SET2_YEAST
ID SET2_YEAST Reviewed; 733 AA.
AC P46995; D6VW19;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE EC=2.1.1.359 {ECO:0000269|PubMed:11839797, ECO:0000269|PubMed:12917322, ECO:0000269|PubMed:20048053};
DE AltName: Full=Lysine N-methyltransferase 3;
DE AltName: Full=SET domain-containing protein 2;
GN Name=SET2; Synonyms=EZL1, KMT3; OrderedLocusNames=YJL168C; ORFNames=J0520;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 594; 605 AND 716.
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 INTERACTION WITH RBP1 AND RBP2.
RX PubMed=12381723; DOI=10.1074/jbc.m209294200;
RA Li J., Moazed D., Gygi S.P.;
RT "Association of the histone methyltransferase Set2 with RNA polymerase II
RT plays a role in transcription elongation.";
RL J. Biol. Chem. 277:49383-49388(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-195 AND CYS-201.
RX PubMed=11839797; DOI=10.1128/mcb.22.5.1298-1306.2002;
RA Strahl B.D., Grant P.A., Briggs S.D., Sun Z.-W., Bone J.R., Caldwell J.A.,
RA Mollah S., Cook R.G., Shabanowitz J., Hunt D.F., Allis C.D.;
RT "Set2 is a nucleosomal histone H3-selective methyltransferase that mediates
RT transcriptional repression.";
RL Mol. Cell. Biol. 22:1298-1306(2002).
RN [5]
RP INTERACTION WITH RNA POLYMERASE II, AND FUNCTION.
RX PubMed=12629047; DOI=10.1101/gad.1055503;
RA Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H.,
RA Strahl B.D.;
RT "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in
RT yeast.";
RL Genes Dev. 17:654-663(2003).
RN [6]
RP INTERACTION WITH RNA POLYMERASE II.
RX PubMed=12511561; DOI=10.1074/jbc.m212134200;
RA Li B., Howe L., Anderson S., Yates J.R. III, Workman J.L.;
RT "The Set2 histone methyltransferase functions through the phosphorylated
RT carboxyl-terminal domain of RNA polymerase II.";
RL J. Biol. Chem. 278:8897-8903(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH RNA POLYMERASE II.
RX PubMed=12773564; DOI=10.1128/mcb.23.12.4207-4218.2003;
RA Krogan N.J., Kim M., Tong A., Golshani A., Cagney G., Canadien V.,
RA Richards D.P., Beattie B.K., Emili A., Boone C., Shilatifard A.,
RA Buratowski S., Greenblatt J.;
RT "Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to
RT transcriptional elongation by RNA polymerase II.";
RL Mol. Cell. Biol. 23:4207-4218(2003).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAINS.
RX PubMed=12917322; DOI=10.1128/mcb.23.17.5972-5978.2003;
RA Landry J., Sutton A., Hesman T., Min J., Xu R.-M., Johnston M.,
RA Sternglanz R.;
RT "Set2-catalyzed methylation of histone H3 represses basal expression of
RT GAL4 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:5972-5978(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH RNA POLYMERASE II.
RX PubMed=12736296; DOI=10.1093/nar/gkg372;
RA Schaft D., Roguev A., Kotovic K.M., Shevchenko A., Sarov M., Shevchenko A.,
RA Neugebauer K.M., Stewart A.F.;
RT "The histone 3 lysine 36 methyltransferase, SET2, is involved in
RT transcriptional elongation.";
RL Nucleic Acids Res. 31:2475-2482(2003).
RN [10]
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 [11]
RP FUNCTION, DOMAIN, AND INTERACTION WITH RNA POLYMERASE II CTD.
RX PubMed=15798214; DOI=10.1128/mcb.25.8.3305-3316.2005;
RA Kizer K.O., Phatnani H.P., Shibata Y., Hall H., Greenleaf A.L.,
RA Strahl B.D.;
RT "A novel domain in Set2 mediates RNA polymerase II interaction and couples
RT histone H3 K36 methylation with transcript elongation.";
RL Mol. Cell. Biol. 25:3305-3316(2005).
RN [12]
RP FUNCTION.
RX PubMed=16227595; DOI=10.1128/mcb.25.21.9447-9459.2005;
RA Rao B., Shibata Y., Strahl B.D., Lieb J.D.;
RT "Dimethylation of histone H3 at lysine 36 demarcates regulatory and
RT nonregulatory chromatin genome-wide.";
RL Mol. Cell. Biol. 25:9447-9459(2005).
RN [13]
RP INTERACTION WITH CYC8.
RX PubMed=16329992; DOI=10.1016/j.bbrc.2005.11.103;
RA Tripic T., Edmondson D.G., Davie J.K., Strahl B.D., Dent S.Y.R.;
RT "The Set2 methyltransferase associates with Ssn6 yet Tup1-Ssn6 repression
RT is independent of histone methylation.";
RL Biochem. Biophys. Res. Commun. 339:905-914(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-522, 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).
RN [16]
RP CATALYTIC ACTIVITY.
RX PubMed=20048053; DOI=10.1128/mcb.01229-09;
RA Lin L.J., Minard L.V., Johnston G.C., Singer R.A., Schultz M.C.;
RT "Asf1 can promote trimethylation of H3 K36 by Set2.";
RL Mol. Cell. Biol. 30:1116-1129(2010).
RN [17]
RP STRUCTURE BY NMR OF 7-33.
RX PubMed=10802733; DOI=10.1038/75144;
RA Macias M.J., Gervais V., Civera C., Oschkinat H.;
RT "Structural analysis of WW domains and design of a WW prototype.";
RL Nat. Struct. Biol. 7:375-379(2000).
RN [18]
RP STRUCTURE BY NMR OF 619-718.
RX PubMed=16286474; DOI=10.1074/jbc.c500423200;
RA Vojnic E., Simon B., Strahl B.D., Sattler M., Cramer P.;
RT "Structure and carboxyl-terminal domain (CTD) binding of the Set2 SRI
RT domain that couples histone H3 Lys36 methylation to transcription.";
RL J. Biol. Chem. 281:13-15(2006).
CC -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. The methyltransferase activity requires
CC the recruitment to the RNA polymerase II, which is CTK1 dependent.
CC {ECO:0000269|PubMed:11839797, ECO:0000269|PubMed:12629047,
CC ECO:0000269|PubMed:12736296, ECO:0000269|PubMed:12773564,
CC ECO:0000269|PubMed:12917322, ECO:0000269|PubMed:15798214,
CC ECO:0000269|PubMed:16227595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00901,
CC ECO:0000269|PubMed:11839797, ECO:0000269|PubMed:12917322,
CC ECO:0000269|PubMed:20048053};
CC -!- SUBUNIT: Interacts with the RNA polymerase II hyperphosphorylated CTD.
CC Interacts with CYC8. {ECO:0000269|PubMed:12381723,
CC ECO:0000269|PubMed:12511561, ECO:0000269|PubMed:12629047,
CC ECO:0000269|PubMed:12736296, ECO:0000269|PubMed:12773564,
CC ECO:0000269|PubMed:15798214, ECO:0000269|PubMed:16329992}.
CC -!- INTERACTION:
CC P46995; P61830: HHT2; NbExp=2; IntAct=EBI-16985, EBI-8098;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC -!- DOMAIN: The AWS and SET domains are necessary for transcription
CC repression. {ECO:0000269|PubMed:12917322, ECO:0000269|PubMed:15798214}.
CC -!- MISCELLANEOUS: Present with 217 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. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00901}.
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DR EMBL; Z49444; CAA89464.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08635.2; -; Genomic_DNA.
DR PIR; S56951; S56951.
DR RefSeq; NP_012367.2; NM_001181601.2.
DR PDB; 1E0N; NMR; -; A=479-505.
DR PDB; 2C5Z; NMR; -; A=620-719.
DR PDB; 7EA5; EM; 3.30 A; K=33-260.
DR PDBsum; 1E0N; -.
DR PDBsum; 2C5Z; -.
DR PDBsum; 7EA5; -.
DR AlphaFoldDB; P46995; -.
DR BMRB; P46995; -.
DR SMR; P46995; -.
DR BioGRID; 33591; 656.
DR DIP; DIP-2150N; -.
DR IntAct; P46995; 62.
DR MINT; P46995; -.
DR STRING; 4932.YJL168C; -.
DR iPTMnet; P46995; -.
DR MaxQB; P46995; -.
DR PaxDb; P46995; -.
DR PRIDE; P46995; -.
DR EnsemblFungi; YJL168C_mRNA; YJL168C; YJL168C.
DR GeneID; 853271; -.
DR KEGG; sce:YJL168C; -.
DR SGD; S000003704; SET2.
DR VEuPathDB; FungiDB:YJL168C; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_1_1_1; -.
DR InParanoid; P46995; -.
DR OMA; CQEKWIA; -.
DR BioCyc; MetaCyc:G3O-31606-MON; -.
DR BioCyc; YEAST:G3O-31606-MON; -.
DR BRENDA; 2.1.1.359; 984.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR EvolutionaryTrace; P46995; -.
DR PRO; PR:P46995; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46995; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IDA:SGD.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR GO; GO:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IDA:SGD.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IMP:SGD.
DR GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; IMP:SGD.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:SGD.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IGI:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:1900049; P:regulation of histone exchange; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:SGD.
DR CDD; cd19172; SET_SETD2; 1.
DR Gene3D; 1.10.1740.100; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR025788; Set2_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF18507; WW_1; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..733
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000186087"
FT DOMAIN 63..118
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 120..237
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 244..260
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 475..507
FT /note="WW"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..718
FT /note="Binding to RNA polymerase II CTD"
FT REGION 672..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 548..630
FT /evidence="ECO:0000255"
FT COMPBIAS 15..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 195
FT /note="R->G: Reduces dramatically histone methyltransferase
FT activity toward nucleosomes."
FT /evidence="ECO:0000269|PubMed:11839797"
FT MUTAGEN 201
FT /note="C->A: Reduces dramatically histone methyltransferase
FT activity toward nucleosomes."
FT /evidence="ECO:0000269|PubMed:11839797"
FT CONFLICT 594
FT /note="A -> F (in Ref. 1; CAA89464)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="A -> S (in Ref. 1; CAA89464)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="A -> G (in Ref. 1; CAA89464)"
FT /evidence="ECO:0000305"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7EA5"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:7EA5"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:7EA5"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7EA5"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:7EA5"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:7EA5"
FT STRAND 481..494
FT /evidence="ECO:0007829|PDB:1E0N"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:1E0N"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:1E0N"
FT HELIX 624..645
FT /evidence="ECO:0007829|PDB:2C5Z"
FT TURN 648..652
FT /evidence="ECO:0007829|PDB:2C5Z"
FT HELIX 655..676
FT /evidence="ECO:0007829|PDB:2C5Z"
FT HELIX 688..712
FT /evidence="ECO:0007829|PDB:2C5Z"
SQ SEQUENCE 733 AA; 84461 MW; 05436B181E88EFF5 CRC64;
MSKNQSVSAS EDEKEILNNN AEGHKPQRLF DQEPDLTEEA LTKFENLDDC IYANKRIGTF
KNNDFMECDC YEEFSDGVNH ACDEDSDCIN RLTLIECVND LCSSCGNDCQ NQRFQKKQYA
PIAIFKTKHK GYGVRAEQDI EANQFIYEYK GEVIEEMEFR DRLIDYDQRH FKHFYFMMLQ
NGEFIDATIK GSLARFCNHS CSPNAYVNKW VVKDKLRMGI FAQRKILKGE EITFDYNVDR
YGAQAQKCYC EEPNCIGFLG GKTQTDAASL LPQNIADALG VTVSMEKKWL KLKKLSGEPI
IKNENENINI EFLQSLEVQP IDSPVDVTKI MSVLLQQDNK IIASKLLKRL FTIDDDSLRH
QAIKLHGYTC FSKMLKLFIT EQPQVDGKGN ETEEDDIKFI KGILDFLLEL PKTTRNGIES
SQIDNVVKTL PAKFPFLKPN CDELLEKWSK FETYKRITKK DINVAASKMI DLRRVRLPPG
WEIIHENGRP LYYNAEQKTK LHYPPSGSSK VFSSRSNTQV NSPSSSGIPK TPGALDSKKH
KLSDEEYERK KQKRLEYERI ALERAKQEEL ESLKQKLKLE NERKSVLEDI IAEANKQKEL
QKEEAKKLVE AKEAKRLKRK TVSQSQRLEH NWNKFFASFV PNLIKKNPQS KQFDHENIKQ
CAKDIVKILT TKELKKDSSR APPDDLTKGK RHKVKEFINS YMDKIILKKK QKKALALSSA
STRMSSPPPS TSS
