JMJ17_ARATH
ID JMJ17_ARATH Reviewed; 1208 AA.
AC F4I240; Q94BQ7; Q9SH34;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Lysine-specific demethylase JMJ17 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.67 {ECO:0000269|PubMed:31038749};
DE AltName: Full=Jumonji domain-containing protein 17 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ17 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 17 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ17 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ17 {ECO:0000305};
GN Name=JMJ17 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At1g63490 {ECO:0000312|Araport:AT1G63490};
GN ORFNames=F2K11.14 {ECO:0000312|EMBL:AAF19696.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 66-1208.
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, MUTAGENESIS OF HIS-172 AND GLU-174, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND REPRESSION BY DROUGHT AND ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=31038749; DOI=10.1111/nph.15874;
RA Huang S., Zhang A., Jin J.B., Zhao B., Wang T.-J., Wu Y., Wang S., Liu Y.,
RA Wang J., Guo P., Ahmad R., Liu B., Xu Z.-Y.;
RT "Arabidopsis histone H3K4 demethylase JMJ17 functions in dehydration stress
RT response.";
RL New Phytol. 223:1372-1387(2019).
CC -!- FUNCTION: Functions as histone H3 'Lys-4' (H3K4me) demethylase involved
CC in the regulation of gene expression (PubMed:31038749). Active on
CC H3K4me1, H3K4me2 and H3K4me3 (PubMed:31038749). Repressor of the
CC abscisic acid (ABA) signaling pathway, especially during stomatal
CC closure regulation (PubMed:31038749). Negative regulator of responses
CC to dehydration stress by binding directly to the chromatin of
CC SRK2E/OST1 and demethylating H3K4me3 to regulates its expression
CC (PubMed:31038749). Together with JMJ14 and JMJ16, required for plant
CC growth and development (PubMed:31038749).
CC {ECO:0000269|PubMed:31038749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone
CC H3] + O2 = CO2 + formaldehyde + N(6),N(6)-dimethyl-L-lysyl(4)-
CC [histone H3] + succinate; Xref=Rhea:RHEA:60212, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61961, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:31038749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213;
CC Evidence={ECO:0000269|PubMed:31038749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] +
CC O2 = CO2 + formaldehyde + N(6)-methyl-L-lysyl(4)-[histone H3] +
CC succinate; Xref=Rhea:RHEA:60216, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, 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:31038749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217;
CC Evidence={ECO:0000269|PubMed:31038749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl(4)-[histone H3] + O2 =
CC CO2 + formaldehyde + L-lysyl(4)-[histone H3] + succinate;
CC Xref=Rhea:RHEA:60220, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
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:31038749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60221;
CC Evidence={ECO:0000269|PubMed:31038749};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000269|PubMed:31038749};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60209;
CC Evidence={ECO:0000269|PubMed:31038749};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:31038749}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, roots, seedlings and
CC siliques, and, at low levels, in leaves and stems.
CC {ECO:0000269|PubMed:18713399, ECO:0000269|PubMed:31038749}.
CC -!- DEVELOPMENTAL STAGE: At the seedling stage, present in the veins of
CC cotyledons, hypocotyls, roots and germinated seedlings
CC (PubMed:31038749). Later observed in leaves, primary and secondary
CC roots, floral tissues, siliques and guard cells (PubMed:31038749).
CC {ECO:0000269|PubMed:31038749}.
CC -!- INDUCTION: Slightly reduced in guard cells upon dehydration stress and
CC abscisic acid (ABA) treatment. {ECO:0000269|PubMed:31038749}.
CC -!- DISRUPTION PHENOTYPE: Increased dehydration stress tolerance associated
CC with abscisic acid (ABA) hypersensitivity during stomatal closure
CC regulation (PubMed:31038749). Ectopic increase in genome-wide H3K4me1,
CC H3K4me2 and H3K4me3 levels and activation of several dehydration
CC stress-responsive genes, including OST1 (PubMed:31038749). The double
CC mutants jmj17-1 jmj14-1 and jmj17-1 jmj16-1 have an early flowering
CC phenotype (especially in long day conditions) (PubMed:31038749). The
CC triple mutant jmj17-1 jmj14-1 jmj16-1 flowers even earlier
CC (PubMed:31038749). {ECO:0000269|PubMed:31038749}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK64062.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC008047; AAF19696.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34105.2; -; Genomic_DNA.
DR EMBL; AY039958; AAK64062.1; ALT_INIT; mRNA.
DR EMBL; BT011572; AAS46255.1; -; mRNA.
DR PIR; D96660; D96660.
DR RefSeq; NP_001319304.1; NM_001334100.1.
DR SMR; F4I240; -.
DR PRIDE; F4I240; -.
DR ProteomicsDB; 202296; -.
DR EnsemblPlants; AT1G63490.1; AT1G63490.1; AT1G63490.
DR GeneID; 842655; -.
DR Gramene; AT1G63490.1; AT1G63490.1; AT1G63490.
DR KEGG; ath:AT1G63490; -.
DR Araport; AT1G63490; -.
DR TAIR; locus:2031290; AT1G63490.
DR HOGENOM; CLU_000946_0_0_1; -.
DR OMA; MMIAKLE; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I240; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0048589; P:developmental growth; IMP:UniProtKB.
DR GO; GO:0034721; P:histone H3-K4 demethylation, trimethyl-H3-K4-specific; IDA:UniProtKB.
DR GO; GO:0031061; P:negative regulation of histone methylation; IDA:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProt.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 2.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Developmental protein; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Repeat;
KW Repressor; Stress response; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1208
FT /note="Lysine-specific demethylase JMJ17"
FT /id="PRO_0000456189"
FT DOMAIN 126..292
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1..36
FT /note="PHD-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 369..421
FT /note="C5HC2"
FT /evidence="ECO:0000255"
FT ZN_FING 1099..1145
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT MOTIF 613..620
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 260
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 1102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT MUTAGEN 172
FT /note="H->A: Abolished histone H3 'Lys-4' (H3K4me)
FT demethylase activity toward H3K4me1, H3K4me2 and H3K4me3
FT leading to ectopic increase in genome-wide H3K4me1, H3K4me2
FT and H3K4me3 levels and a better dehydration stress
FT tolerance; when associated with A-174."
FT /evidence="ECO:0000269|PubMed:31038749"
FT MUTAGEN 174
FT /note="E->A: Abolished histone H3 'Lys-4' (H3K4me)
FT demethylase activity toward H3K4me1, H3K4me2 and H3K4me3
FT leading to ectopic increase in genome-wide H3K4me1, H3K4me2
FT and H3K4me3 levels and a better dehydration stress
FT tolerance; when associated with A-172."
FT /evidence="ECO:0000269|PubMed:31038749"
FT CONFLICT 455
FT /note="K -> KQ (in Ref. 3; AAK64062/AAS46255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1208 AA; 137055 MW; F9C70ADAB8F45F44 CRC64;
MLLCDSCNKG WHIYCLSPPL KHIPLGNWYC LECLNTDEET FGFVPGKCLL LEDFKRIADR
AKRKWFGSGT VSRTQIEKKF WEIVEGSGGE VEVMYGNDLD TSVYGSGFPR IGDQRPESVE
ADIWDEYCGS PWNLNNMPKL KGSMLQAIRH NINGVTVPWL YLGMLFSSFC WHFEDHCFYS
VNYLHWGEAK CWYGIPGSAA SAFEKVMRKT LPDLFDAQPD LLFQLVTMLS PTVLQENKVP
VYTVLQEPGN FVITFPKSFH AGFNFGLNCA EAVNFATADW LPYGGSGAEL YRLYRKPSVI
SHEELLCVVA KGNCCNNEGS IHLKKELLRI YSKEKTWREQ LWKSGILRSS PMFVPECADS
VGIEEDPTCI ICQQFLHLSA IVCNCRPSVF ACLEHWKHLC ECEPTKLRLE YRYTLAELDM
MVQEVEKFGG CKTQETKISQ RPSSGTKRSI ALNKKEGMQV SQARPADKWL LRASKVLDAA
FSSVEYATLL KESEQFLWAG SEMDRVRDVT KSLNKAKIWA EAVSDCLSKV EGEVNDDSMK
VHLEFIDELL RVNPVPCFNS GYLKLKDYAE EARKLSEKID SALSSSPTIT QLELLHSEVS
RSPISLKKHE ILSKKISSAK MLAKRAKRYL TDAKPPGIEM DALFKLNSEM LELHVQLPET
EGILDLVKKS ESARDKSNKV LTGSLSLENV EELLHEFDSF SINVPELNIL RQYHVDTLSW
ISRFNDVMVD VREGKDQRKL ISDLSSLLRD GASLGIQVEG LPLVEVELKK ASCREKARTV
YTARKSLDFI EQLLSEAVIL HIEEEEIFVE ISGILSTARC WEERASTILE NETQMYELKD
LVRMSVNIDA VLPTLQGIEN TISSAETWLQ KSEPFLSATS SMASSPCSML ELPVLKDLVT
QAKLLNVQLQ EPRILETLLL NCERWQCDNH QLLQETEDLL DNAKIDDGTH SNILPKIMDL
ITRVDSARRS GLALGLNFDE LPKLRTASLK LGWCCKTITL SSSSPTSELL EDVGKPSLQH
IQQHLKEGQT LEILPEEYYL GKRLMELKDT GLEWAKRARK VVTDSGALAL EDVFELISEG
ENLPVHAEQE LQSLRARSML HCICLKPYNS RSMVSCSQCG EWYHTYCLKL HWRPKAYVCS
ACCPLAETTP QIDPARATEP ERPSLNQRRT RMVATDAAVN DLKWKTRKHI KRTTKRSPQV
HILPWFFT
