SET1_YEAST
ID SET1_YEAST Reviewed; 1080 AA.
AC P38827; D3DL69;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000269|PubMed:11805083};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=Lysine N-methyltransferase 2;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; Synonyms=KMT2, YTX1; OrderedLocusNames=YHR119W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9398665; DOI=10.1091/mbc.8.12.2421;
RA Nislow C., Ray E., Pillus L.;
RT "SET1, a yeast member of the Trithorax family, functions in transcriptional
RT silencing and diverse cellular processes.";
RL Mol. Biol. Cell 8:2421-2436(1997).
RN [4]
RP FUNCTION, AND INTERACTION WITH MEC3.
RX PubMed=9988274; DOI=10.1038/5991;
RA Corda Y., Schramke V., Longhese M.P., Smokvina T., Paciotti V., Brevet V.,
RA Gilson E., Geli V.;
RT "Interaction between Set1p and checkpoint protein Mec3p in DNA repair and
RT telomere functions.";
RL Nat. Genet. 21:204-208(1999).
RN [5]
RP IDENTIFICATION IN THE SET1 COMPLEX, AND FUNCTION OF THE SET1 COMPLEX.
RX PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
RA Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
RA Aasland R., Stewart A.F.;
RT "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and
RT methylates histone 3 lysine 4.";
RL EMBO J. 20:7137-7148(2001).
RN [6]
RP FUNCTION.
RX PubMed=11751634; DOI=10.1101/gad.940201;
RA Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y.R.,
RA Winston F., Allis C.D.;
RT "Histone H3 lysine 4 methylation is mediated by Set1 and required for cell
RT growth and rDNA silencing in Saccharomyces cerevisiae.";
RL Genes Dev. 15:3286-3295(2001).
RN [7]
RP SUBUNIT.
RX PubMed=11687631; DOI=10.1073/pnas.231473398;
RA Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P.,
RA Johnston M., Greenblatt J.F., Shilatifard A.;
RT "COMPASS: a complex of proteins associated with a trithorax-related SET
RT domain protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001).
RN [8]
RP FUNCTION.
RX PubMed=11818070; DOI=10.1016/s0960-9822(01)00652-2;
RA Bryk M., Briggs S.D., Strahl B.D., Curcio M.J., Allis C.D., Winston F.;
RT "Evidence that Set1, a factor required for methylation of histone H3,
RT regulates rDNA silencing in S. cerevisiae by a Sir2-independent
RT mechanism.";
RL Curr. Biol. 12:165-170(2002).
RN [9]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11805083; DOI=10.1074/jbc.c200023200;
RA Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J.,
RA Johnston M., Shilatifard A.;
RT "COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric
RT silencing of gene expression.";
RL J. Biol. Chem. 277:10753-10755(2002).
RN [10]
RP FUNCTION.
RX PubMed=12353038; DOI=10.1038/nature01080;
RA Santos-Rosa H., Schneider R., Bannister A.J., Sherriff J., Bernstein B.E.,
RA Emre N.C.T., Schreiber S.L., Mellor J., Kouzarides T.;
RT "Active genes are tri-methylated at K4 of histone H3.";
RL Nature 419:407-411(2002).
RN [11]
RP IDENTIFICATION IN THE SET1 COMPLEX, AND FUNCTION OF THE SET1 COMPLEX.
RX PubMed=11752412; DOI=10.1073/pnas.221596698;
RA Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L.;
RT "A trithorax-group complex purified from Saccharomyces cerevisiae is
RT required for methylation of histone H3.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:90-94(2002).
RN [12]
RP FUNCTION.
RX PubMed=12060701; DOI=10.1073/pnas.082249499;
RA Bernstein B.E., Humphrey E.L., Erlich R.L., Schneider R., Bouman P.,
RA Liu J.S., Kouzarides T., Schreiber S.L.;
RT "Methylation of histone H3 Lys 4 in coding regions of active genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8695-8700(2002).
RN [13]
RP FUNCTION.
RX PubMed=14636589; DOI=10.1016/s1097-2765(03)00438-6;
RA Santos-Rosa H., Schneider R., Bernstein B.E., Karabetsou N., Morillon A.,
RA Weise C., Schreiber S.L., Mellor J., Kouzarides T.;
RT "Methylation of histone H3 K4 mediates association of the Isw1p ATPase with
RT chromatin.";
RL Mol. Cell 12:1325-1332(2003).
RN [14]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [15]
RP FUNCTION.
RX PubMed=12845608; DOI=10.1002/yea.995;
RA Boa S., Coert C., Patterton H.-G.;
RT "Saccharomyces cerevisiae Set1p is a methyltransferase specific for lysine
RT 4 of histone H3 and is required for efficient gene expression.";
RL Yeast 20:827-835(2003).
RN [16]
RP FUNCTION OF THE COMPASS COMPLEX.
RX PubMed=15949446; DOI=10.1016/j.molcel.2005.05.009;
RA Morillon A., Karabetsou N., Nair A., Mellor J.;
RT "Dynamic lysine methylation on histone H3 defines the regulatory phase of
RT gene transcription.";
RL Mol. Cell 18:723-734(2005).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625 AND THR-875, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634,
CC ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:11805083,
CC ECO:0000269|PubMed:11818070, ECO:0000269|PubMed:12060701,
CC ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608,
CC ECO:0000269|PubMed:14636589, ECO:0000269|PubMed:15949446,
CC ECO:0000269|PubMed:9398665, ECO:0000269|PubMed:9988274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000269|PubMed:11805083};
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:0000269|PubMed:12353038};
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:0000269|PubMed:12353038};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex which consists of
CC SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and
CC SWD3(1). Interacts with MEC3. {ECO:0000269|PubMed:11687631,
CC ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11752412,
CC ECO:0000269|PubMed:9988274}.
CC -!- INTERACTION:
CC P38827; P43132: BRE2; NbExp=7; IntAct=EBI-16977, EBI-27115;
CC P38827; Q02574: MEC3; NbExp=3; IntAct=EBI-16977, EBI-10658;
CC P38827; P38337: SHG1; NbExp=5; IntAct=EBI-16977, EBI-21106;
CC P38827; P0CS90: SSC1; NbExp=2; IntAct=EBI-16977, EBI-8637;
CC P38827; P36104: SWD2; NbExp=6; IntAct=EBI-16977, EBI-26608;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; U00059; AAB68867.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06813.1; -; Genomic_DNA.
DR PIR; S48961; S48961.
DR RefSeq; NP_011987.1; NM_001179249.1.
DR PDB; 2J8A; X-ray; 3.00 A; A=247-375.
DR PDB; 6VEN; EM; 3.37 A; N=762-1080.
DR PDBsum; 2J8A; -.
DR PDBsum; 6VEN; -.
DR AlphaFoldDB; P38827; -.
DR SMR; P38827; -.
DR BioGRID; 36552; 485.
DR ComplexPortal; CPX-1039; COMPASS complex.
DR DIP; DIP-4616N; -.
DR ELM; P38827; -.
DR IntAct; P38827; 36.
DR MINT; P38827; -.
DR STRING; 4932.YHR119W; -.
DR iPTMnet; P38827; -.
DR MaxQB; P38827; -.
DR PaxDb; P38827; -.
DR PRIDE; P38827; -.
DR EnsemblFungi; YHR119W_mRNA; YHR119W; YHR119W.
DR GeneID; 856519; -.
DR KEGG; sce:YHR119W; -.
DR SGD; S000001161; SET1.
DR VEuPathDB; FungiDB:YHR119W; -.
DR eggNOG; KOG1080; Eukaryota.
DR GeneTree; ENSGT00940000169211; -.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; P38827; -.
DR OMA; LHQPLNT; -.
DR BioCyc; YEAST:G3O-31161-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR EvolutionaryTrace; P38827; -.
DR PRO; PR:P38827; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38827; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IGI:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IMP:CACAO.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IMP:CACAO.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IMP:CACAO.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:CACAO.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IMP:CACAO.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IGI:SGD.
DR GO; GO:1905088; P:positive regulation of synaptonemal complex assembly; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006479; P:protein methylation; IMP:CACAO.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:CACAO.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:SGD.
DR GO; GO:1903341; P:regulation of meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0055092; P:sterol homeostasis; IMP:CACAO.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP:CACAO.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
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; IPR044570; Set1-like.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 2.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1080
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000186086"
FT DOMAIN 938..1055
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1064..1080
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 875
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:2J8A"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:2J8A"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2J8A"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2J8A"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:2J8A"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:2J8A"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:2J8A"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2J8A"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:2J8A"
FT HELIX 342..364
FT /evidence="ECO:0007829|PDB:2J8A"
FT HELIX 804..824
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 835..837
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 900..917
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 918..920
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 940..944
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 946..956
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 963..966
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 969..972
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 974..986
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 994..998
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 1001..1009
FT /evidence="ECO:0007829|PDB:6VEN"
FT HELIX 1011..1014
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 1022..1030
FT /evidence="ECO:0007829|PDB:6VEN"
FT STRAND 1033..1042
FT /evidence="ECO:0007829|PDB:6VEN"
SQ SEQUENCE 1080 AA; 123912 MW; B7FA5D60F71063FD CRC64;
MSNYYRRAHA SSGSYRQPQE QPQYSRSGHY QYSNGHSHQQ YSSQYNQRRR YNHNDGTRRR
YNDDRPHSSN NASTRQYYAT NNSQSGPYVN KKSDISSRRG MSQSRYSNSN VHNTLASSSG
SLPTESALLL QQRPPSVLRY NTDNLKSKFH YFDPIKGEFF NKDKMLSWKA TDKEFSETGY
YVVKELQDGQ FKFKIKHRHP EIKASDPRNE NGIMTSGKVA THRKCRNSLI LLPRISYDRY
SLGPPPSCEI VVYPAQDSTT TNIQDISIKN YFKKYGEISH FEAFNDPNSA LPLHVYLIKY
ASSDGKINDA AKAAFSAVRK HESSGCFIMG FKFEVILNKH SILNNIISKF VEINVKKLQK
LQENLKKAKE KEAENEKAKE LQGKDITLPK EPKVDTLSHS SGSEKRIPYD LLGVVNNRPV
LHVSKIFVAK HRFCVEDFKY KLRGYRCAKF IDHPTGIYII FNDIAHAQTC SNAESGNLTI
MSRSRRIPIL IKFHLILPRF QNRTRFNKSS SSSNSTNVPI KYESKEEFIE ATAKQILKDL
EKTLHVDIKK RLIGPTVFDA LDHANFPELL AKRELKEKEK RQQIASKIAE DELKRKEEAK
RDFDLFGLYG GYAKSNKRNL KRHNSLALDH TSLKRKKLSN GIKPMAHLLN EETDSKETTP
LNDEGITRVS KEHDEEDENM TSSSSEEEEE EAPDKKFKSE SEPTTPESDH LHGIKPLVPD
QNGSSDVLDA SSMYKPTATE IPEPVYPPEE YDLKYSQTLS SMDLQNAIKD EEDMLILKQL
LSTYTPTVTP ETSAALEYKI WQSRRKVLEE EKASDWQIEL NGTLFDSELQ PGSSFKAEGF
RKIADKLKIN YLPHRRRVHQ PLNTVNIHNE RNEYTPELCQ REESSNKEPS DSVPQEVSSS
RDNRASNRRF QQDIEAQKAA IGTESELLSL NQLNKRKKPV MFARSAIHNW GLYALDSIAA
KEMIIEYVGE RIRQPVAEMR EKRYLKNGIG SSYLFRVDEN TVIDATKKGG IARFINHCCD
PNCTAKIIKV GGRRRIVIYA LRDIAASEEL TYDYKFEREK DDEERLPCLC GAPNCKGFLN
