SET1A_MOUSE
ID SET1A_MOUSE Reviewed; 1716 AA.
AC E9PYH6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Histone-lysine N-methyltransferase SETD1A;
DE EC=2.1.1.364 {ECO:0000305|PubMed:24550110};
DE AltName: Full=SET domain-containing protein 1A;
GN Name=Setd1a;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24550110; DOI=10.1242/dev.098152;
RA Bledau A.S., Schmidt K., Neumann K., Hill U., Ciotta G., Gupta A.,
RA Torres D.C., Fu J., Kranz A., Stewart A.F., Anastassiadis K.;
RT "The H3K4 methyltransferase Setd1a is first required at the epiblast stage,
RT whereas Setd1b becomes essential after gastrulation.";
RL Development 141:1022-1035(2014).
RN [4]
RP FUNCTION, AND INTERACTION WITH NAP1L1.
RX PubMed=29490266; DOI=10.1016/j.celrep.2018.02.019;
RA Qiao H., Li Y., Feng C., Duo S., Ji F., Jiao J.;
RT "Nap1l1 controls embryonic neural progenitor cell proliferation and
RT differentiation in the developing brain.";
RL Cell Rep. 22:2279-2293(2018).
RN [5]
RP FUNCTION.
RX PubMed=31197650; DOI=10.1007/s12264-019-00400-w;
RA Yu X., Yang L., Li J., Li W., Li D., Wang R., Wu K., Chen W., Zhang Y.,
RA Qiu Z., Zhou W.;
RT "De novo and inherited SETD1A variants in early-onset epilepsy.";
RL Neurosci. Bull. 35:1045-1057(2019).
CC -!- FUNCTION: Histone methyltransferase that catalyzes methyl group
CC transfer from S-adenosyl-L-methionine to the epsilon-amino group of
CC 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of
CC chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3
CC methylation marks at active chromatin sites where transcription and DNA
CC repair take place (By similarity). Responsible for H3K4me3 enriched
CC promoters and transcriptional programming of inner mass stem cells and
CC neuron progenitors during embryogenesis (PubMed:24550110,
CC PubMed:29490266, PubMed:31197650). Required for H3K4me1 mark at stalled
CC replication forks. Mediates FANCD2-dependent nucleosome remodeling and
CC RAD51 nucleofilaments stabilization at reversed forks, protecting them
CC from nucleolytic degradation. Does not methylate 'Lys-4' of histone H3
CC if the neighboring 'Lys-9' residue is already methylated (By
CC similarity). {ECO:0000250|UniProtKB:O15047,
CC ECO:0000269|PubMed:24550110, ECO:0000269|PubMed:29490266,
CC ECO:0000269|PubMed:31197650}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000305|PubMed:24550110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000305|PubMed:24550110};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000305|PubMed:24550110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269;
CC Evidence={ECO:0000305|PubMed:24550110};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000305|PubMed:24550110};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60273;
CC Evidence={ECO:0000305|PubMed:24550110};
CC -!- SUBUNIT: Component of the SET1A complex composed of the catalytic
CC subunit SETD1A, WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and
CC DPY30 homotrimer (By similarity). Forms a core complex with the
CC evolutionary conserved subcomplex WRAD composed of WDR5, RBBP5,
CC ASH2L/ASH2 and DPY30 subunits; WRAD differentially stimulates the
CC methyltransferase activity (By similarity). Interacts with BOD1L1 (via
CC COMPASS-Shg1 domain) at replication forks (By similarity). Interacts
CC with HCFC1. Interacts with ASH2/ASH2L, CXXC1/CFP1 and RBBP5. Interacts
CC (via the RRM domain) with WDR82. Interacts (via the RRM domain) with
CC hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large
CC subunit (POLR2A) only in the presence of WDR82. Binds specifically to
CC CTD heptad repeats phosphorylated on 'Ser-5' of each heptad. Interacts
CC with ZNF335. Interacts with SUPT6H (By similarity). Interacts with
CC NAP1L1 (PubMed:29490266). Interacts (via WIN motif) with WDR5 (By
CC similarity). {ECO:0000250|UniProtKB:O15047,
CC ECO:0000269|PubMed:29490266}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550110}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O15047}. Chromosome
CC {ECO:0000250|UniProtKB:O15047}. Note=Localizes to a largely non-
CC overlapping set of euchromatic nuclear speckles with SETD1B, suggesting
CC that SETD1A and SETD1B each bind to a unique set of target genes.
CC {ECO:0000250|UniProtKB:O15047}.
CC -!- DEVELOPMENTAL STAGE: High expression is detected in the oocyte that
CC declines to a stable level from the 8-cell stage until 8.5 dpc.
CC {ECO:0000269|PubMed:24550110}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos fail to gastrulate and die before
CC or at 7.5 dpc. {ECO:0000269|PubMed:24550110}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AC149222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40144.1; -.
DR RefSeq; NP_821172.2; NM_178029.3.
DR RefSeq; XP_017177700.1; XM_017322211.1.
DR RefSeq; XP_017177701.1; XM_017322212.1.
DR RefSeq; XP_017177702.1; XM_017322213.1.
DR RefSeq; XP_017177703.1; XM_017322214.1.
DR AlphaFoldDB; E9PYH6; -.
DR SMR; E9PYH6; -.
DR IntAct; E9PYH6; 3.
DR MINT; E9PYH6; -.
DR STRING; 10090.ENSMUSP00000047672; -.
DR iPTMnet; E9PYH6; -.
DR PhosphoSitePlus; E9PYH6; -.
DR EPD; E9PYH6; -.
DR jPOST; E9PYH6; -.
DR MaxQB; E9PYH6; -.
DR PaxDb; E9PYH6; -.
DR PeptideAtlas; E9PYH6; -.
DR PRIDE; E9PYH6; -.
DR ProteomicsDB; 335332; -.
DR Ensembl; ENSMUST00000047075; ENSMUSP00000047672; ENSMUSG00000042308.
DR Ensembl; ENSMUST00000047157; ENSMUSP00000037600; ENSMUSG00000042308.
DR GeneID; 233904; -.
DR KEGG; mmu:233904; -.
DR UCSC; uc009jwt.1; mouse.
DR CTD; 9739; -.
DR MGI; MGI:2446244; Setd1a.
DR VEuPathDB; HostDB:ENSMUSG00000042308; -.
DR eggNOG; KOG1080; Eukaryota.
DR GeneTree; ENSGT00940000162290; -.
DR HOGENOM; CLU_001226_2_0_1; -.
DR InParanoid; E9PYH6; -.
DR OMA; DNGEKDH; -.
DR OrthoDB; 1234689at2759; -.
DR PhylomeDB; E9PYH6; -.
DR TreeFam; TF106436; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR BioGRID-ORCS; 233904; 29 hits in 77 CRISPR screens.
DR ChiTaRS; Setd1a; mouse.
DR PRO; PR:E9PYH6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PYH6; protein.
DR Bgee; ENSMUSG00000042308; Expressed in embryonic post-anal tail and 194 other tissues.
DR ExpressionAtlas; E9PYH6; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:BHF-UCL.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; NAS:BHF-UCL.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:1902275; P:regulation of chromatin organization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISO:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR CDD; cd12548; RRM_Set1A; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR034467; Set1A_RRM.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037841; SETD1A.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR PANTHER; PTHR45814:SF3; PTHR45814:SF3; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; DNA damage; Methyltransferase;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..1716
FT /note="Histone-lysine N-methyltransferase SETD1A"
FT /id="PRO_0000445151"
FT DOMAIN 84..172
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1577..1694
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1700..1716
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 194..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1459
FT /note="Interaction with CFP1"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT REGION 1459..1546
FT /note="Interaction with ASH2L, RBBP5 and WDR5"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT REGION 1480..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1307..1311
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT MOTIF 1501..1506
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT COMPBIAS 220..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1008
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15047"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15047"
SQ SEQUENCE 1716 AA; 186060 MW; F578D5A2276F2D73 CRC64;
MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVS DSKYTPVEDL
QDPRCHVRSK ARDFSLPVPK FKLDEFYIGQ IPLKEVTFAR LNDNVRETFL KDMCRKYGEV
EEVEILLHPR TRKHLGLARV LFTSTRGAKE TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY
ELIVNGSYTP QTVPTGGKAL SEKFQGSGAA AETTEARRRS SSDTAAYPAG TTVGGTPGNG
TPCSQDTNFS SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
SENSYQDSFS RRHFSTSSAP ATTATATSAT AAATAASSSS SSSSSSSSSS SSSSSASQFR
GSDSSYPAYY ESWNRYQRHT SYPPRRATRE DPSGASFAEN TAERFPPSYT SYLAPEPNRS
TDQDYRPPAS EAPPPEPPEP GGGGGGSGGG GGGGGGGGGG APSPEREEAR TPPRPASPAR
SGSPAPETTN ESVPFAQHSS LDSRIEMLLK EQRSKFSFLA SDTEEEEENS SAGPGARDAG
AEVPSGAGHG PCTPPPAPAN FEDVAPTGSG EPGAARESPK ANGQNQASPC SSGEDMEISD
DDRGGSPPPA PTPPQQPPPP PPPPPPPPPP YLASLPLGYP PHQPAYLLPP RPDGPPPPEY
PPPPPPPPPH IYDFVNSLEL MDRLGAQWGG MPMSFQMQTQ MLTRLHQLRQ GKGLTAASAG
PPGGAFGEAF LPFPPPQEAA YGLPYALYTQ GQEGRGSYSR EAYHLPLPMA AEPLPSSSVS
GEEARLPHRE EAEIAESKVL PSAGTVGRVL ATLVQEMKSI MQRDLNRKMV ENVAFGAFDQ
WWESKEEKAK PFQNAAKQQA KEEDKEKMKL KEPGMLSLVD WAKSGGITGI EAFAFGSGLR
GALRLPSFKV KRKEPSEISE ASEEKRPRPS TPAEEDEDDP EREKEAGEPG RPGTKPPKRD
EERGKTQGKH RKSFTLDSEG EEASQESSSE KDEDDDDEDE EDEEQEEAVD ATKKEAEASD
GEDEDSDSSS QCSLYADSDG ENGSTSDSES GSSSSSSSSS SSSSSSSSSE SSSEEEEQSA
VIPSASPPRE VPEPLPAPDE KPETDGLVDS PVMPLSEKET LPTQPAGPAE EPPPSVPQPP
AEPPAGPPDA APRLDERPSS PIPLLPPPKK RRKTVSFSAA EEAPVPEPST AAPLQAKSSG
PVSRKVPRVV ERTIRNLPLD HASLVKSWPE EVARGGRNRA GGRVRSTEEE EATESGTEVD
LAVLADLALT PARRGLATLP TGDDSEATET SDEAERPSPL LSHILLEHNY ALAIKPPPTT
PAPRPLEPAP ALAALFSSPA DEVLEAPEVV VAEAEEPKQQ LQQQHPEQEG EEEEEDEEEE
SESSESSSSS SSDEEGAIRR RSLRSHTRRR RPPLPPPPPP PPSFEPRSEF EQMTILYDIW
NSGLDLEDMS YLRLTYERLL QQTSGADWLN DTHWVQHTIT NLSTPKRKRR PQDGPREHQT
GSARSEGYYP ISKKEKDKYL DVCPVSARQL EGGDTQGTNR VLSERRSEQR RLLSAIGTSA
IMDSDLLKLN QLKFRKKKLR FGRSRIHEWG LFAMEPIAAD EMVIEYVGQN IRQMVADMRE
KRYVQEGIGS SYLFRVDHDT IIDATKCGNL ARFINHCCTP NCYAKVITIE SQKKIVIYSK
QPIGVDEEIT YDYKFPLEDN KIPCLCGTES CRGSLN
