DXS_ARATH
ID DXS_ARATH Reviewed; 717 AA.
AC Q38854; O23407; O49738;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic;
DE Short=1-deoxyxylulose-5-phosphate synthase {ECO:0000303|PubMed:10982425};
DE Short=DXP synthase {ECO:0000303|PubMed:10982425};
DE Short=DXPS;
DE EC=2.2.1.7 {ECO:0000269|PubMed:10982425};
DE AltName: Full=Protein CLOROPLASTOS ALTERADOS 1;
DE Flags: Precursor;
GN Name=DXS; Synonyms=CLA1, DEF; OrderedLocusNames=At4g15560;
GN ORFNames=dl3821w;
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, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8653115; DOI=10.1046/j.1365-313x.1996.9050649.x;
RA Mandel M.A., Feldmann K.A., Herrera-Estrella L., Rocha-Sosa M., Leon P.;
RT "CLA1, a novel gene required for chloroplast development, is highly
RT conserved in evolution.";
RL Plant J. 9:649-658(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Camara B.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10982425; DOI=10.1104/pp.124.1.95;
RA Estevez J.M., Cantero A., Romero C., Kawaide H., Jimenez L.F., Kuzuyama T.,
RA Seto H., Kamiya Y., Leon P.;
RT "Analysis of the expression of CLA1, a gene that encodes the 1-
RT deoxyxylulose 5-phosphate synthase of the 2-C-methyl-D-erythritol-4-
RT phosphate pathway in Arabidopsis.";
RL Plant Physiol. 124:95-104(2000).
RN [8]
RP FUNCTION, AND PATHWAY.
RX PubMed=11264287; DOI=10.1074/jbc.m100854200;
RA Estevez J.M., Cantero A., Reindl A., Reichler S., Leon P.;
RT "1-Deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic
RT isoprenoid biosynthesis in plants.";
RL J. Biol. Chem. 276:22901-22909(2001).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=12447549; DOI=10.1007/s00425-002-0871-9;
RA Nagata N., Suzuki M., Yoshida S., Muranaka T.;
RT "Mevalonic acid partially restores chloroplast and etioplast development in
RT Arabidopsis lacking the non-mevalonate pathway.";
RL Planta 216:345-350(2002).
RN [10]
RP INDUCTION.
RX PubMed=15863698; DOI=10.1104/pp.104.058735;
RA Hsieh M.H., Goodman H.M.;
RT "The Arabidopsis IspH homolog is involved in the plastid nonmevalonate
RT pathway of isoprenoid biosynthesis.";
RL Plant Physiol. 138:641-653(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=18236010; DOI=10.1007/s11103-008-9297-5;
RA Hsieh M.H., Chang C.Y., Hsu S.J., Chen J.J.;
RT "Chloroplast localization of methylerythritol 4-phosphate pathway enzymes
RT and regulation of mitochondrial genes in ispD and ispE albino mutants in
RT Arabidopsis.";
RL Plant Mol. Biol. 66:663-673(2008).
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC xylulose-5-phosphate (DXP). Is a limiting enzyme for plastidic
CC isoprenoid biosynthesis and essential for chloroplast development.
CC {ECO:0000269|PubMed:10982425, ECO:0000269|PubMed:11264287,
CC ECO:0000269|PubMed:8653115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:59776; EC=2.2.1.7;
CC Evidence={ECO:0000269|PubMed:10982425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12606;
CC Evidence={ECO:0000269|PubMed:10982425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC {ECO:0000269|PubMed:10982425, ECO:0000269|PubMed:11264287}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q38854; Q9SDN0: ATJ20; NbExp=4; IntAct=EBI-4476357, EBI-6897500;
CC Q38854; Q38854: DXS; NbExp=5; IntAct=EBI-4476357, EBI-4476357;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:18236010}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10982425}.
CC -!- INDUCTION: Circadian-regulated with a peak in the late period of dark
CC phase and early period of the light phase.
CC {ECO:0000269|PubMed:15863698}.
CC -!- DISRUPTION PHENOTYPE: Albino phenotype and seedling lethal when
CC homozygous. The phenotype is caused by an early arrest in chloroplast
CC differentiation. {ECO:0000269|PubMed:10982425,
CC ECO:0000269|PubMed:12447549, ECO:0000269|PubMed:8653115}.
CC -!- MISCELLANEOUS: Plants over-expressing CLA1 show increased levels of
CC plastid isoprenoids derived from the methylerythritol 4-phosphate (MEP)
CC pathway, such as chlorophylls, tocopherols, carotenoids, abscisic acid,
CC and gibberellin (PubMed:11264287). Mutant plants treated with exogenous
CC mevalonic acid partially recover chlorophyll accumulation and plastid
CC development (PubMed:12447549). {ECO:0000305|PubMed:11264287,
CC ECO:0000305|PubMed:12447549}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74713.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U27099; AAC49368.1; -; mRNA.
DR EMBL; Y14333; CAA74713.1; ALT_INIT; mRNA.
DR EMBL; Z97339; CAB45992.1; -; Genomic_DNA.
DR EMBL; AL161542; CAB78598.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83625.1; -; Genomic_DNA.
DR EMBL; BT002340; AAN86173.1; -; mRNA.
DR PIR; H85171; H85171.
DR PIR; T52289; T52289.
DR RefSeq; NP_193291.1; NM_117647.3.
DR PDB; 7BZX; EM; 4.00 A; A/B=59-717.
DR PDB; 7BZY; EM; 3.70 A; 11/13=59-717.
DR PDBsum; 7BZX; -.
DR PDBsum; 7BZY; -.
DR AlphaFoldDB; Q38854; -.
DR SMR; Q38854; -.
DR BioGRID; 12527; 16.
DR IntAct; Q38854; 4.
DR STRING; 3702.AT4G15560.1; -.
DR BindingDB; Q38854; -.
DR ChEMBL; CHEMBL2285355; -.
DR iPTMnet; Q38854; -.
DR PaxDb; Q38854; -.
DR PRIDE; Q38854; -.
DR ProteomicsDB; 222172; -.
DR EnsemblPlants; AT4G15560.1; AT4G15560.1; AT4G15560.
DR GeneID; 827230; -.
DR Gramene; AT4G15560.1; AT4G15560.1; AT4G15560.
DR KEGG; ath:AT4G15560; -.
DR Araport; AT4G15560; -.
DR TAIR; locus:2130374; AT4G15560.
DR eggNOG; KOG0523; Eukaryota.
DR HOGENOM; CLU_009227_1_4_1; -.
DR InParanoid; Q38854; -.
DR OMA; QVGYHAQ; -.
DR OrthoDB; 354970at2759; -.
DR PhylomeDB; Q38854; -.
DR BioCyc; ARA:AT4G15560-MON; -.
DR BioCyc; MetaCyc:AT4G15560-MON; -.
DR BRENDA; 2.2.1.7; 399.
DR UniPathway; UPA00064; UER00091.
DR PRO; PR:Q38854; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38854; baseline and differential.
DR Genevisible; Q38854; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IBA:GO_Central.
DR GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:TAIR.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; TAS:TAIR.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02007; TPP_DXS; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR HAMAP; MF_00315; DXP_synth; 1.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43322; PTHR43322; 1.
DR Pfam; PF13292; DXP_synthase_N; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00204; dxs; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Plastid; Reference proteome; Thiamine biosynthesis; Thiamine pyrophosphate;
KW Transferase; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..717
FT /note="1-deoxy-D-xylulose-5-phosphate synthase,
FT chloroplastic"
FT /id="PRO_0000007393"
FT BINDING 146
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187..189
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 219..220
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="V -> I (in Ref. 2; CAA74713)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="L -> V (in Ref. 2; CAA74713)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="E -> V (in Ref. 1; AAC49368 and 2; CAA74713)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="K -> E (in Ref. 1; AAC49368 and 2; CAA74713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 76833 MW; 005A5E5585116A4F CRC64;
MASSAFAFPS YIITKGGLST DSCKSTSLSS SRSLVTDLPS PCLKPNNNSH SNRRAKVCAS
LAEKGEYYSN RPPTPLLDTI NYPIHMKNLS VKELKQLSDE LRSDVIFNVS KTGGHLGSSL
GVVELTVALH YIFNTPQDKI LWDVGHQSYP HKILTGRRGK MPTMRQTNGL SGFTKRGESE
HDCFGTGHSS TTISAGLGMA VGRDLKGKNN NVVAVIGDGA MTAGQAYEAM NNAGYLDSDM
IVILNDNKQV SLPTATLDGP SPPVGALSSA LSRLQSNPAL RELREVAKGM TKQIGGPMHQ
LAAKVDEYAR GMISGTGSSL FEELGLYYIG PVDGHNIDDL VAILKEVKST RTTGPVLIHV
VTEKGRGYPY AERADDKYHG VVKFDPATGR QFKTTNKTQS YTTYFAEALV AEAEVDKDVV
AIHAAMGGGT GLNLFQRRFP TRCFDVGIAE QHAVTFAAGL ACEGLKPFCA IYSSFMQRAY
DQVVHDVDLQ KLPVRFAMDR AGLVGADGPT HCGAFDVTFM ACLPNMIVMA PSDEADLFNM
VATAVAIDDR PSCFRYPRGN GIGVALPPGN KGVPIEIGKG RILKEGERVA LLGYGSAVQS
CLGAAVMLEE RGLNVTVADA RFCKPLDRAL IRSLAKSHEV LITVEEGSIG GFGSHVVQFL
ALDGLLDGKL KWRPMVLPDR YIDHGAPADQ LAEAGLMPSH IAATALNLIG APREALF
