JMJ27_ARATH
ID JMJ27_ARATH Reviewed; 840 AA.
AC Q8VYB9; Q9SV29;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Lysine-specific demethylase JMJ27 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.65 {ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643};
DE AltName: Full=Jumonji domain-containing protein 27 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ27 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 27 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ27 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) monodemethylase JMJ27 {ECO:0000305};
GN Name=JMJ27 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At4g00990 {ECO:0000312|Araport:AT4G00990};
GN ORFNames=F3I3 {ECO:0000312|EMBL:CAB45782.1};
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=18713399; DOI=10.1111/j.1744-7909.2008.00692.x;
RA Lu F., Li G., Cui X., Liu C., Wang X.-J., Cao X.;
RT "Comparative analysis of JmjC domain-containing proteins reveals the
RT potential histone demethylases in Arabidopsis and rice.";
RL J. Integr. Plant Biol. 50:886-896(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP INDUCTION BY PSEUDOMONAS SYRINGAE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=28650521; DOI=10.1111/tpj.13623;
RA Dutta A., Choudhary P., Caruana J., Raina R.;
RT "JMJ27, an Arabidopsis H3K9 histone demethylase, modulates defense against
RT Pseudomonas syringae and flowering time.";
RL Plant J. 91:1015-1028(2017).
RN [6]
RP FUNCTION, MUTAGENESIS OF HIS-546 AND ASP-548, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, INTERACTION WITH RPN1A, REPRESSION BY RPN1A, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY DROUGHT.
RC STRAIN=cv. Columbia;
RX PubMed=34197643; DOI=10.1111/nph.17593;
RA Wang Q., Liu P., Jing H., Zhou X.F., Zhao B., Li Y., Jin J.B.;
RT "JMJ27-mediated histone H3K9 demethylation positively regulates drought-
RT stress responses in Arabidopsis.";
RL New Phytol. 232:221-236(2021).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-9' (H3K9me) of
CC histone H3 with a specific activity for H3K9me1 and H3K9me2
CC (PubMed:28650521, PubMed:34197643). No activity on H3K4, H3K27, H3K36,
CC H3R2 and H4R3 methyl marks, but weak activity on H3K9me3
CC (PubMed:28650521, PubMed:34197643). Involved in regulation of gene
CC expression (PubMed:28650521). Regulates flowering time by repressing
CC the major flowering regulator CONSTANS (CO) and promoting FLOWERING
CC LOCUS C (FLC) (PubMed:28650521). Exhibits a positive impact on abscisic
CC acid- (ABA), hydrogen peroxide- (H(2)O(2)) and calcium- (Ca(2+))
CC induced stomatal closure (PubMed:34197643). Promotes stomatal-closure-
CC dependent drought-stress responses through its histone demethylase
CC activity toward at least GOLS2 and RD20 loci, thus protecting them from
CC silencing by removing H3K9me2 marks in drought conditions
CC (PubMed:34197643). Required for plant defenses leading to resistance
CC against the virulent bacterial pathogen Pseudomonas syringae pv. tomato
CC DC3000 (Pst DC3000) via a negative regulation of WRKY25 (a repressor of
CC defense) and by triggering the expression of several pathogenesis-
CC related (PR) proteins (e.g. PR1, PR3, PR4 and PR5) (PubMed:28650521).
CC {ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(9)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:60192, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15542, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60193;
CC Evidence={ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(9)-[histone H3] + O2 =
CC CO2 + formaldehyde + L-lysyl(9)-[histone H3] + succinate;
CC Xref=Rhea:RHEA:60196, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61929; Evidence={ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60197;
CC Evidence={ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60189;
CC Evidence={ECO:0000269|PubMed:28650521, ECO:0000269|PubMed:34197643};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8GUI6};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
CC -!- SUBUNIT: Interacts with RPN1A. {ECO:0000269|PubMed:34197643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643}. Cytoplasm {ECO:0000269|PubMed:28650521}.
CC Note=Mainly observed in the nucleus, but also, to a lower extent, in
CC the cytoplasm. {ECO:0000269|PubMed:28650521}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, inflorescences, flowers and
CC siliques, and, at low levels, in roots, leaves (including vascular
CC bundles) and stems (PubMed:18713399, PubMed:28650521, PubMed:34197643).
CC Particularly observed in stomatal guard cells (PubMed:34197643).
CC {ECO:0000269|PubMed:18713399, ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643}.
CC -!- INDUCTION: Negatively regulated by RPN1A via proteasome-mediated
CC protein degradation in non-drought conditions (PubMed:34197643).
CC Accumulates in response to drought (PubMed:34197643). Induced by the
CC virulent bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst
CC DC3000) (PubMed:28650521). {ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643}.
CC -!- DISRUPTION PHENOTYPE: Higher accumulation of histone H3 methylation
CC H3K9me1 and H3K9me2 marks, including hypermethylation of histones (H3)
CC at CO and FLC promoters during flowering and at PR1 and WRKY25
CC promoters upon pathogenic interaction (PubMed:28650521). Early
CC flowering probably due to misregulation of CO and FLC
CC (PubMed:28650521). Higher water loss leading to an increased
CC sensitivity to drought and associated with reduced abscisic
CC acid- (ABA), hydrogen peroxide- (H(2)O(2)) and calcium- (Ca(2+))
CC induced stomatal closure (PubMed:34197643). Impaired resistance to the
CC virulent bacterial pathogen Pseudomonas syringae pv. tomato DC3000 (Pst
CC DC3000) associated with compromised expression of pathogenesis-related
CC (PR) genes (e.g. PR1, PR3, PR4 and PR5), but an enhanced accumulation
CC of WRKY25 (PubMed:28650521). {ECO:0000269|PubMed:28650521,
CC ECO:0000269|PubMed:34197643}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45782.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80908.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL080237; CAB45782.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80908.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81964.1; -; Genomic_DNA.
DR EMBL; AY072204; AAL60025.1; -; mRNA.
DR EMBL; AY096708; AAM20342.1; -; mRNA.
DR PIR; B85013; B85013.
DR PIR; T10539; T10539.
DR RefSeq; NP_192008.3; NM_116327.5.
DR SMR; Q8VYB9; -.
DR IntAct; Q8VYB9; 1.
DR STRING; 3702.AT4G00990.1; -.
DR PRIDE; Q8VYB9; -.
DR ProteomicsDB; 185218; -.
DR EnsemblPlants; AT4G00990.1; AT4G00990.1; AT4G00990.
DR GeneID; 827933; -.
DR Gramene; AT4G00990.1; AT4G00990.1; AT4G00990.
DR Araport; AT4G00990; -.
DR TAIR; locus:2125221; AT4G00990.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_0_1; -.
DR OMA; INEPIAG; -.
DR OrthoDB; 1185631at2759; -.
DR BRENDA; 1.14.11.65; 399.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYB9; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 2.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Metal-binding; Nucleus; Oxidoreductase; Plant defense;
KW Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..840
FT /note="Lysine-specific demethylase JMJ27"
FT /id="PRO_0000456193"
FT DOMAIN 502..798
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 80..127
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 546
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 548
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 766
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MUTAGEN 546
FT /note="H->A: Impaired H3K9me1/2 demethylase activity; when
FT associated with A-548."
FT /evidence="ECO:0000269|PubMed:34197643"
FT MUTAGEN 548
FT /note="D->A: Impaired H3K9me1/2 demethylase activity; when
FT associated with A-546."
FT /evidence="ECO:0000269|PubMed:34197643"
SQ SEQUENCE 840 AA; 96105 MW; 0C8C3D7B6D464B7D CRC64;
MEKMRGKRIR PRDSGELVED GRSESERKTR KKENDVVSKG RIGRGRGRGE VSKRSIEIDI
SNPEKDIKPD GSRKCLGSTC HHCKILTSES DLIFCSKCNK KCYCFDCIKR SYSERTHEEV
RAACPFCMMT CICRACLRLP LVIKPPSEKD TDVKLKQLQY LLVKVLPVLK DIYTEQNREL
EIESTIRGHP VTEANIKRCK LDPSERIYCD LCRTSIANFH RSCPNKNCSV DICLSCCKEL
SEGFHQERDG KKNAEGKGYE CRIPAGQGKD SDAYVPLHFS TWKLNSDSSI PCPPKECGGC
GTSTLELRRL WKRDWVEKLI TNAEKCTLNF RPTDVDIVHE CSSCSTNSDS IRRQAAFRKN
AHDNFLYSPN AVDLAEDDIA HFQFHWMKAE PVIVRNVLEK TSGLSWEPMV MWRACREMDP
KRKGTEEETT KVKALDCLDW CEVEINLHQF FEGYLEGRMH KNGWPEMLKL KDWPPSDLFE
KRLPRHNAEF IAALPFFDYT DPKSGILNLA TRFPEGSLKP DLGPKTYIAY GFHEELNRGD
SVTKLHCDIS DAVNVLTHTA KVEIPPVKYQ NIKVHQKKYA EAMLQKQQYS GQVKEASELE
NKSMKEVDES KKDLKDKAAN EEQSNNSSRP SGSGEAEKVI ISKEDNPTQP AVSTSVESIQ
EQKLDAPKET DGNTNERSKA VHGGAVWDIF RREDVPKLIQ FLKRHEHEFR HFNNEPLESV
IHPIHDQTMF LSDSQKKQLK EEFDIEPWTF EQHLGEAVFI PAGCPHQVRN RQSCIKVALD
FVAPESVEEC LRLTQEFRRL PKDHSSSEDK LELKKIALYA ASSAIREVKG LMQSSRRSDT
