQQQQMAR SSQEEKEEKE KEKEADKEEE KQDAENEKEE
LSKEKTDDTS GEDNDEKEAV ASKGRKTANS QGRRKGRITR SMANEANHEE TATPQQSSEL
ASMEMNESSR WTEEEMETAK KGLLEHGRNW SAIARMVGSK TVSQCKNFYF NYKKRQNLDE
ILQQHKLKME KERNARRKKK KTPAAASEET AFPPAAEDEE MEASGASANE EELAEEAEAS
QASGNEVPRV GECSGPAAVN NSSDTESVPS PRSEATKDTG PKPTGTEALP AATQPPVPPP
EEPAVAPAEP SPVPDASGPP SPEPSPSPAA PPATVDKDEQ EAPAAPAPQT EDAKEQKSEA
EEIDVGKPEE PEASEEPPES VKSDHKEETE EEPEDKAKGT EAIETVSEAP LKVEEAGSKA
AVTKGSSSGA TQDSDSSATC SADEVDEPEG GDKGRLLSPR PSLLTPAGDP RASTSPQKPL
DLKQLKQRAA AIPPIVTKVH EPPREDTVPP KPVPPVPPPT QHLQPEGDVS QQSGGSPRGK
SRSPVPPAEK EAEKPAFFPA FPTEGPKLPT EPPRWSSGLP FPIPPREVIK TSPHAADPSA
FSYTPPGHPL PLGLHDSARP VLPRPPISNP PPLISSAKHP GVLERQLGAI SQQGMSVQLR
VPHSEHAKAP MGPLTMGLPL AVDPKKLGTA LGSATSGSIT KGLPSTRAAD GPSYRGSITH
GTPADVLYKG TISRIVGEDS PSRLDRARED TLPKGHVIYE GKKGHVLSYE GGMSVSQCSK
EDGRSSSGPP HETAAPKRTY DMMEGRVGRT VTSASIEGLM GRAIPEQHSP HLKEQHHIRG
SITQGIPRSY VEAQEDYLRR EAKLLKREGT PPPPPPPRDL TETYKPRPLD PLGPLKLKPT
HEGVVATVKE AGRSIHEIPR EELRRTPELP LAPRPLKEGS ITQGTPLKYD SGAPSTGTKK
HDVRSIIGSP GRPFPALHPL DIMADARALE RACYEESLKS RSGTSSGAGG SITRGAPVVV
PELGKPRQSP LTYEDHGAPF TSHLPRGSPV TTREPTPRLQ EGSLLSSKAS QDRKLTSTPR
EIAKSPHSTV PEHHPHPISP YEHLLRGVTG VDLYRGHIPL AFDPTSIPRG IPLEAAAAAY
YLPRHLAPSP TYPHLYPPYL IRGYPDTAAL ENRQTIINDY ITSQQMHHNA ASAMAQRADM
LRGLSPRESS LALNYAAGPR GIIDLSQVPH LPVLVPPTPG TPATAIDRLA YLPTAPPPFS
SRHSSSPLSP GGPTHLAKPT ATSSSERERE RERERDKSIL TSTTTVEHAP IWRPGTEQSS
GAGGSSRPAS HTHQHSPISP RTQDALQQRP SVLHNTSMKG VVTSVEPGTP TVLRWARSTS
TSSPVRPAAT FPPATHCPLG GTLEGVYPTL MEPVLLPKET SRVARPERPR VDAGHAFLTK
PPAREPASSP SKSSEPRSLA PPSSSHTAIA RTPAKNLAPH HASPDPPAPT SASDLHREKT
QSKPFSIQEL ELRSLGYHSG AGYSPDGVEP ISPVSSPSLT HDKGLSKPLE ELEKSHLEGE
LRHKQPGPMK LSAEAAHLPH LRPLPESQPS SSPLLQTAPG IKGHQRVVTL AQHISEVITQ
DYTRHHPQQL SGPLPAPLYS FPGASCPVLD LRRPPSDLYL PPPDHGTPAR GSPHSEGGKR
SPEPSKTSVL GSSEDAIEPV SPPEGMTEPG HARSTAYPLL YRDGEQGEPR MGSKSPGNTS
QPPAFFSKLT ESNSAMVKSK KQEINKKLNT HNRNEPEYNI GQPGTEIFNM PAITGAGLMT
CRSQAVQEHA STNMGLEAII RKALMGKYDQ WEEPPPLGAN AFNPLNASAS LPAAAMPITT
ADGRSDHALT SPGGGGKAKV SGRPSSRKAK SPAPGLASGD RPPSVSSVHS EGDCNRRTPL
TNRVWEDRPS SAGSTPFPYN PLIMRLQAGV MASPPPPGLA AGSGPLAGPH HAWDEEPKPL
LCSQYETLSD SE


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