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Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5)

 BAZ2A_MOUSE             Reviewed;        1889 AA.
Q91YE5; Q3U235; Q80U42;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 2.
30-AUG-2017, entry version 141.
RecName: Full=Bromodomain adjacent to zinc finger domain protein 2A;
AltName: Full=Transcription termination factor I-interacting protein 5;
Short=TTF-I-interacting protein 5;
Short=Tip5;
Name=Baz2a; Synonyms=Kiaa0314, Tip5;
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 [LARGE SCALE MRNA] OF 1-703 (ISOFORM 3).
STRAIN=NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 40-1889 (ISOFORM 1), FUNCTION,
SUBCELLULAR LOCATION, AND INTERACTION WITH SMARCA5 AND TTF1.
PubMed=11532953; DOI=10.1093/emboj/20.17.4892;
Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R.,
Laengst G., Grummt I.;
"NoRC -- a novel member of mammalian ISWI-containing chromatin
remodeling machines.";
EMBO J. 20:4892-4900(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1889 (ISOFORM 2).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND SIN3A, AND
MUTAGENESIS OF TYR-1814.
PubMed=12198165; DOI=10.1093/emboj/cdf460;
Zhou Y., Santoro R., Grummt I.;
"The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
gene promoter and represses RNA polymerase I transcription.";
EMBO J. 21:4632-4640(2002).
[5]
INTERACTION WITH TTF1.
PubMed=15292447; DOI=10.1093/nar/gkh732;
Nemeth A., Strohner R., Grummt I., Laengst G.;
"The chromatin remodeling complex NoRC and TTF-I cooperate in the
regulation of the mammalian rRNA genes in vivo.";
Nucleic Acids Res. 32:4091-4099(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN BROMO AND PHD-TYPE ZINC-FINGER,
AND INTERACTION WITH DNMT1; DNM3B; HDAC1 AND SMARCA5.
PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
Zhou Y., Grummt I.;
"The PHD finger/bromodomain of NoRC interacts with acetylated histone
H4K16 and is sufficient for rDNA silencing.";
Curr. Biol. 15:1434-1438(2005).
[7]
RNA-BINDING, DOMAIN MBD, AND MUTAGENESIS OF 570-TRP-TYR-571.
PubMed=16678107; DOI=10.1016/j.molcel.2006.03.028;
Mayer C., Schmitz K.-M., Li J., Grummt I., Santoro R.;
"Intergenic transcripts regulate the epigenetic state of rRNA genes.";
Mol. Cell 22:351-361(2006).
[8]
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).
[9]
SUBCELLULAR LOCATION, AND RNA-BINDING.
PubMed=18600236; DOI=10.1038/embor.2008.109;
Mayer C., Neubert M., Grummt I.;
"The structure of NoRC-associated RNA is crucial for targeting the
chromatin remodelling complex NoRC to the nucleolus.";
EMBO Rep. 9:774-780(2008).
[10]
ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 570-TRP-TYR-571 AND LYS-672.
PubMed=19578370; DOI=10.1038/ncb1914;
Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.;
"Reversible acetylation of the chromatin remodelling complex NoRC is
required for non-coding RNA-dependent silencing.";
Nat. Cell Biol. 11:1010-1016(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1042; SER-1174;
SER-1374; SER-1377; SER-1383 AND THR-1738, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, 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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, 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).
-!- FUNCTION: Essential component of the NoRC (nucleolar remodeling
complex) complex, a complex that mediates silencing of a fraction
of rDNA by recruiting histone-modifying enzymes and DNA
methyltransferases, leading to heterochromatin formation and
transcriptional silencing. In the complex, it plays a central role
by being recruited to rDNA and by targeting chromatin modifying
enzymes such as HDAC1, leading to repress RNA polymerase I
transcription. Recruited to rDNA via its interaction with TTF1 and
its ability to recognize and bind histone H4 acetylated on 'Lys-
16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac
but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs
that are complementary in sequence to the rDNA promoter; pRNA-
binding is required for heterochromatin formation and rDNA
silencing. {ECO:0000269|PubMed:11532953,
ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498}.
-!- SUBUNIT: Component of the NoRC complex, at least composed of
SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for
recruitment of the NoRC complex to rDNA. Interacts with DNMT1,
DNM3B, HDAC1 and SIN3A. Interacts with BEND3 and USP21 (By
similarity). {ECO:0000250|UniProtKB:Q9UIF9,
ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165,
ECO:0000269|PubMed:15292447, ECO:0000269|PubMed:16085498}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165,
ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:18600236,
ECO:0000269|PubMed:19578370}. Note=Colocalizes with the basal RNA
polymerase I transcription factor UBF in the nucleolus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q91YE5-1; Sequence=Displayed;
Name=2;
IsoId=Q91YE5-2; Sequence=VSP_037963;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q91YE5-3; Sequence=VSP_037962;
Note=No experimental confirmation available.;
-!- DOMAIN: The bromo domain and the PHD-type zinc finger recognize
and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2
domains play a central role in the recritment of chromatin
silencing proteins such as DNMT1, DNMT3B and HDAC1.
-!- DOMAIN: The MBD (methyl-CpG-binding) domain, also named TAM
domain, specifically recognizes and binds a conserved stem-loop
structure the association within pRNA. Binding to pRNA induces a
conformational change of BAZ2A/TIP5 and is essential for targeting
the NoRC complex to the nucleolus.
-!- PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its
stabilization. {ECO:0000250|UniProtKB:Q9UIF9}.
-!- PTM: Acetylation at Lys-672 by KAT8/MOF promotes its dissociation
from pRNA, affecting heterochromatin formation, nucleosome
positioning and rDNA silencing. Deacetylation by SIRT1 in late S
phase enhances pRNA-binding, allowing de novo DNA methylation and
heterochromatin formation. Acetylation is high during S phase and
declines to background levels in late S phase when the silent
copies of rRNA genes are replicated.
{ECO:0000269|PubMed:19578370}.
-!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
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EMBL; AK155523; BAE33307.1; -; mRNA.
EMBL; AJ309544; CAC69992.1; -; mRNA.
EMBL; AK122243; BAC65525.1; -; mRNA.
UniGene; Mm.252213; -.
ProteinModelPortal; Q91YE5; -.
SMR; Q91YE5; -.
IntAct; Q91YE5; 1.
STRING; 10090.ENSMUSP00000044359; -.
iPTMnet; Q91YE5; -.
PhosphoSitePlus; Q91YE5; -.
PaxDb; Q91YE5; -.
PRIDE; Q91YE5; -.
MGI; MGI:2151152; Baz2a.
eggNOG; KOG1245; Eukaryota.
eggNOG; COG5076; LUCA.
HOGENOM; HOG000169644; -.
HOVERGEN; HBG107494; -.
InParanoid; Q91YE5; -.
PhylomeDB; Q91YE5; -.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-573389; NoRC negatively regulates rRNA expression.
ChiTaRS; Baz2a; mouse.
PRO; PR:Q91YE5; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_BAZ2A; -.
GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042393; F:histone binding; ISO:MGI.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; ISO:MGI.
GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
GO; GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
GO; GO:0070869; P:heterochromatin assembly involved in chromatin silencing; IDA:MGI.
GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
GO; GO:0051567; P:histone H3-K9 methylation; IDA:MGI.
GO; GO:0070933; P:histone H4 deacetylation; IDA:MGI.
GO; GO:0034770; P:histone H4-K20 methylation; IDA:MGI.
GO; GO:0016479; P:negative regulation of transcription from RNA polymerase I promoter; IMP:CACAO.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR018501; DDT_dom.
InterPro; IPR016177; DNA-bd_dom.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR028940; TIP5.
InterPro; IPR028942; WHIM1_dom.
InterPro; IPR028941; WHIM2_dom.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR22880:SF191; PTHR22880:SF191; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF02791; DDT; 1.
Pfam; PF01429; MBD; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF15612; WHIM1; 1.
Pfam; PF15613; WSD; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00384; AT_hook; 4.
SMART; SM00297; BROMO; 1.
SMART; SM00571; DDT; 1.
SMART; SM00391; MBD; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF54171; SSF54171; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50827; DDT; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
Coiled coil; Complete proteome; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; RNA-binding; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1889 Bromodomain adjacent to zinc finger
domain protein 2A.
/FTId=PRO_0000211173.
DOMAIN 538 609 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
DOMAIN 839 904 DDT. {ECO:0000255|PROSITE-
ProRule:PRU00063}.
DOMAIN 1794 1864 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DNA_BIND 641 653 A.T hook 1.
DNA_BIND 662 674 A.T hook 2.
DNA_BIND 1176 1188 A.T hook 3.
DNA_BIND 1390 1402 A.T hook 4.
ZN_FING 1662 1712 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
COILED 686 813 {ECO:0000255}.
COMPBIAS 652 777 Lys-rich.
COMPBIAS 1045 1051 Poly-Glu.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 501 501 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 540 540 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 672 672 N6-acetyllysine; by KAT8.
{ECO:0000269|PubMed:19578370}.
MOD_RES 790 790 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1174 1174 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1374 1374 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1377 1377 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1383 1383 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1545 1545 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 1733 1733 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 1738 1738 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1755 1755 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
MOD_RES 1767 1767 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIF9}.
CROSSLNK 857 857 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIF9}.
CROSSLNK 1141 1141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIF9}.
CROSSLNK 1163 1163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIF9}.
CROSSLNK 1662 1662 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIF9}.
CROSSLNK 1695 1695 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIF9}.
VAR_SEQ 305 305 L -> LA (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_037962.
VAR_SEQ 1712 1712 Missing (in isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_037963.
MUTAGEN 570 571 WY->GA: Impairs interaction with pRNA and
heterochromatin formation but retains
ability to trigger DNA methylation and
silence rDNA transcription.
{ECO:0000269|PubMed:16678107,
ECO:0000269|PubMed:19578370}.
MUTAGEN 672 672 K->R: Abolishes acetylation by KAT8/MOF,
leading to increase interaction with TTF1
and association with pRNA.
{ECO:0000269|PubMed:19578370}.
MUTAGEN 1814 1814 Y->F: Impairs binding to chromatin.
{ECO:0000269|PubMed:12198165}.
CONFLICT 41 42 NF -> SL (in Ref. 1; CAC69992).
{ECO:0000305}.
SEQUENCE 1889 AA; 209618 MW; 14E7A817877EB114 CRC64;
MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST
VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS ANPGNNLKDP PLLSQFPGGQ
YPLNGILGGN RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP
NGPPSFFTSP QTSPMLGSSI QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL
EEEQPELKMC GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE
PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA FSLLADDSQT
SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ SSNFQRPLTE PAPDQPPSTQ
LHPAVSPTAS PAASLTASAE ISPAVSPVAS SPVPPEVFVA VSPASSPALP AISLEASMTT
PVTSPQGSPE PSPAAAFQTV SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT
PEEVRLPLQH GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE
HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN EKAKNKEVPK
VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA KMTKNKKKMR QKVQRGESQT
PVQGQARNKR KQDTKSLKQK DTKKKLKAEK EKMKTKQEKL KEKVKREKKE KVKAKGKEGP
RARPSCRADK TLATQKRLEE QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR
AFSDCLTIVE FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH
DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR TQPFQAQPPQ
QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV EGRLRRLKTA LAKRTGRPEV
MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE ENTTAVHGRR GRKEGEIDVA ASSIPELERH
IEKLSKRQLF FRKKLLHSSQ MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI
KQETESLMEV VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR
ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL SQSAFLSWLS
QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ SCPGPQGPWF NFSAQIPCDA
APTPPPAVSE DQPTPSLQLL ASSKPMNTPG AANPCSPVQL SSTHLPGGTP KRLSGDSEEM
SQSPTGLGQP KRRGRPPSKF FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA
LHPRGIREKA LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD
LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP WRGRGREGTV
PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV EKALLSTPNG APDGTSTEIS
YEITPRVRVW RQTLERCRSA AQVCLCMGQL ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC
DGCDRGCHIY CHRPKMEAVP EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP
EGDSRRRMLS RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW
PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF DNCQTFNEDD
SEVGKAGHVM RRFFESRWEE FYQGKQANL


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