LEU31_ARATH
ID LEU31_ARATH Reviewed; 409 AA.
AC Q9FMT1; Q8VXU4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=3-isopropylmalate dehydrogenase 1, chloroplastic {ECO:0000303|PubMed:15849421};
DE Short=3-IPM-DH 1 {ECO:0000303|PubMed:15849421};
DE Short=AtIMDH1 {ECO:0000303|PubMed:15849421, ECO:0000303|PubMed:19674406};
DE Short=IMDH 1 {ECO:0000303|PubMed:15849421};
DE EC=1.1.1.85 {ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:19674406, ECO:0000269|PubMed:20840499};
DE AltName: Full=Beta-IPM dehydrogenase 1 {ECO:0000303|PubMed:15849421};
DE AltName: Full=Isopropylmalate dehydrogenase 1 {ECO:0000303|PubMed:19493961};
DE Short=AtIMD1 {ECO:0000303|PubMed:19493961};
DE AltName: Full=Methylthioalkylmalate dehydrogenase 1 {ECO:0000303|PubMed:19493961};
DE Flags: Precursor;
GN Name=IMDH1 {ECO:0000303|PubMed:15849421};
GN Synonyms=IMD1 {ECO:0000303|PubMed:19493961},
GN IPMDH1 {ECO:0000303|PubMed:20840499}, MAM-D1 {ECO:0000303|PubMed:19493961};
GN OrderedLocusNames=At5g14200 {ECO:0000312|Araport:AT5G14200};
GN ORFNames=MUA22.20 {ECO:0000312|EMBL:BAB08299.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=15849421; DOI=10.1271/bbb.69.806;
RA Nozawa A., Takano J., Miwa K., Nakagawa Y., Fujiwara T.;
RT "Cloning of cDNAs encoding isopropylmalate dehydrogenase from Arabidopsis
RT thaliana and accumulation patterns of their transcripts.";
RL Biosci. Biotechnol. Biochem. 69:806-810(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19493961; DOI=10.1093/pcp/pcp079;
RA Sawada Y., Kuwahara A., Nagano M., Narisawa T., Sakata A., Saito K.,
RA Hirai M.Y.;
RT "Omics-based approaches to methionine side chain elongation in Arabidopsis:
RT characterization of the genes encoding methylthioalkylmalate isomerase and
RT methylthioalkylmalate dehydrogenase.";
RL Plant Cell Physiol. 50:1181-1190(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-232 AND CYS-390,
RP CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY WOUNDING
RP AND JASMONIC ACID, DEVELOPMENTAL STAGE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=19674406; DOI=10.1111/j.1365-313x.2009.03990.x;
RA He Y., Mawhinney T.P., Preuss M.L., Schroeder A.C., Chen B., Abraham L.,
RA Jez J.M., Chen S.;
RT "A redox-active isopropylmalate dehydrogenase functions in the biosynthesis
RT of glucosinolates and leucine in Arabidopsis.";
RL Plant J. 60:679-690(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PHE-137, TISSUE SPECIFICITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=21697089; DOI=10.1074/jbc.m111.262519;
RA He Y., Galant A., Pang Q., Strul J.M., Balogun S.F., Jez J.M., Chen S.;
RT "Structural and functional evolution of isopropylmalate dehydrogenases in
RT the leucine and glucosinolate pathways of Arabidopsis thaliana.";
RL J. Biol. Chem. 286:28794-28801(2011).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
RP ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20840499; DOI=10.1111/j.1469-8137.2010.03460.x;
RA He Y., Chen L., Zhou Y., Mawhinney T.P., Chen B., Kang B.-H., Hauser B.A.,
RA Chen S.;
RT "Functional characterization of Arabidopsis thaliana isopropylmalate
RT dehydrogenases reveals their important roles in gametophyte development.";
RL New Phytol. 189:160-175(2011).
CC -!- FUNCTION: Involved in both glucosinolate and leucine biosynthesis;
CC catalyzes the oxidative decarboxylation step in both leucine
CC biosynthesis (primary metabolism) and methionine chain elongation of
CC glucosinolates (specialized metabolism) (PubMed:19674406,
CC PubMed:19493961, PubMed:21697089). Catalyzes the oxidation of 3-
CC carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate, 3-IPM) to 3-
CC carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-
CC methyl-2 oxopentanoate (PubMed:15849421, PubMed:20840499). Required
CC during pollen development and involved in embryo sac development
CC (PubMed:20840499). More active on 3-isopropylmalate and NAD(+) than
CC towards D-malate (PubMed:19674406). {ECO:0000269|PubMed:15849421,
CC ECO:0000269|PubMed:19493961, ECO:0000269|PubMed:19674406,
CC ECO:0000269|PubMed:20840499, ECO:0000269|PubMed:21697089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.85;
CC Evidence={ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:19674406,
CC ECO:0000269|PubMed:20840499};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P93832};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P50455};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000250|UniProtKB:P50455};
CC -!- ACTIVITY REGULATION: Regulated by a thiol-based redox modification;
CC oxidation by CuCl(2) leads to a decreased activity.
CC {ECO:0000269|PubMed:19674406}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.3 uM for 3-(2'-methylthio)ethylmalate
CC {ECO:0000269|PubMed:21697089};
CC KM=25.2 uM for 3-isopropylmalate (at pH 7.5 and in reduced form)
CC {ECO:0000269|PubMed:19674406, ECO:0000269|PubMed:20840499,
CC ECO:0000269|PubMed:21697089};
CC KM=187.1 uM for NAD(+) (at pH 7.5 and in reduced form)
CC {ECO:0000269|PubMed:19674406};
CC KM=1100 uM for D-malate (at pH 7.5 and in reduced form)
CC {ECO:0000269|PubMed:19674406};
CC KM=68.62 uM for 3-isopropylmalate (at pH 7.5 and in oxidized form)
CC {ECO:0000269|PubMed:19674406};
CC KM=242.1 uM for NAD(+) (at pH 7.5 and in oxidized form)
CC {ECO:0000269|PubMed:19674406};
CC KM=1400 uM for D-malate (at pH 7.5 and in oxidized form)
CC {ECO:0000269|PubMed:19674406};
CC Vmax=0.93 umol/min/mg enzyme with 3-isopropylmalate as substrate (at
CC pH 7.5 and in reduced form) {ECO:0000269|PubMed:19674406,
CC ECO:0000269|PubMed:20840499};
CC Vmax=1.01 umol/min/mg enzyme with NAD(+) as substrate (at pH 7.5 and
CC in reduced form) {ECO:0000269|PubMed:19674406};
CC Vmax=0.16 umol/min/mg enzyme with D-malate as substrate (at pH 7.5
CC and in reduced form) {ECO:0000269|PubMed:19674406};
CC Vmax=0.45 umol/min/mg enzyme with 3-isopropylmalate as substrate (at
CC pH 7.5 and in oxidized form) {ECO:0000269|PubMed:19674406};
CC Vmax=0.82 umol/min/mg enzyme with NAD(+) as substrate (at pH 7.5 and
CC in oxidized form) {ECO:0000269|PubMed:19674406};
CC Vmax=0.11 umol/min/mg enzyme with D-malate as substrate (at pH 7.5
CC and in oxidized form) {ECO:0000269|PubMed:19674406};
CC Note=kcat is 37 min(-1) with 3-isopropylmalate as substrate
CC (PubMed:20840499, PubMed:21697089). kcat is 51 min(-1) with 3-(2'-
CC methylthio)ethylmalate as substrate (PubMed:21697089).
CC {ECO:0000269|PubMed:20840499, ECO:0000269|PubMed:21697089};
CC pH dependence:
CC Optimum pH is 7.6. {ECO:0000269|PubMed:19674406};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:19674406};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000269|PubMed:15849421,
CC ECO:0000269|PubMed:19674406, ECO:0000269|PubMed:20840499}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:19493961, ECO:0000269|PubMed:19674406}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P12010}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19674406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FMT1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings, leaves, stems and
CC roots and, to a lower extent, in flowers, pollen and siliques.
CC {ECO:0000269|PubMed:15849421, ECO:0000269|PubMed:19674406,
CC ECO:0000269|PubMed:20840499, ECO:0000269|PubMed:21697089}.
CC -!- DEVELOPMENTAL STAGE: In young seedlings, expressed in all tissues
CC except in the root tip. Later accumulates in cotyledons, newly emerging
CC leaves and the lower region of roots. In rosettes, predominantly
CC observed in the main veins of leaves. In flowers, present in petals,
CC pistils and in the ends of young siliques.
CC {ECO:0000269|PubMed:19674406}.
CC -!- INDUCTION: By wounding and jasmonic acid (MeJA).
CC {ECO:0000269|PubMed:19674406}.
CC -!- DISRUPTION PHENOTYPE: No discernible vegetative or reproductive
CC phenotypes except a slight reduction of both male and female
CC transmission efficiency, but decreased leucine biosynthetic enzyme
CC activities and lower free leucine concentrations (PubMed:19674406,
CC PubMed:20840499). The double mutant ipmdh2 ipmdh3 is lethal in male
CC gametophytes (small aborted pollen grains abnormal in cellular
CC structure, and arrested in germination) and had reduced transmission
CC through female gametophytes (slow embryo sacs development)
CC (PubMed:20840499). In atimd1-1 and atipmdh1 mutants, reduced levels of
CC methionine-derived glucosinolates (Met-GSLs) with long chains (C7-C8)
CC and, to some extent, with short chains (C4-C6) (PubMed:19493961,
CC PubMed:19674406, PubMed:21697089). Altered glucosinolate profile is
CC restored by constructs expressing IPMDH2-L134F or IPMDH3-L133F mutants
CC (PubMed:21697089). {ECO:0000269|PubMed:19493961,
CC ECO:0000269|PubMed:19674406, ECO:0000269|PubMed:20840499,
CC ECO:0000269|PubMed:21697089}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AB007650; BAB08299.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91997.1; -; Genomic_DNA.
DR EMBL; AY074587; AAL67125.1; -; mRNA.
DR RefSeq; NP_196924.1; NM_121424.6. [Q9FMT1-1]
DR AlphaFoldDB; Q9FMT1; -.
DR SMR; Q9FMT1; -.
DR BioGRID; 16547; 22.
DR STRING; 3702.AT5G14200.1; -.
DR iPTMnet; Q9FMT1; -.
DR PaxDb; Q9FMT1; -.
DR PRIDE; Q9FMT1; -.
DR EnsemblPlants; AT5G14200.1; AT5G14200.1; AT5G14200. [Q9FMT1-1]
DR GeneID; 831270; -.
DR Gramene; AT5G14200.1; AT5G14200.1; AT5G14200. [Q9FMT1-1]
DR KEGG; ath:AT5G14200; -.
DR Araport; AT5G14200; -.
DR TAIR; locus:2174668; AT5G14200.
DR eggNOG; KOG0786; Eukaryota.
DR InParanoid; Q9FMT1; -.
DR PhylomeDB; Q9FMT1; -.
DR BioCyc; ARA:AT5G14200-MON; -.
DR BioCyc; MetaCyc:AT5G14200-MON; -.
DR BRENDA; 1.1.1.85; 399.
DR UniPathway; UPA00048; UER00072.
DR PRO; PR:Q9FMT1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMT1; baseline and differential.
DR Genevisible; Q9FMT1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; ISS:TAIR.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009553; P:embryo sac development; IMP:UniProtKB.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009098; P:leucine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR HAMAP; MF_01033; LeuB_type1; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR PANTHER; PTHR42979; PTHR42979; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00169; leuB; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast; Leucine biosynthesis;
KW Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..409
FT /note="3-isopropylmalate dehydrogenase 1, chloroplastic"
FT /id="PRO_0000014455"
FT BINDING 118..133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT BINDING 322..338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT SITE 137
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:21697089"
FT SITE 185
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT SITE 232
FT /note="Essential for redox regulation"
FT /evidence="ECO:0000269|PubMed:19674406"
FT SITE 236
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P93832"
FT SITE 390
FT /note="Essential for redox regulation"
FT /evidence="ECO:0000269|PubMed:19674406"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 137
FT /note="F->L: Reduced activity toward 3-(2'-methylthio)-
FT ethylmalate, but enhanced catalytic efficiency with 3-
FT isopropylmalate."
FT /evidence="ECO:0000269|PubMed:21697089"
FT MUTAGEN 232
FT /note="C->S: Reduced sensitivity to oxidation on enzyme
FT activity regulation."
FT /evidence="ECO:0000269|PubMed:19674406"
FT MUTAGEN 390
FT /note="C->S: Reduced sensitivity to oxidation on enzyme
FT activity regulation."
FT /evidence="ECO:0000269|PubMed:19674406"
FT CONFLICT 251
FT /note="T -> A (in Ref. 4; AAL67125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44162 MW; 471293D4C3FB55DD CRC64;
MAAFLQTNIS LNAIKIVPGK YSSLTDHQFR APYRIRCAAA SPGKKRYNIA LLPGDGIGPE
VISVAKNVLQ KAGSLEGLEF DFKEMPVGGA ALDLVGVPLP EETFTAAKLS DAILLGAIGG
YKWDKNEKHL RPEMALFYLR RDLKVFANLR PATVLPQLVD ASTLKKEVAE GVDMMIVREL
TGGIYFGEPR GITINENGEE VGVSTEIYAA HEIDRIARVA FETARKRRGK LCSVDKANVL
DASILWRKRV TALASEYPDV ELSHMYVDNA AMQLIRDPKQ FDTIVTNNIF GDILSDEASM
ITGSIGMLPS ASLGESGPGL FEPIHGSAPD IAGQDKANPL ATILSAAMLL KYGLGEEKAA
KRIEDAVVDA LNKGFRTGDI YSPGNKLVGC KEMGEEVLKS VESKVPATV
