JMJ16_ARATH
ID JMJ16_ARATH Reviewed; 1209 AA.
AC C0SUT9; Q9FRS3;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative lysine-specific demethylase JMJ16 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214};
DE AltName: Full=Jumonji domain-containing protein 16 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ16 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 16 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ16 {ECO:0000305};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) monodemethylase JMJ16 {ECO:0000305};
GN Name=JMJ16 {ECO:0000303|PubMed:18713399};
GN Synonyms=PKDM7D {ECO:0000303|PubMed:20202164};
GN OrderedLocusNames=At1g08620 {ECO:0000312|Araport:AT1G08620};
GN ORFNames=F22O13.10 {ECO:0000312|EMBL:AAF99757.1};
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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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 DISRUPTION PHENOTYPE.
RX PubMed=20202164; DOI=10.1111/j.1365-313x.2010.04182.x;
RA Yang W., Jiang D., Jiang J., He Y.;
RT "A plant-specific histone H3 lysine 4 demethylase represses the floral
RT transition in Arabidopsis.";
RL Plant J. 62:663-673(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [7]
RP FUNCTION, MUTAGENESIS OF HIS-407 AND GLU-409, DISRUPTION PHENOTYPE,
RP DEVELOPMENTAL STAGE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=30712008; DOI=10.1105/tpc.18.00693;
RA Liu P., Zhang S., Zhou B., Luo X., Zhou X.F., Cai B., Jin Y.H., Niu D.,
RA Lin J., Cao X., Jin J.B.;
RT "The histone H3K4 demethylase JMJ16 represses leaf senescence in
RT Arabidopsis.";
RL Plant Cell 31:430-443(2019).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, INTERACTION WITH MMD1,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=32572214; DOI=10.1038/s41477-020-0697-0;
RA Wang J., Yu C., Zhang S., Ye J., Dai H., Wang H., Huang J., Cao X., Ma J.,
RA Ma H., Wang Y.;
RT "Cell-type-dependent histone demethylase specificity promotes meiotic
RT chromosome condensation in Arabidopsis.";
RL Nat. Plants 6:823-837(2020).
CC -!- FUNCTION: Functions as histone H3 'Lys-4' (H3K4me) demethylase involved
CC in the negative regulation of gene expression (PubMed:30712008,
CC PubMed:32572214). Active on H3K4me1, H3K4me2 and H3K4me3
CC (PubMed:30712008, PubMed:32572214). Not active on mono-, di- and
CC trimethylated H3K9, H3K27 and H3K36 in somatic cells (PubMed:30712008,
CC PubMed:32572214). However, also active on H3K9 when in complex with
CC MMD1, a meiocyte-specific histone reader (PubMed:32572214). Together
CC with MMD1, promotes gene expression in male meiocytes in an H3K9me3-
CC dependent manner, and contributes to meiotic chromosome condensation by
CC triggering some condensin promoters (e.g. CAP-D3 and CAP-H)
CC (PubMed:32572214). Together with JMJ14 and JMJ17, required for plant
CC growth and development (PubMed:31038749). Represses leaf senescence in
CC an age-dependent manner by demethylating H3K4me3 activating histone
CC marks at senescence-associated genes (SAGs) loci, including WRKY53 and
CC SAG201, thus preventing their premature expression (PubMed:30712008).
CC {ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:31038749,
CC ECO:0000269|PubMed:32572214}.
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:30712008, ECO:0000269|PubMed:32572214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60213;
CC Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214};
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:30712008,
CC ECO:0000269|PubMed:32572214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60217;
CC Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214};
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:30712008,
CC ECO:0000269|PubMed:32572214};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60221;
CC Evidence={ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:32572214};
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 MMD1 in the nucleus of male meiocytes,
CC especially on pachytene chromosomes. {ECO:0000269|PubMed:32572214}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:32572214}.
CC -!- TISSUE SPECIFICITY: Confined to inflorescences.
CC {ECO:0000269|PubMed:18713399}.
CC -!- DEVELOPMENTAL STAGE: Fades out gradually during aging.
CC {ECO:0000269|PubMed:30712008}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20202164). Abnormal accumulation of reactive oxygen
CC species (ROS) (PubMed:30712008). Hypermethylation of histone H3 'Lys-4'
CC (H3K4me3) (PubMed:30712008, PubMed:32572214). Enhanced expression of
CC genes involved in leaf senescence (e.g. WRKY53 and SAG201) associated
CC with H3K4me3 leading to an early leaf senescence phenotype
CC (PubMed:30712008, PubMed:32572214). Partial sterility with abnormally
CC short siliques and dead pollen grains leading to silique abortion
CC (PubMed:30712008, PubMed:32572214). Male meiocytes are defective in
CC meiotic chromosome condensation (PubMed:32572214). Slightly early
CC flowering (PubMed:30712008). Increased H3K9me3 levels specifically in
CC male meiocytes leading to greater number of down-regulated than up-
CC regulated genes (PubMed:32572214). The double mutant jmj17-1 jmj16-1
CC has an early flowering phenotype (especially in long day conditions)
CC (PubMed:31038749). {ECO:0000269|PubMed:20202164,
CC ECO:0000269|PubMed:30712008, ECO:0000269|PubMed:31038749,
CC ECO:0000269|PubMed:32572214}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99757.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003981; AAF99757.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28318.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28319.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM57962.1; -; Genomic_DNA.
DR EMBL; AB493442; BAH30280.1; -; mRNA.
DR PIR; G86218; G86218.
DR PIR; T00715; T00715.
DR RefSeq; NP_001184940.1; NM_001198011.2.
DR RefSeq; NP_001318955.1; NM_001331778.1.
DR RefSeq; NP_001320435.1; NM_001331779.1.
DR AlphaFoldDB; C0SUT9; -.
DR SMR; C0SUT9; -.
DR BioGRID; 22625; 3.
DR STRING; 3702.AT1G08620.1; -.
DR iPTMnet; C0SUT9; -.
DR PaxDb; C0SUT9; -.
DR PRIDE; C0SUT9; -.
DR ProteomicsDB; 232236; -.
DR EnsemblPlants; AT1G08620.1; AT1G08620.1; AT1G08620.
DR EnsemblPlants; AT1G08620.2; AT1G08620.2; AT1G08620.
DR EnsemblPlants; AT1G08620.4; AT1G08620.4; AT1G08620.
DR GeneID; 837384; -.
DR Gramene; AT1G08620.1; AT1G08620.1; AT1G08620.
DR Gramene; AT1G08620.2; AT1G08620.2; AT1G08620.
DR Gramene; AT1G08620.4; AT1G08620.4; AT1G08620.
DR KEGG; ath:AT1G08620; -.
DR Araport; AT1G08620; -.
DR TAIR; locus:2025635; AT1G08620.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_8_0_1; -.
DR InParanoid; C0SUT9; -.
DR OMA; TWEPAVE; -.
DR PhylomeDB; C0SUT9; -.
DR PRO; PR:C0SUT9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0SUT9; baseline and differential.
DR Genevisible; C0SUT9; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032183; F:SUMO binding; IPI:TAIR.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0048589; P:developmental growth; IMP:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
DR GO; GO:0010032; P:meiotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:UniProtKB.
DR GO; GO:1900056; P:negative regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:1905821; P:positive regulation of chromosome condensation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1903409; P:reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR004198; Znf_C5HC2.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Meiosis; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1209
FT /note="Putative lysine-specific demethylase JMJ16"
FT /id="PRO_0000429995"
FT DOMAIN 146..187
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 361..527
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 974..1032
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 1034..1124
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT ZN_FING 617..667
FT /note="C5HC2"
FT /evidence="ECO:0000255"
FT REGION 872..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 217..224
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 873..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 409
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 495
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 617
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 633
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 643
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT MUTAGEN 407
FT /note="H->A: Abolished H3K4 demethylase activity leading to
FT early leaf senescence; when associated with A-409."
FT /evidence="ECO:0000269|PubMed:30712008"
FT MUTAGEN 409
FT /note="E->A: Abolished H3K4 demethylase activity leading to
FT early leaf senescence; when associated with A-407."
FT /evidence="ECO:0000269|PubMed:30712008"
SQ SEQUENCE 1209 AA; 134993 MW; 45496ACCDED2E133 CRC64;
MGTELMRICV KEDSDDLPSV PPGFESYATF TLKRVVPATT SDKAKTPAIE SVSATEQAKM
EVESDEAKAA RALRRRPWIN HSGCDDDGDC AANNDNAASQ NPDQNCDVKP ALPKGVVRGC
EECKDCQKVT ARWHPDEARR PDLEDAPVFY PSEEEFEDTL NYIAKIRPEA EKYGICRIVP
PPSWKPPCPL KEKQVWEGSK FTTRVQRVDK LQNRSSMKKI SKLPNQMRKK KRKCMKMGMD
SVTNGMGDPC SASTGMNELE TFGFEPGPGF TLKDFQKYAD EFKAQYFKKS ETSTDDKCKV
DNSIDCWEPA LEDVEGEYWR IVDKATEEIE VLYGADLETG VFGSGFPKIS SSHNASSSED
KYAKSGWNLN NFPRLPGSLL KYEGSDISGV LVPWLYIGMC FSSFCWHVED HHLYSLNYMH
WGAPKLWYGV GGKDAVKLEE AMRKHLPDLF EEQPDLLHKL VTQLSPSKLK TAGVPVHRCV
QHAGEFVLTF PRAYHAGFNS GFNCAEAVNV APVDWLPHGQ IAIELYCQQG RKTSISHDKL
LLGAAREVVK ADWELNLLRK NTVDNLRWKA FSAKDGILAK TLKARIDMER TRREFLCNSS
LALKMHSNFD ATNERECCIC FFDLHLSAAG CRCSPEKYSC LTHVKELCSC PWVTKYFLFR
YDIDELNVLV EAVEGKLSSV YRWARQDLGL ALSTDVSGSK MEIDEEGKVH KDPTPQTTAL
SGKDLQLKVT SKEVSKELEK TSKLSHVNLL LKEKEEQITS SHCMKPVKEE TVCDSSDPNV
SACQPSEGGI ICMTAVKSAS GKKNSQSLPN DVILLSDDEY DIPRKRGSVR RDAISSGKKL
EIRERPTHVL ALEASAKIAA PICQREGDSL RDTRNTISLP TNDQKTMRRD VPSSTSHAEV
NAEATGLTQD ICNRMATNSH GGGKPTSCKS KNSGGLAIVD VVDGTRSSSG TPSCSQNNSP
DRFIRQKGPR IAKVVRRINC NVEPLSYGCV LSGKSWCSRR AIFPKGFRSR VKYINILDPT
NMCFYISEIL DAGRNSPLFM VYLESNPSEV FVHMSPTRCW EMVRERVNQE ITKQHKAGKS
DLPPLQPSGS PDGFEMFGYS SPAIVQAIEA LDVNRVCTDY WDSRPYSRPQ VQFPANPLLR
EANTSGRSNV GNLQLNPGHH ISPTGINSIL KVLFKKASME ELSSLQEVLS ETNSDMVTEL
VKEEIQNRR
