BRWD1_MOUSE
ID BRWD1_MOUSE Reviewed; 2304 AA.
AC Q921C3; E9QAC1; Q921C2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Bromodomain and WD repeat-containing protein 1;
DE AltName: Full=WD repeat-containing protein 9;
GN Name=Brwd1; Synonyms=Wdr9;
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 [MRNA] (ISOFORMS A AND B).
RA Scott H.S., Barras C., Mittaz L., Michaud J., Guidi S., Scamuffa N.,
RA Antonarakis S.;
RT "Isolation and characterization of a new chromosome 21 gene, WDR9, with
RT different alternatively spliced transcripts and different protein forms.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12359327; DOI=10.1016/s0167-4781(02)00421-9;
RA Ramos V.C., Vidal-Taboada J.M., Bergonon S., Egeo A., Fisher E.M.C.,
RA Scartezzini P., Oliva R.;
RT "Characterisation and expression analysis of the WDR9 gene, located in the
RT Down critical region-2 of the human chromosome 21.";
RL Biochim. Biophys. Acta 1577:377-383(2002).
RN [4]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA4, AND
RP FUNCTION.
RX PubMed=12889071; DOI=10.1002/dvdy.10344;
RA Huang H., Rambaldi I., Daniels E., Featherstone M.;
RT "Expression of the Wdr9 gene and protein products during mouse
RT development.";
RL Dev. Dyn. 227:608-614(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1830, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1782; SER-1784 AND SER-1789,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-687; SER-697; SER-1609;
RP SER-1611; SER-1751; SER-1752; SER-1782; SER-1784; SER-1789; SER-1810;
RP SER-1830; THR-1853; SER-1857; THR-2151 AND SER-2153, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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: May be a transcriptional activator. May be involved in
CC chromatin remodeling. Plays a role in the regulation of cell morphology
CC and cytoskeletal organization. Required in the control of cell shape.
CC {ECO:0000269|PubMed:12889071}.
CC -!- SUBUNIT: Interacts with SMARCA4. {ECO:0000269|PubMed:12889071}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12889071}. Nucleus
CC {ECO:0000269|PubMed:12889071}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q921C3-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q921C3-2; Sequence=VSP_018552, VSP_018553;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12359327}.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed during development. Expression
CC begins to increase at 7.5 dpc, peaks at 10.5-11.5 dpc, and decreases
CC from 14.5 dpc. Weakly expressed at late embryonic stages.
CC {ECO:0000269|PubMed:12889071}.
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DR EMBL; AJ292467; CAC44373.1; -; mRNA.
DR EMBL; AJ292468; CAC44374.1; -; mRNA.
DR EMBL; AC144797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49923.1; -. [Q921C3-1]
DR RefSeq; NP_001096649.1; NM_001103179.1. [Q921C3-2]
DR RefSeq; NP_660107.2; NM_145125.3. [Q921C3-1]
DR AlphaFoldDB; Q921C3; -.
DR SMR; Q921C3; -.
DR BioGRID; 220337; 3.
DR IntAct; Q921C3; 2.
DR STRING; 10090.ENSMUSP00000023631; -.
DR iPTMnet; Q921C3; -.
DR PhosphoSitePlus; Q921C3; -.
DR EPD; Q921C3; -.
DR jPOST; Q921C3; -.
DR MaxQB; Q921C3; -.
DR PaxDb; Q921C3; -.
DR PRIDE; Q921C3; -.
DR ProteomicsDB; 265240; -. [Q921C3-1]
DR ProteomicsDB; 265241; -. [Q921C3-2]
DR Antibodypedia; 23299; 105 antibodies from 22 providers.
DR DNASU; 93871; -.
DR Ensembl; ENSMUST00000023631; ENSMUSP00000023631; ENSMUSG00000022914. [Q921C3-1]
DR Ensembl; ENSMUST00000099502; ENSMUSP00000097101; ENSMUSG00000022914. [Q921C3-1]
DR Ensembl; ENSMUST00000232755; ENSMUSP00000156497; ENSMUSG00000022914. [Q921C3-2]
DR GeneID; 93871; -.
DR KEGG; mmu:93871; -.
DR UCSC; uc008aci.2; mouse. [Q921C3-1]
DR UCSC; uc008ack.2; mouse. [Q921C3-2]
DR CTD; 54014; -.
DR MGI; MGI:1890651; Brwd1.
DR VEuPathDB; HostDB:ENSMUSG00000022914; -.
DR eggNOG; KOG0644; Eukaryota.
DR GeneTree; ENSGT00950000183107; -.
DR InParanoid; Q921C3; -.
DR OMA; EGEWGMK; -.
DR OrthoDB; 240778at2759; -.
DR TreeFam; TF324197; -.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR BioGRID-ORCS; 93871; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Brwd1; mouse.
DR PRO; PR:Q921C3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q921C3; protein.
DR Bgee; ENSMUSG00000022914; Expressed in animal zygote and 271 other tissues.
DR ExpressionAtlas; Q921C3; baseline and differential.
DR Genevisible; Q921C3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 1.20.920.10; -; 2.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF47370; SSF47370; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Bromodomain; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..2304
FT /note="Bromodomain and WD repeat-containing protein 1"
FT /id="PRO_0000235986"
FT REPEAT 184..223
FT /note="WD 1"
FT REPEAT 226..265
FT /note="WD 2"
FT REPEAT 268..311
FT /note="WD 3"
FT REPEAT 322..365
FT /note="WD 4"
FT REPEAT 366..405
FT /note="WD 5"
FT REPEAT 424..463
FT /note="WD 6"
FT REPEAT 466..506
FT /note="WD 7"
FT REPEAT 514..553
FT /note="WD 8"
FT DOMAIN 1178..1248
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1332..1402
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 663..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1542..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..2085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2117..2189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1696..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1762..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..1939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2134..2158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1751
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1853
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1889
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 1939
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 2004
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSI6"
FT MOD_RES 2040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 2151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 2179..2294
FT /note="ESVRKDREPHTKMRPCMLNEKDAVQMHSDTLKAKTVPEKVPRRCATVAANKI
FT KMMCNLKEVVSGPENVGIRTISRKLPYRQASAAAKKKLLSVYKEDDAPIHSENEKELYL
FT RRFRS -> GKPSSSNSPKTARHPRQSKGPRLNVDDNDWEDLDYAKAKGVVRLSKIQTR
FT NQGRRTVRYHDGEDDRSIESALELTDRTLRP (in isoform B)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_018552"
FT VAR_SEQ 2295..2304
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_018553"
FT CONFLICT 97..103
FT /note="ISRVTSL -> KERGTSR (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="I -> V (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="M -> I (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 970
FT /note="R -> P (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="R -> G (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="C -> L (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 1053
FT /note="F -> L (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="Q -> P (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 1091
FT /note="E -> D (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="E -> K (in Ref. 1; CAC44373/CAC44374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2304 AA; 259228 MW; EC86E1A680C1060E CRC64;
MAEPSPARRP VPLIESELYF LIARYLSAGP CRRAAQVLVQ ELEQYQLLPK RLDWEGNEHN
RSYEELVLSN KHVAPDHLLQ ICQRIGPMLD KEVPPSISRV TSLLGAGRQS LLRTAKDCRH
TVWKGSAFAA LHRGRPPEMP VNYGPPPSLV EIHRGRQLTG CSTFSTAFPG TMYQHIKMHR
RILGHLSAVY CVAFDRTGHR IFTGSDDCLV KIWSTHNGRL LSTLRGHSAE ISDMAVNYEN
TLIAAGSCDK IIRVWCLRTC APVAVLQGHT GSITSLQFSP MAKGPQRYMV STGADGTVCF
WQWDLESLKF SPRPLKFTEK PRPGVQMLCS SFSVGGMFLA TGSTDHVIRM YFLGFDAPEK
IAELESHTDK VDSIQFCNNG DRFLSGSRDG TARIWRFEQL EWRSILLDMS ARISGDTSSE
EERFMKPKVT MIAWNQDDST VVTAVNDHVL KVWSSYTGQL LHNLLGHADE VFVLETHPFD
SRIMLSAGHD GSIFIWDITK GIKMKHYFNM IEGQGHGAVF DCKFSQDGQH FACTDSHGHL
LIFGFGCSKP YEKIPDQMFF HTDYRPLIRD SNNYVLDEQT QQAPHLMPPP FLVDVDGNPH
PTKFQRLVPG RENSADEHLV PQLGYVATSD GEVIEQIISL HTNDSGDASP ESSVLDGMIR
QLQQQQDQRL GVDQDGTANG LPSGEGTPRR GSFRRLSLDI QSPPNIGLRR SGQVEGVRQM
HQNAPRSQIA TERDLQAWKR RVVVPEAPPG MFRRLEDIRI ERGEEERNLY VIGRKKKTFQ
VPQKSNSMVL VSQSRQRTCR RKYANYSRRN ADQCELSSGN ESSGSVRHET SYDQSEGSCS
SEDDEWRNDR RSGSDSDSSS DSSSQYSDWT ADTGINLQPP LRMSCRRRVT RFCSTSEDEM
SMENISPPKR RRKRRKESKP KRESLRRMTP AELANMEHLY EFHPPVWITD TTLRKSPFVP
QMGDEVMYFR QGHEAYIEAV RRNNIYELNP HKEPWRKMDL RDQELVKIVG LRYEVGPPTL
CCLKLAFIDP ATGRLTDKSF SIRYHDMPDV IDFLVLRQFY DEARQRNWQP CDRFRSIIDD
AWWFGTVLSQ EPYQPQYPDS HFQCYIVRWD NTETEKLSPW DMEPIPDNVD PPEELGASIS
VTSDELEKLL YKPQEGEWGQ RSRDEECDRI ISGIDQLLNL DIAAAFAGPV DLCTYPKYCT
VVAYPTDLYT IRMRLVNRFY RRLSALIWEV RYIEHNARTF NEPESVIARS AKKITDQLLK
FIKNQDCTNI SELCNTSDND EDDSADDLDD SDLPKTSSGR RKVHNWKRRS RASGCIESDW
RRQCKALLIL IFQCEDSEPF RQPVDLDEYP DYRDIIDTPM DFGTVRETLE AGNYDSPVEF
CKDIRLIFSN AKAYTPNKRS KIYSMTLRLS ALFEEKMKKI SFDFKIGQKF KEKLRRSQRF
KQRQNCNGAV PGDRRRRNVK QKQFKSQTKV IPQLMCPPSQ STSSKVPLSA TRKTSAGVSS
GFTSGDSSDS AGSLERVRRQ RPEVLRSGSV LFGSEMEDFL ATSSSSSASN SSEESKASPG
ARESSLRSGV LRGSNLGVTR TRAARRKAGS VSLENGCGRK ATRKRVYLSD SDNNSVETDE
NLKNRKCGSS RKVLRKCAAV AASKIKLMSD AEDSSSESPC SGRKLPHRNA SAVARKKLLH
NSDDQSLKSE TEELKDQNQS LLISGPHSVH NSISDSESDS DLRATRKTWN ANGCTSHTAA
TCKTKSRPIE SSEEDSRCHG SDHGPSSTGD PSTSGQKLRA DSISEEADSE PESSVLCKNT
HLCKKAKILS DSEDCEEKCG ERRGPEVEGS PVSEALREAI LAPQCLSHRG SETDVDSDGG
AVREKSYSNE NGSVSLENGQ RRKVSRKSSS DKESNLQVTQ KSPKDRSSPS RITQRASVAT
DKMKLTSDAE DLSLESVCTR SKRRRKKPAR FACTPAKTAL SSEEKHAHCE VPEAQPACRN
KLPEPEHQDS AENPSQAASA DLNSGGGSSF EQRKSIQSRQ MGAVCVRPPP KTQSSSAGLS
QENARSQTLD SETSLPSESV LTQKATVESN FEEELNYGLR RWNGRRLRTY GKAPLSRTAQ
VTPSLQASAE VGVKRRRMHP EVDGEDVPGQ MGSSGCGPDT SPKASDLGSV TDSDVDCTDN
TQTQRKKKRK GKARVLSKES VRKDREPHTK MRPCMLNEKD AVQMHSDTLK AKTVPEKVPR
RCATVAANKI KMMCNLKEVV SGPENVGIRT ISRKLPYRQA SAAAKKKLLS VYKEDDAPIH
SENEKELYLR RFRSRKEKAQ PTPR
