JMJ24_ARATH
ID JMJ24_ARATH Reviewed; 944 AA.
AC F4HZD1; B9DFI4; B9DGQ5; C0SUU1; O04024; Q0WLZ4;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=E3 ubiquitin-protein ligase JMJ24 {ECO:0000303|PubMed:26798133, ECO:0000303|PubMed:26979329};
DE EC=2.3.2.27 {ECO:0000269|PubMed:26798133, ECO:0000269|PubMed:26979329};
DE AltName: Full=Inactive histone demethylase JMJ24 {ECO:0000303|PubMed:18713399, ECO:0000303|PubMed:26979329};
DE AltName: Full=Jumonji domain-containing protein 24 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ24 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 24 {ECO:0000303|PubMed:18713399};
GN Name=JMJ24 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At1g09060 {ECO:0000312|Araport:AT1G09060};
GN ORFNames=F7G19.7 {ECO:0000312|EMBL:AAB70402.1};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-911 (ISOFORM 2).
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 557-944 (ISOFORM 1/2).
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 [6]
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RDR2, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26119694; DOI=10.1111/tpj.12924;
RA Deng S., Xu J., Liu J., Kim S.-H., Shi S., Chua N.-H.;
RT "JMJ24 binds to RDR2 and is required for the basal level transcription of
RT silenced loci in Arabidopsis.";
RL Plant J. 83:770-782(2015).
RN [8]
RP FUNCTION, MUTAGENESIS OF CYS-243; HIS-244 AND CYS-263, CATALYTIC ACTIVITY,
RP PTM, DOMAIN, SUBUNIT, AND INTERACTION WITH CMT3.
RC STRAIN=cv. Columbia;
RX PubMed=26798133; DOI=10.1101/gad.274647.115;
RA Deng S., Jang I.-C., Su L., Xu J., Chua N.-H.;
RT "JMJ24 targets CHROMOMETHYLASE3 for proteasomal degradation in
RT Arabidopsis.";
RL Genes Dev. 30:251-256(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, PTM, INTERACTION WITH
RP UBC10, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=26979329; DOI=10.1104/pp.15.01688;
RA Kabelitz T., Brzezinka K., Friedrich T., Gorka M., Graf A., Kappel C.,
RA Baeurle I.;
RT "A JUMONJI protein with E3 ligase and histone H3 binding activities affects
RT transposon silencing in Arabidopsis.";
RL Plant Physiol. 171:344-358(2016).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=28400174; DOI=10.1016/j.gep.2017.04.001;
RA Audonnet L., Shen Y., Zhou D.-X.;
RT "JMJ24 antagonizes histone H3K9 demethylase IBM1/JMJ25 function and
RT interacts with RNAi pathways for gene silencing.";
RL Gene Expr. Patterns 25:1-7(2017).
CC -!- FUNCTION: Binds histone H3 but seems to have lost demethylase activity
CC probably due to its inability to bind iron Fe(2+) (PubMed:26979329).
CC Possesses E3 ubiquitin ligase activity and targets directly CMT3 for
CC proteasomal degradation to initiate destabilization of the
CC heterochromatic state (e.g. CHG cytosine methylation and H3K9me2) of
CC endogenous silenced loci (PubMed:26798133, PubMed:26979329). Required
CC for the removal of repressive H3K9me2 histone marks to facilitate the
CC transcription of AtSN1, AtMu1c, solo LTR and SDC, thus counteracting
CC their transcriptional silencing (PubMed:26119694, PubMed:26979329).
CC Mainly required to promote the basal level transcription of silenced
CC loci such as TE and repeats targeted by RNA-dependent DNA methylation
CC (RdDM) for silencing, a specialized branch of the RNA interference
CC (RNAi) pathway (PubMed:26119694, PubMed:28400174, PubMed:26979329).
CC Cooperates also with RNAi pathways for gene silencing both by
CC contributing to the production of 24-nt siRNA to initiate RdDM and by
CC recruiting RDR2 to enable local transcripts to make dsRNA
CC (PubMed:26119694, PubMed:28400174). Antagonizes histone H3K9
CC demethylase IBM1/JMJ25 function (PubMed:28400174).
CC {ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26798133,
CC ECO:0000269|PubMed:26979329, ECO:0000269|PubMed:28400174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:26798133,
CC ECO:0000269|PubMed:26979329};
CC -!- SUBUNIT: Homodimer (PubMed:26798133). Interacts with RDR2
CC (PubMed:26119694). Binds to CMT3 (PubMed:26798133). Associates with the
CC E2 ubiquitin-conjugating enzyme UBC10 (PubMed:26979329).
CC {ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26798133,
CC ECO:0000269|PubMed:26979329}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26979329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HZD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HZD1-2; Sequence=VSP_061594;
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, flowers, roots,
CC siliques, leaves and stems, especially in the vasculature (mainly
CC phloem), with highest levels in floral organs.
CC {ECO:0000269|PubMed:18713399, ECO:0000269|PubMed:28400174}.
CC -!- DOMAIN: The RING-type domain is necessary for E3 ubiquitin ligase
CC activity. {ECO:0000269|PubMed:26798133}.
CC -!- DOMAIN: The JmjC domain is involved in histone H3 binding.
CC {ECO:0000269|PubMed:26979329}.
CC -!- PTM: Self-ubiquitinates. {ECO:0000269|PubMed:26798133,
CC ECO:0000269|PubMed:26979329}.
CC -!- DISRUPTION PHENOTYPE: Reduced RNA-dependent DNA methylation (RdDM)
CC target transcripts levels (PubMed:26119694). Increased DNA (e.g. CHG
CC cytosine methylation) and histone (e.g. H3K9me2) methylation, including
CC on FWA, QQS and SDC loci and on retrotransposon-derived solo long
CC terminal repeat (solo LTR), AtSN1 and SDC loci leading to their reduced
CC expression (PubMed:26119694, PubMed:26798133). Increased silencing of
CC the DNA transposon AtMu1c leading to slightly decreased transcript
CC levels (PubMed:26979329). Lower 24-nt small RNAs (smRNAs) accumulation
CC as a result of AtSN1 derepression (PubMed:26119694). The double mutant
CC rdr2-1 jmj24-1 exhibits an increased expression of retrotransposon-
CC derived solo long terminal repeat (solo LTR) and SDC due to their
CC derepression (PubMed:26119694). Several subtle developmental defects
CC (e.g. slightly larger organ, abnormal floral organs and altered
CC inflorescence branching) by modified expression of a relatively small
CC number of genes at the vegetative stage (PubMed:28400174). Complements
CC partially growth defects and expression changes caused by the loss of
CC JMJ25/IBM1 mostly at vegetative stage, but the double mutant jmj24-3
CC ibm1-4 has synergistic effect on root growth (PubMed:28400174).
CC {ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:26798133,
CC ECO:0000269|PubMed:26979329, ECO:0000269|PubMed:28400174}.
CC -!- MISCELLANEOUS: Misses iron Fe(2+)-binding sites required for
CC demethylase activity. {ECO:0000269|PubMed:26979329}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70402.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC000106; AAB70402.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28388.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28389.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28390.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61128.1; -; Genomic_DNA.
DR EMBL; AK316783; BAH19501.1; -; mRNA.
DR EMBL; AK317241; BAH19922.1; -; mRNA.
DR EMBL; AB493444; BAH30282.1; -; mRNA.
DR EMBL; AK230041; BAF01863.1; -; mRNA.
DR PIR; F86222; F86222.
DR RefSeq; NP_001031007.1; NM_001035930.1.
DR RefSeq; NP_001318961.1; NM_001331803.1.
DR RefSeq; NP_172380.2; NM_100777.3.
DR RefSeq; NP_973798.1; NM_202069.3.
DR SMR; F4HZD1; -.
DR STRING; 3702.AT1G09060.3; -.
DR PRIDE; F4HZD1; -.
DR ProteomicsDB; 183538; -.
DR EnsemblPlants; AT1G09060.3; AT1G09060.3; AT1G09060.
DR EnsemblPlants; AT1G09060.4; AT1G09060.4; AT1G09060.
DR GeneID; 837427; -.
DR Gramene; AT1G09060.3; AT1G09060.3; AT1G09060.
DR Gramene; AT1G09060.4; AT1G09060.4; AT1G09060.
DR KEGG; ath:AT1G09060; -.
DR Araport; AT1G09060; -.
DR TAIR; locus:2036014; AT1G09060.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_0_1; -.
DR InParanoid; F4HZD1; -.
DR OMA; WYSDIPI; -.
DR OrthoDB; 1185631at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HZD1; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031011; C:Ino80 complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0010425; P:DNA methylation on cytosine within a CNG sequence; IMP:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:UniProtKB.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:TAIR.
DR GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0070920; P:regulation of production of small RNA involved in gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR014977; WRC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF08879; WRC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51667; WRC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..944
FT /note="E3 ubiquitin-protein ligase JMJ24"
FT /id="PRO_0000456191"
FT DOMAIN 38..83
FT /note="WRC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01002"
FT DOMAIN 621..873
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 217..269
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT MOTIF 73..80
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 323..330
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT VAR_SEQ 1..14
FT /note="Missing (in isoform 2)"
FT /id="VSP_061594"
FT MUTAGEN 243
FT /note="C->S: Impaired self-ubiquitination and E3 ubiquitin
FT ligase activity; when associated with S-263."
FT /evidence="ECO:0000269|PubMed:26798133"
FT MUTAGEN 244
FT /note="H->A: Impaired self-ubiquitination and E3 ubiquitin
FT ligase activity; when associated with S-263."
FT /evidence="ECO:0000269|PubMed:26798133"
FT MUTAGEN 263
FT /note="C->S: Impaired self-ubiquitination and E3 ubiquitin
FT ligase activity; when associated with S-243. Impaired self-
FT ubiquitination and E3 ubiquitin ligase activity; when
FT associated with A-244."
FT /evidence="ECO:0000269|PubMed:26798133"
SQ SEQUENCE 944 AA; 107230 MW; 925BA57062AE4BD8 CRC64;
MQVNFDETCD SVIRMNANEQ TRSANGIGNG NGESIPGIPD DLRCKRSDGK QWRCTAMSMA
DKTVCEKHYI QAKKRAANSA FRANQKKAKR RSSLGETDTY SEGKMDDFEL PVTSIDHYNN
GLASASKSNG RLEKRHNKSL MRYSPETPMM RSFSPRVAVD LNDDLGRDVV MFEEGYRSYR
TPPSVAVMDP TRNRSHQSTS PMEYSAASTD VSAESLGEIC HQCQRKDRER IISCLKCNQR
AFCHNCLSAR YSEISLEEVE KVCPACRGLC DCKSCLRSDN TIKVRIREIP VLDKLQYLYR
LLSAVLPVIK QIHLEQCMEV ELEKRLREVE IDLVRARLKA DEQMCCNVCR IPVVDYYRHC
PNCSYDLCLR CCQDLREESS VTISGTNQNV QDRKGAPKLK LNFSYKFPEW EANGDGSIPC
PPKEYGGCGS HSLNLARIFK MNWVAKLVKN AEEIVSGCKL SDLLNPDMCD SRFCKFAERE
ESGDNYVYSP SLETIKTDGV AKFEQQWAEG RLVTVKMVLD DSSCSRWDPE TIWRDIDELS
DEKLREHDPF LKAINCLDGL EVDVRLGEFT RAYKDGKNQE TGLPLLWKLK DWPSPSASEE
FIFYQRPEFI RSFPFLEYIH PRLGLLNVAA KLPHYSLQND SGPKIYVSCG TYQEISAGDS
LTGIHYNMRD MVYLLVHTSE ETTFERVRKT KPVPEEPDQK MSENESLLSP EQKLRDGELH
DLSLGEASME KNEPELALTV NPENLTENGD NMESSCTSSC AGGAQWDVFR RQDVPKLSGY
LQRTFQKPDN IQTDFVSRPL YEGLFLNEHH KRQLRDEFGV EPWTFEQHRG EAIFIPAGCP
FQITNLQSNI QVALDFLCPE SVGESARLAE EIRCLPNDHE AKLQILEIGK ISLYAASSAI
KEVQKLVLDP KFGAELGFED SNLTKAVSHN LDEATKRPQQ NSCT
