ATXR3_ARATH
ID ATXR3_ARATH Reviewed; 2335 AA.
AC O23372; Q0WVL9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Histone-lysine N-methyltransferase ATXR3 {ECO:0000305};
DE EC=2.1.1.354 {ECO:0000269|PubMed:20937886};
DE AltName: Full=Protein SET DOMAIN GROUP 2 {ECO:0000303|PubMed:11691919, ECO:0000303|PubMed:21037105, ECO:0000303|PubMed:31429787};
DE AltName: Full=Trithorax-related protein 3 {ECO:0000303|PubMed:11691919};
DE Short=TRX-related protein 3 {ECO:0000303|PubMed:11691919};
GN Name=ATXR3 {ECO:0000303|PubMed:11691919};
GN Synonyms=SDG2 {ECO:0000303|PubMed:21037105, ECO:0000303|PubMed:31429787},
GN SET2 {ECO:0000303|PubMed:11691919};
GN OrderedLocusNames=At4g15180 {ECO:0000312|Araport:AT4G15180};
GN ORFNames=dl3635w {ECO:0000312|EMBL:CAB10297.1},
GN FCAALL.214 {ECO:0000312|EMBL:CAB78560.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-517.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21037105; DOI=10.1105/tpc.110.079962;
RA Berr A., McCallum E.J., Menard R., Meyer D., Fuchs J., Dong A., Shen W.H.;
RT "Arabidopsis SET DOMAIN GROUP2 is required for H3K4 trimethylation and is
RT crucial for both sporophyte and gametophyte development.";
RL Plant Cell 22:3232-3248(2010).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20937886; DOI=10.1073/pnas.1010478107;
RA Guo L., Yu Y., Law J.A., Zhang X.;
RT "SET DOMAIN GROUP2 is the major histone H3 lysine 4 trimethyltransferase in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18557-18562(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=31429787; DOI=10.1186/s13059-019-1777-1;
RA Song Q., Huang T.-Y., Yu H.H., Ando A., Mas P., Ha M., Chen Z.J.;
RT "Diurnal regulation of SDG2 and JMJ14 by circadian clock oscillators
RT orchestrates histone modification rhythms in Arabidopsis.";
RL Genome Biol. 20:RESEARCH170.1-RESEARCH170.12(2019).
CC -!- FUNCTION: Histone methyltransferase specifically required for
CC trimethylation of 'Lys-4' of histone H3 (H3K4me3) and is crucial for
CC both sporophyte and gametophyte development (PubMed:21037105,
CC PubMed:20937886). Function as a diurnal 'writer' to counteract the
CC nocturne 'eraser' demethylase activity of JMJ14 thus orchestrating the
CC circadian rythm of histone modifications (e.g. H3K4me3) and modulating
CC the rythmic expression of diurnal target genes; this mechanism relies
CC also on the circadian clock oscillators CCA1 and LHY (PubMed:31429787).
CC {ECO:0000269|PubMed:20937886, ECO:0000269|PubMed:21037105,
CC ECO:0000269|PubMed:31429787}.
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:20937886};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:20937886}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring in the
CC morning under diurnal but not constant light conditions in a CCA1- and
CC LHY-dependent manner. {ECO:0000269|PubMed:31429787}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic effects on plant growth and
CC development, including dwarf size, aberrant root development and
CC sterile flowers (PubMed:20937886, PubMed:21037105). Decreased levels of
CC CCA1 and LHY circadian oscillators transcription factors as well as of
CC other clock genes such as TOC1, PRR5, PRR7, PRR9, GI, ELF3, ELF4, and
CC LUX associated with reduced H3K4me3 levels near their promoters
CC (PubMed:31429787). {ECO:0000269|PubMed:20937886,
CC ECO:0000269|PubMed:21037105, ECO:0000269|PubMed:31429787}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78560.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97338; CAB10297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78560.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83565.1; -; Genomic_DNA.
DR EMBL; AK226725; BAE98829.1; -; mRNA.
DR PIR; G71415; G71415.
DR RefSeq; NP_193253.4; NM_117606.5.
DR AlphaFoldDB; O23372; -.
DR STRING; 3702.AT4G15180.1; -.
DR iPTMnet; O23372; -.
DR PaxDb; O23372; -.
DR PRIDE; O23372; -.
DR ProteomicsDB; 241103; -.
DR EnsemblPlants; AT4G15180.1; AT4G15180.1; AT4G15180.
DR GeneID; 827183; -.
DR Gramene; AT4G15180.1; AT4G15180.1; AT4G15180.
DR KEGG; ath:AT4G15180; -.
DR Araport; AT4G15180; -.
DR TAIR; locus:2129755; AT4G15180.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_000704_0_0_1; -.
DR InParanoid; O23372; -.
DR OMA; HISYVHI; -.
DR OrthoDB; 28425at2759; -.
DR PhylomeDB; O23372; -.
DR PRO; PR:O23372; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23372; baseline and differential.
DR Genevisible; O23372; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:TAIR.
DR GO; GO:0048440; P:carpel development; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR025640; GYF_2.
DR InterPro; IPR045606; SDG2_C.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF14237; GYF_2; 1.
DR Pfam; PF19633; SDG2_C; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..2335
FT /note="Histone-lysine N-methyltransferase ATXR3"
FT /id="PRO_0000233360"
FT DOMAIN 1765..1904
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1914..1930
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 30..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 67..74
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 527..534
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1382..1389
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 30..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1903
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1918
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 1920
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 1925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
SQ SEQUENCE 2335 AA; 267060 MW; 26BA2C3AF6B346EA CRC64;
MSDGGVACMP LLNIMEKLPI VEKTTLCGGN ESKTAATTEN GHTSIATKVP ESQPANKPSA
SSQPVKKKRI VKVIRKVVKR RPKQPQKQAD EQLKDQPPSQ VVQLPAESQL QIKEQDKKSE
FKGGTSGVKE VENGGDSGFK DEVEEGELGT LKLHEDLENG EISPVKSLQK SEIEKGEIVG
ESWKKDEPTK GEFSHLKYHK GYVERRDFSA DKNWKGGKEE REFRSWRDPS DEIEKGEFIP
DRWQKMDTGK DDHSYIRSRR NGVDREKTWK YEYEYERTPP GGRFVNEDIY HQREFRSGLD
RTTRISSKIV IEENLHKNEY NNSSNFVKEY SSTGNRLKRH GAEPDSIERK HSYADYGDYG
SSKCRKLSDD CSRSLHSDHY SQHSAERLYR DSYPSKNSSL EKYPRKHQDA SFPAKAFSDK
HGHSPSRSDW SPHDRSRYHE NRDRSPYARE RSPYIFEKSS HARKRSPRDR RHHDYRRSPS
YSEWSPHDRS RPSDRRDYIP NFMEDTQSDR NRRNGHREIS RKSGVRERRD CQTGTELEIK
HKYKESNGKE STSSSKELQG KNILYNNSLL VEKNSVCDSS KIPVPCATGK EPVQVGEAPT
EELPSMEVDM DICDTPPHEP MASDSSLGKW FYLDYYGTEH GPARLSDLKA LMEQGILFSD
HMIKHSDNNR WLVNPPEAPG NLLEDIADTT EAVCIEQGAG DSLPELVSVR TLPDGKEIFV
ENREDFQIDM RVENLLDGRT ITPGREFETL GEALKVNVEF EETRRCVTSE GVVGMFRPMK
RAIEEFKSDD AYGSESDEIG SWFSGRWSCK GGDWIRQDEA SQDRYYKKKI VLNDGFPLCL
MQKSGHEDPR WHHKDDLYYP LSSSRLELPL WAFSVVDERN QTRGVKASLL SVVRLNSLVV
NDQVPPIPDP RAKVRSKERC PSRPARPSPA SSDSKRESVE SHSQSTASTG QDSQGLWKTD
TSVNTPRDRL CTVDDLQLHI GDWFYTDGAG QEQGPLSFSE LQKLVEKGFI KSHSSVFRKS
DKIWVPVTSI TKSPETIAML RGKTPALPSA CQGLVVSETQ DFKYSEMDTS LNSFHGVHPQ
FLGYFRGKLH QLVMKTFKSR DFSAAINDVV DSWIHARQPK KESEKYMYQS SELNSCYTKR
ARLMAGESGE DSEMEDTQMF QKDELTFEDL CGDLTFNIEG NRSAGTVGIY WGLLDGHALA
RVFHMLRYDV KSLAFASMTC RHWKATINSY KDISRQVDLS SLGPSCTDSR LRSIMNTYNK
EKIDSIILVG CTNVTASMLE EILRLHPRIS SVDITGCSQF GDLTVNYKNV SWLRCQNTRS
GELHSRIRSL KQTTDVAKSK GLGGDTDDFG NLKDYFDRVE KRDSANQLFR RSLYKRSKLY
DARRSSAILS RDARIRRWAI KKSEHGYKRV EEFLASSLRG IMKQNTFDFF ALKVSQIEEK
MKNGYYVSHG LRSVKEDISR MCREAIKDEL MKSWQDGSGL SSATKYNKKL SKTVAEKKYM
SRTSDTFGVN GASDYGEYAS DREIKRRLSK LNRKSFSSES DTSSELSDNG KSDNYSSASA
SESESDIRSE GRSQDLRIEK YFTADDSFDS VTEEREWGAR MTKASLVPPV TRKYEVIEKY
AIVADEEEVQ RKMRVSLPED YGEKLNAQRN GIEELDMELP EVKEYKPRKL LGDEVLEQEV
YGIDPYTHNL LLDSMPGELD WSLQDKHSFI EDVVLRTLNR QVRLFTGSGS TPMVFPLRPV
IEELKESARE ECDIRTMKMC QGVLKEIESR SDDKYVSYRK GLGVVCNKEG GFGEEDFVVE
FLGEVYPVWK WFEKQDGIRS LQENKTDPAP EFYNIYLERP KGDADGYDLV VVDAMHMANY
ASRICHSCRP NCEAKVTAVD GHYQIGIYSV RAIEYGEEIT FDYNSVTESK EEYEASVCLC
GSQVCRGSYL NLTGEGAFQK VLKDWHGLLE RHRLMLEACV LNSVSEEDYL ELGRAGLGSC
LLGGLPDWMI AYSARLVRFI NFERTKLPEE ILKHNLEEKR KYFSDIHLDV EKSDAEVQAE
GVYNQRLQNL AVTLDKVRYV MRHVFGDPKN APPPLERLTP EETVSFVWNG DGSLVDELLQ
SLSPHLEEGP LNELRSKIHG HDPSGSADVL KELQRSLLWL RDEIRDLPCT YKCRNDAAAD
LIHIYAYTKC FFKVREYQSF ISSPVHISPL DLGAKYADKL GESIKEYRKT YGENYCLGQL
IYWYNQTNTD PDLTLVKATR GCLSLPDVAS FYAKAQKPSK HRVYGPKTVK TMVSQMSKQP
QRPWPKDKIW TFKSTPRVFG SPMFDAVLNN SSSLDRELLQ WLRNRRHVFQ ATWDS
