SET1B_MOUSE
ID SET1B_MOUSE Reviewed; 1985 AA.
AC Q8CFT2; Q80TK9; Q8CFQ8; Q8CGD1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Histone-lysine N-methyltransferase SETD1B;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:Q9UPS6};
DE AltName: Full=SET domain-containing protein 1B;
GN Name=Setd1b; Synonyms=Kiaa1076, Set1b;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 883-1985 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1090-1985 (ISOFORM 2).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17355966; DOI=10.1074/jbc.m609809200;
RA Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT "Identification and characterization of the human Set1B histone H3-Lys4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:13419-13428(2007).
RN [5]
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1301; SER-1678 AND
RP SER-1682, AND IDENTIFICATION BY 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).
RN [7]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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 [8]
RP FUNCTION.
RX PubMed=29916805; DOI=10.7554/elife.27157;
RA Schmidt K., Zhang Q., Tasdogan A., Petzold A., Dahl A., Arneth B.M.,
RA Slany R., Fehling H.J., Kranz A., Stewart A.F., Anastassiadis K.;
RT "The H3K4 methyltransferase Setd1b is essential for hematopoietic stem and
RT progenitor cell homeostasis in mice.";
RL Elife 7:0-0(2018).
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). Plays an essential role in
CC regulating the transcriptional programming of multipotent hematopoietic
CC progenitor cells and lymphoid lineage specification during
CC hematopoiesis (PubMed:29916805). {ECO:0000250|UniProtKB:Q9UPS6,
CC ECO:0000269|PubMed:29916805}.
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:0000250|UniProtKB:Q9UPS6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
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:0000250|UniProtKB:Q9UPS6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
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:0000250|UniProtKB:Q9UPS6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60273;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC -!- SUBUNIT: Component of the SET1B/COMPASS complex composed of the
CC catalytic subunit SETD1A, WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1,
CC HCFC1, DPY30 homotrimer and BOD1. 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. Interacts with HCFC1 and ASH2L/ASH2.
CC Interacts (via the RRM domain) with WDR82. Interacts (via the RRM
CC domain) with hyperphosphorylated C-terminal domain (CTD) of RNA
CC polymerase II large subunit (POLR2A) only in the presence of WDR82.
CC Binds specifically to CTD heptad repeats phosphorylated on 'Ser-5' of
CC each heptad. Interacts with RBM15. Interacts (via WIN motif) with WDR5.
CC {ECO:0000250|UniProtKB:Q9UPS6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24550110}. Nucleus
CC speckle {ECO:0000250}. Chromosome {ECO:0000250}. Note=Localizes to a
CC largely non-overlapping set of euchromatic nuclear speckles with
CC SETD1A, suggesting that SETD1A and SETD1B each bind to a unique set of
CC target genes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CFT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CFT2-2; Sequence=VSP_030851;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17355966}.
CC -!- DEVELOPMENTAL STAGE: During preimplantation development expressed
CC through all stages from oocyte to blastocyst. High expression is
CC detected in oocyte that declines to a stable level from the 8-cell
CC stage until 8.5 dpc. Expressed in the blastocyst in both the inner cell
CC mass and the trophectoderm. {ECO:0000269|PubMed:24550110}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos show growth retardation from 7.5
CC dpc and die before 11.5 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; AC158114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038367; AAH38367.2; -; mRNA.
DR EMBL; BC040775; AAH40775.1; -; mRNA.
DR EMBL; BC041681; AAH41681.1; -; mRNA.
DR EMBL; AK122435; BAC65717.1; -; mRNA.
DR CCDS; CCDS59684.1; -. [Q8CFT2-1]
DR RefSeq; NP_001035488.2; NM_001040398.2. [Q8CFT2-1]
DR AlphaFoldDB; Q8CFT2; -.
DR SMR; Q8CFT2; -.
DR BioGRID; 228940; 4.
DR IntAct; Q8CFT2; 1.
DR MINT; Q8CFT2; -.
DR STRING; 10090.ENSMUSP00000133933; -.
DR iPTMnet; Q8CFT2; -.
DR PhosphoSitePlus; Q8CFT2; -.
DR EPD; Q8CFT2; -.
DR jPOST; Q8CFT2; -.
DR MaxQB; Q8CFT2; -.
DR PaxDb; Q8CFT2; -.
DR PeptideAtlas; Q8CFT2; -.
DR PRIDE; Q8CFT2; -.
DR ProteomicsDB; 261160; -. [Q8CFT2-1]
DR ProteomicsDB; 261161; -. [Q8CFT2-2]
DR Antibodypedia; 9774; 121 antibodies from 26 providers.
DR Ensembl; ENSMUST00000056053; ENSMUSP00000134686; ENSMUSG00000038384. [Q8CFT2-1]
DR Ensembl; ENSMUST00000163030; ENSMUSP00000133933; ENSMUSG00000038384. [Q8CFT2-1]
DR Ensembl; ENSMUST00000174836; ENSMUSP00000134461; ENSMUSG00000038384. [Q8CFT2-2]
DR GeneID; 208043; -.
DR KEGG; mmu:208043; -.
DR UCSC; uc008zng.2; mouse. [Q8CFT2-1]
DR CTD; 23067; -.
DR MGI; MGI:2652820; Setd1b.
DR VEuPathDB; HostDB:ENSMUSG00000038384; -.
DR eggNOG; KOG1080; Eukaryota.
DR GeneTree; ENSGT00940000154575; -.
DR HOGENOM; CLU_001226_0_0_1; -.
DR InParanoid; Q8CFT2; -.
DR OMA; RMPIEEC; -.
DR OrthoDB; 1234689at2759; -.
DR PhylomeDB; Q8CFT2; -.
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; 208043; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Setd1b; mouse.
DR PRO; PR:Q8CFT2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CFT2; protein.
DR Bgee; ENSMUSG00000038384; Expressed in humerus cartilage element and 227 other tissues.
DR ExpressionAtlas; Q8CFT2; baseline and differential.
DR Genevisible; Q8CFT2; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISO:MGI.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR CDD; cd12549; RRM_Set1B; 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; IPR034468; Set1B_RRM.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037842; SETD1B.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR PANTHER; PTHR45814:SF1; PTHR45814:SF1; 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; Alternative splicing; Chromatin regulator; Chromosome;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..1985
FT /note="Histone-lysine N-methyltransferase SETD1B"
FT /id="PRO_0000316994"
FT DOMAIN 92..180
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1846..1963
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1969..1985
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1786..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1764..1769
FT /note="WDR5 interaction motif (WIN)"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT COMPBIAS 234..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1082
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1250..1265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPS6"
FT MOD_RES 1678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1139..1179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_030851"
FT CONFLICT 1222
FT /note="A -> V (in Ref. 3; BAC65717)"
FT /evidence="ECO:0000305"
FT CONFLICT 1411
FT /note="S -> G (in Ref. 3; BAC65717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1985 AA; 215352 MW; 760EA261769292EC CRC64;
MENSHPHHHH QQPPPQPGPS GERRNHHWRS YKLMIDPALK KGHHKLYRYD GQHFSLAMSS
NRPVEIVEDP RVVGIWTKNK ELELSVPKFK IDEFYVGPVP PKQVTFAKLN DNVRENFLRD
MCKKYGEVEE VEILYNPKTK KHLGIAKVVF ATVRGAKEAV QHLHSTSVMG NIIHVELDTK
GETRMRFYEL LVTGRYTPQT LPVGELDAIS PIVSETLQLS DALKRLKDGS LSAGCGSGSS
SVTPNSGGTP FSQDTAYSSC RLDTPNSYGQ GTPITPRLGT PFSQDSSYSS RQPTPSYLFS
QDPTATFKAR RHESKFTDAY NRRHEHHYVH NSAVAGATAP FRGSSDLSFG TVGSSGTPFK
AQSQDATTFA HTPPPAQTAT ASGFKSAFSP YQTPAPPFPP PPEEPTATAA FGSRDSGEFR
RAPAPPPLPP AEPPAKEKPG TPPGPPPPDS NSMELGGRPT FGWSPEPCDS PGTPTLESSP
AGPEKPHDSL DSRIEMLLKE QRTKLPFLRE QDSDTEIQME GSPISSSSSQ LSPLSHFGTN
SQPGFRGPSP PSSRPSSTGL EDISPTPLPD SDEDEDLGLG LGPRPPPEPG PPDPMGLLGQ
TAEVDLDLAG DRTPTSERMD EGQQSSGEDM EISDDEMPSA PITSADCPKP MVVTPGAGAV
AAPNVLAPNL PLPPPPGFPP LPPPPPPPPP QPGFPMPPPL PPPPPPPPPA HPAVTVPPPP
LPAPPGVPPP PILPPLPPFP PGLFPVMQVD MSHVLGGQWG GMPMSFQMQT QMLSRLMTGQ
GACPYPPFMA AAAAAASAGL QFVNLPPYRS PFSLSNSGPG RGQHWPPLPK FDPSVPPPGY
IPRQEDPHKA TVDGVLLVVL KELKAIMKRD LNRKMVEVVA FRAFDEWWDK KERMAKASLT
PVKSGEHKDE DRPKPKDRIA SCLLESWGKG EGLGYEGLGL GIGLRGAIRL PSFKVKRKEP
PDTASSGDQK RLRPSTSVDE EDEESERERD RDIADAPCEL TKRDPKSVGV RRRPGRPLEL
DSGGEEDEKE SLSASSSSSA SSSSGSSTTS PSSSASDKEE EDRESTEEEE EEEEEEAEEE
EEEGPRSRIS SPSSSSSSDK DDEDDNEADS DGQIDSDIDD QGAPLSEASE KDNGDSEEEE
TESITTSKAP AESSSSSSES SGSSEFESSS ESESSSSSSE DEEEMTVPGV EEEEEEEEEE
EKETAMAAAT VVAMAEESMP PAGGQDFEQD RAEVPLGPRG PMRESLGTEE EVDIEAEDEV
PEMQAPELEE PPLPMGARKL EGSPEPPEEP GPNTQGDMLL SPELPARETE EAQLPSPPEH
GPESDLDMEP EPPPMLSLPL QPPLPPPRLL RPPSPPPEPE TPEPPKPPVP LEPPPEDHPP
RTPGLCGSLA KSQSTETVPA TPGGEPPLSG SSSGLSLSSP QVPGSPFSYP SPSPGLSSGG
LPRTPGRDFS FTPTFPEPSG PLLLPVCPLP TGRRDERTGP LASPVLLETG LPLPLPLPLP
LPLALPVPVL RAQPRPPPQL PPLLPATLAP CPTPIKRKPG RPRRSPPSML SLDGPLVRPP
PGPALGRDLL LLPGQPPAPI FPSAHDPRAV TLDFRNTGIP APPPPLPPQP PPPPPPPPVE
STKLPFKELD NQWPSEAIPP GPRRDEVTEE YVDLAKVRGP WRRPPKKRHE DLVAPSASPE
PSPPQPLFRP RSEFEEMTIL YDIWNGGIDE EDIRFLCVTY ERLLQQDNGM DWLNDTLWVY
HPSTSLSSAK KKKREDGIRE HVTGCARSEG FYTIDKKDKL RYLNSSRAST DEPPMDTQGM
SIPAQPHAST RAGSERRSEQ RRLLSSFTGS CDSDLLKFNQ LKFRKKKLKF CKSHIHDWGL
FAMEPIAADE MVIEYVGQNI RQVIADMREK RYEDEGIGSS YMFRVDHDTI IDATKCGNFA
RFINHSCNPN CYAKVITVES QKKIVIYSKQ HINVNEEITY DYKFPIEDVK IPCLCGSENC
RGTLN
