ARI1B_MOUSE
ID ARI1B_MOUSE Reviewed; 2306 AA.
AC E9Q4N7;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=AT-rich interactive domain-containing protein 1B;
DE Short=ARID domain-containing protein 1B {ECO:0000305};
DE AltName: Full=BRG1-associated factor 250b {ECO:0000305};
DE Short=BAF250B {ECO:0000305};
GN Name=Arid1b {ECO:0000312|MGI:MGI:1926129}; Synonyms=Baf250b {ECO:0000305};
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 FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES.
RX PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA Aebersold R., Graef I.A., Crabtree G.R.;
RT "An essential switch in subunit composition of a chromatin remodeling
RT complex during neural development.";
RL Neuron 55:201-215(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-480 AND ARG-599, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [5]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=22952240; DOI=10.1074/jbc.r111.309302;
RA Euskirchen G., Auerbach R.K., Snyder M.;
RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
RT functions.";
RL J. Biol. Chem. 287:30897-30905(2012).
RN [6]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=26601204; DOI=10.1126/sciadv.1500447;
RA Kadoch C., Crabtree G.R.;
RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic
RT insights gained from human genomics.";
RL Sci. Adv. 1:E1500447-E1500447(2015).
CC -!- FUNCTION: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Component of SWI/SNF chromatin remodeling complexes that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. Belongs to the neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) and the neuron-specific chromatin remodeling
CC complex (nBAF complex). During neural development a switch from a
CC stem/progenitor to a postmitotic chromatin remodeling mechanism occurs
CC as neurons exit the cell cycle and become committed to their adult
CC state. The transition from proliferating neural stem/progenitor cells
CC to postmitotic neurons requires a switch in subunit composition of the
CC npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (PubMed:17640523). Binds DNA
CC non-specifically. {ECO:0000250|UniProtKB:Q8NFD5,
CC ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in some
CC of which it can be mutually exclusive with ARID1B/BAF250B. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible combinations developmentally and tissue
CC specific. Component of the BAF (SWI/SNF-A) complex, which includes at
CC least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In
CC muscle cells, the BAF complex also contains DPF3. Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of a
CC SWI/SNF-like EBAFb complex, at least composed of SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57, SMARCD1/BAF60A,
CC SMARCD2/BAF60B, SMARCC1/BAF155, SMARCC2/BAF170, ARID1B/BAF250B,
CC MLLT1/ENL and actin. Interacts through its C-terminus with
CC SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A. Interacts with
CC SMARCC1/BAF155 (By similarity). {ECO:0000250|UniProtKB:Q8NFD5,
CC ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC E9Q4N7; Q3TKT4: Smarca4; NbExp=5; IntAct=EBI-6900614, EBI-1210244;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFD5,
CC ECO:0000255|PROSITE-ProRule:PRU00355}.
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DR EMBL; AC126929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49929.1; -.
DR RefSeq; NP_001078824.1; NM_001085355.1.
DR AlphaFoldDB; E9Q4N7; -.
DR SMR; E9Q4N7; -.
DR IntAct; E9Q4N7; 3.
DR STRING; 10090.ENSMUSP00000111463; -.
DR iPTMnet; E9Q4N7; -.
DR PhosphoSitePlus; E9Q4N7; -.
DR jPOST; E9Q4N7; -.
DR MaxQB; E9Q4N7; -.
DR PaxDb; E9Q4N7; -.
DR PeptideAtlas; E9Q4N7; -.
DR PRIDE; E9Q4N7; -.
DR ProteomicsDB; 273938; -.
DR Antibodypedia; 19980; 171 antibodies from 27 providers.
DR GeneID; 239985; -.
DR KEGG; mmu:239985; -.
DR UCSC; uc008aey.1; mouse.
DR CTD; 57492; -.
DR MGI; MGI:1926129; Arid1b.
DR VEuPathDB; HostDB:ENSMUSG00000069729; -.
DR eggNOG; KOG2510; Eukaryota.
DR InParanoid; E9Q4N7; -.
DR OMA; WKLYVAV; -.
DR OrthoDB; 256110at2759; -.
DR PhylomeDB; E9Q4N7; -.
DR TreeFam; TF320364; -.
DR Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 239985; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Arid1b; mouse.
DR PRO; PR:E9Q4N7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9Q4N7; protein.
DR Bgee; ENSMUSG00000069729; Expressed in rostral migratory stream and 233 other tissues.
DR ExpressionAtlas; E9Q4N7; baseline and differential.
DR Genevisible; E9Q4N7; MM.
DR GO; GO:0035060; C:brahma complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:MGI.
DR GO; GO:0097026; P:dendritic cell dendrite assembly; IMP:MGI.
DR GO; GO:0060996; P:dendritic spine development; IMP:MGI.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR038040; ARID1B.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021906; BAF250/Osa.
DR InterPro; IPR033388; BAF250_C.
DR PANTHER; PTHR12656; PTHR12656; 2.
DR PANTHER; PTHR12656:SF11; PTHR12656:SF11; 2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF12031; BAF250_C; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Coiled coil; DNA-binding; Methylation;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..2306
FT /note="AT-rich interactive domain-containing protein 1B"
FT /id="PRO_0000442428"
FT DOMAIN 1123..1214
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1765..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1941..1961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 495..499
FT /note="LXXLL"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOTIF 1428..1447
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O14497"
FT MOTIF 2106..2110
FT /note="LXXLL"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT COMPBIAS 76..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..172
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1811
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 480
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 599
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 631
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 1612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 1785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
FT MOD_RES 1847
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFD5"
SQ SEQUENCE 2306 AA; 242882 MW; 836CF54776C7E814 CRC64;
MAARAAAAAR ARAGSGERRA PSGPRPAPGA RDLETGARGA VAAPGPILGG GDGGLNNVHH
HPLHPRHDLN MAHSASAAAA ASSNSAQSGR SEAALKEGGS AAALSSSAAV AASSSSAGPG
STMETGLLPN HKLKAVGEAP AAPPHQQHHH HHAHHHHHHH AHHLHHLHHH HALQQQLNQF
QQPQPPQPQQ QQPPPPPQQQ HPTANNSLGG AGGGAPQPGP DMEQPQHGGA KDSVAGNQAD
PQGQPLLSKP GDEDDAPPKM GEPAGSRYEH PGLGAQQQPA PVAVPGGGGG PAAVSEFNNY
YGSAAPASGG PGGRAGPCFD QHGGQQSPGM GMMHSASAAA GAPSSMDPLQ NSHEGYPNSQ
YNHYPGYSRP GAGGGGGGGG GGGGSGGGGG GGGAGGAGGA AAAAAGAGAV AAAAAAAAAA
AAAAGGGGGG GYGSSSSGYG VLSSPRQQGG GMMMGPGGGG AASLSKAAAG AAAAAGGFQR
FAGQNQHPSG ATPTLNQLLT SPSPMMRSYG GSYPDYSSSS APPPPSQPQS QAAAGAAAGG
QQAAAGMGLG KDLGAQYAAA SPAWAAAQQR SHPAMSPGTP GPTMGRSQGS PMDPMVMKRP
QLYGMGTHPH SQPQQSSPYP GGSYGPPGAQ RYPLGMQGRA PGALGGLQYP QQQMPPQYGQ
QAVSGYCQQG QQPYYNQQPQ PSHLPPQAQY LQPAAAQSQQ RYQPQQDMSQ EGYGTRSQPP
LAPGKSNHED LNLIQQERPS SLPDLSGSID DLPTGTEATL SSAVSASGST SSQGDQSNPA
QSPFSPHASP HLSSIPGGPS PSPVGSPVGS NQSRSGPISP ASIPGSQMPP QPPGSQSESS
SHPALSQSPM PQERGNYSRT PTYSGVPSAS YSGPGPGMGI NANNQMHGQG PAQPCGAMPL
GRMPSAGMQN RPFPGTMSSV TPSSPGMSQQ GGPGMGPPMP TVNRKAQEAA AAVMQAAANS
AQSRQGSFPG MNQSGLVASS SPYSQSMNNN SSLMSTQAQP YSMTPTMVNS STASMGLADM
MSPSESKLSV PLKADGKEEG VSQPESKSKD SYGSQGISQP PTPGNLPVPS PMSPSSASIS
SFHGDESDSI SSPGWPKTPS SPKSSSSSTT GEKITKVYEL GNEPERKLWV DRYLTFMEER
GSPVSSLPAV GKKPLDLFRL YVCVKEIGGL AQVNKNKKWR ELATNLNVGT SSSAASSLKK
QYIQYLFAFE CKTERGEEPP PEVFSTGDSK KQPKLQPPSP ANSGSLQGPQ TPQSTGSNSM
AEVPGDLKPP TPASTPHGQM TPMQSGRSST VSVHDPFSDV SDSAYPKRNS MTPNAPYQQG
MGMPDMMGRM PYEPNKDPFS GMRKVPGSSE PFMTQGQVPN SGMQDMYNQS PSGAMSNLGM
GQRQQFPYGT SYDRRHEAYG QQYPGQGPPT GQPPYGGHQP GLYPQQPNYK RHMDGMYGPP
AKRHEGDMYN MQYGSQQQEM YNQYGGSYSG PDRRPIQGQY PYPYNRERMQ GPGQMQPHGI
PPQMMGGPMQ SSSSEGPQQN MWATRNDMPY PYQSRQGPGG PAQAPPYPGM NRTDDMMVPE
QRINHESQWP SHVSQRQPYM SSSASMQPIT RPPQSSYQTP PSLPNHISRA PSPASFQRSL
ESRMSPSKSP FLPTMKMQKV MPTVPTSQVT GPPPQPPPIR REITFPPGSV EASQPILKQR
RKITSKDIVT PEAWRVMMSL KSGLLAESTW ALDTINILLY DDSTVATFNL SQLSGFLELL
VEYFRKCLID IFGILMEYEV GDPSQKALDH RSGKKDDSQS LEDDSGKEDD DAECLVEEEE
EEEEEEEDSE KIESEGKSSP ALAAPDASVD PKETPKQASK FDKLPIKIVK KNKLFVVDRS
DKLGRVQEFS SGLLHWQLGG GDTTEHIQTH FESKMEIPPR RRPPPPLSST GKKKELEGKG
DSEEQPEKSI IATIDDVLSA RPGALPEDTN PGPQTDSGKF PFGIQQAKSH RNIRLLEDEP
RSRDETPLCT IAHWQDSLAK RCICVSNIVR SLSFVPGNDA EMSKHPGLVL ILGKLILLHH
EHPERKRAPQ TYEKEEDEDK GVACSKDEWW WDCLEVLRDN TLVTLANISG QLDLSAYTES
ICLPILDGLL HWMVCPSAEA QDPFPTVGPN SVLSPQRLVL ETLCKLSIQD NNVDLILATP
PFSRQEKFYA TLVRYVGDRK NPVCREMSMA LLSNLAQGDT LAARAIAVQK GSIGNLISFL
EDGVTMAQYQ QSQHNLMHMQ PPPLEPPSVD MMCRAAKALL AMARVDENRS EFLLHEGRLL
DISISAVLNS LVASVICDVL FQIGQL
