ID   G3PA1_ARATH             Reviewed;         396 AA.
AC   P25856; Q41184; Q9LSE6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 3.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase GAPA1, chloroplastic;
DE            EC=1.2.1.13;
DE   AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase A subunit 1;
DE   Flags: Precursor;
GN   Name=GAPA1; Synonyms=GAPA; OrderedLocusNames=At3g26650;
GN   ORFNames=MLJ15.4, MLJ15_5;
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 [GENOMIC DNA / MRNA].
RX   PubMed=1916285; DOI=10.1016/0378-1119(91)90242-4;
RA   Shih M.-C., Heinrich P., Goodman H.M.;
RT   "Cloning and chromosomal mapping of nuclear genes encoding chloroplast and
RT   cytosolic glyceraldehyde-3-phosphate-dehydrogenase from Arabidopsis
RT   thaliana.";
RL   Gene 104:133-138(1991).
RN   [2]
RP   ERRATUM OF PUBMED:1916285.
RX   PubMed=1398114; DOI=10.1016/0378-1119(92)90290-6;
RA   Shih M.-C., Heinrich P., Goodman H.M.;
RL   Gene 119:317-319(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Shoot;
RX   PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA   Quigley F., Dao P., Cottet A., Mache R.;
RT   "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT   III.";
RL   Nucleic Acids Res. 24:4313-4318(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA   Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA   Garin J., Joyard J., Rolland N.;
RT   "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT   thaliana.";
RL   Mol. Cell. Proteomics 2:325-345(2003).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15533878; DOI=10.1093/jxb/eri020;
RA   Marri L., Sparla F., Pupillo P., Trost P.;
RT   "Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate
RT   dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana.";
RL   J. Exp. Bot. 56:73-80(2005).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19675149; DOI=10.1104/pp.109.143701;
RA   Munoz-Bertomeu J., Cascales-Minana B., Mulet J.M., Baroja-Fernandez E.,
RA   Pozueta-Romero J., Kuhn J.M., Segura J., Ros R.;
RT   "Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to
RT   altered root development and affects the sugar and amino acid balance in
RT   Arabidopsis.";
RL   Plant Physiol. 151:541-558(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, AND
RP   SUBUNIT.
RX   PubMed=20516587; DOI=10.1107/s1744309110013527;
RA   Fermani S., Sparla F., Marri L., Thumiger A., Pupillo P., Falini G.,
RA   Trost P.;
RT   "Structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase
RT   (isoform A4) from Arabidopsis thaliana in complex with NAD.";
RL   Acta Crystallogr. F 66:621-626(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 60-396 IN COMPLEX WITH NAD, AND
RP   SUBUNIT.
RX   PubMed=22514274; DOI=10.1074/jbc.m112.350355;
RA   Fermani S., Trivelli X., Sparla F., Thumiger A., Calvaresi M., Marri L.,
RA   Falini G., Zerbetto F., Trost P.;
RT   "Conformational selection and folding-upon-binding of intrinsically
RT   disordered protein CP12 regulate photosynthetic enzymes assembly.";
RL   J. Biol. Chem. 287:21372-21383(2012).
CC   -!- FUNCTION: Involved in the photosynthetic reductive pentose phosphate
CC       pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-
CC       diphosphoglycerate by NADPH (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC       chains (GAPDH 1). {ECO:0000269|PubMed:20516587,
CC       ECO:0000269|PubMed:22514274}.
CC   -!- INTERACTION:
CC       P25856; Q9LZP9: CP12-2; NbExp=4; IntAct=EBI-1554434, EBI-449218;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral
CC       membrane protein. Plastid, chloroplast stroma.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and stems.
CC       {ECO:0000269|PubMed:15533878}.
CC   -!- INDUCTION: Repressed by darkness and sucrose.
CC       {ECO:0000269|PubMed:15533878}.
CC   -!- MISCELLANEOUS: Plants contain three types of GAPDH: NAD-dependent
CC       cytosolic forms which participate in glycolysis, NAD-dependent
CC       chloroplastic forms which participate in plastidic glycolysis and NADP-
CC       dependent chloroplastic forms which participate in the photosynthetic
CC       reductive pentose phosphate pathway (Calvin-Benson cycle). All the
CC       forms are encoded by distinct genes.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD10209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M64114; AAD10209.1; ALT_INIT; mRNA.
DR   EMBL; M64117; AAA32793.1; -; Genomic_DNA.
DR   EMBL; S45910; AAB23532.1; -; Genomic_DNA.
DR   EMBL; X98130; CAA66816.1; -; Genomic_DNA.
DR   EMBL; AB026648; BAB01730.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77191.1; -; Genomic_DNA.
DR   EMBL; AY058140; AAL25556.1; -; mRNA.
DR   EMBL; AY058107; AAL24215.1; -; mRNA.
DR   EMBL; AF428431; AAL16200.1; -; mRNA.
DR   EMBL; AY075637; AAL91645.1; -; mRNA.
DR   EMBL; AY142053; AAM98317.1; -; mRNA.
DR   PIR; JQ1285; JQ1285.
DR   RefSeq; NP_566796.2; NM_113576.4.
DR   PDB; 3K2B; X-ray; 2.60 A; A/B/C/D/E/F/G/H/O/Q=60-396.
DR   PDB; 3QV1; X-ray; 2.00 A; A/B/C/D/E/F=60-396.
DR   PDB; 3RVD; X-ray; 2.70 A; A/B/C/D/E/F/G/H/O/Q=61-396.
DR   PDB; 6KEZ; X-ray; 3.50 A; A/B/C/D/E/F/G/H=61-396.
DR   PDBsum; 3K2B; -.
DR   PDBsum; 3QV1; -.
DR   PDBsum; 3RVD; -.
DR   PDBsum; 6KEZ; -.
DR   AlphaFoldDB; P25856; -.
DR   SMR; P25856; -.
DR   BioGRID; 7607; 9.
DR   IntAct; P25856; 2.
DR   MINT; P25856; -.
DR   STRING; 3702.P25856; -.
DR   iPTMnet; P25856; -.
DR   PaxDb; 3702-AT3G26650-1; -.
DR   ProteomicsDB; 228893; -.
DR   EnsemblPlants; AT3G26650.1; AT3G26650.1; AT3G26650.
DR   GeneID; 822277; -.
DR   Gramene; AT3G26650.1; AT3G26650.1; AT3G26650.
DR   KEGG; ath:AT3G26650; -.
DR   Araport; AT3G26650; -.
DR   TAIR; AT3G26650; GAPA.
DR   eggNOG; KOG0657; Eukaryota.
DR   HOGENOM; CLU_030140_0_2_1; -.
DR   InParanoid; P25856; -.
DR   OrthoDB; 3165299at2759; -.
DR   PhylomeDB; P25856; -.
DR   BioCyc; ARA:AT3G26650-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G26650-MONOMER; -.
DR   BRENDA; 1.2.1.13; 399.
DR   UniPathway; UPA00116; -.
DR   EvolutionaryTrace; P25856; -.
DR   PRO; PR:P25856; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P25856; baseline and differential.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0099080; C:supramolecular complex; IDA:CAFA.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:CAFA.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0051287; F:NAD binding; IDA:CAFA.
DR   GO; GO:0050661; F:NADP binding; IDA:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR   GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   PANTHER; PTHR43148:SF13; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE GAPA1, CHLOROPLASTIC; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
DR   SWISS-2DPAGE; P25856; -.
DR   World-2DPAGE; 0003:P25856; -.
DR   Genevisible; P25856; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Calvin cycle; Chloroplast; Membrane; NADP; Oxidoreductase;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           61..396
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase GAPA1,
FT                   chloroplastic"
FT                   /id="PRO_0000010416"
FT   ACT_SITE        213
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         71..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:20516587,
FT                   ECO:0000269|PubMed:22514274"
FT   BINDING         95
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:20516587,
FT                   ECO:0000269|PubMed:22514274"
FT   BINDING         140
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:20516587,
FT                   ECO:0000269|PubMed:22514274"
FT   BINDING         212..214
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..272
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         376
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:20516587,
FT                   ECO:0000269|PubMed:22514274"
FT   SITE            240
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        172
FT                   /note="I -> M (in Ref. 1; AAA32793/AAD10209 and 3;
FT                   CAA66816)"
FT                   /evidence="ECO:0000305"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           71..81
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           99..107
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          119..129
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           147..150
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           165..173
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          177..183
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          206..209
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           213..229
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          231..241
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           273..280
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           282..284
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          288..296
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          301..311
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           315..327
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            328..333
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          334..337
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           343..346
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          352..356
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           357..359
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   TURN            364..366
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   STRAND          367..374
FT                   /evidence="ECO:0007829|PDB:3QV1"
FT   HELIX           378..393
FT                   /evidence="ECO:0007829|PDB:3QV1"
SQ   SEQUENCE   396 AA;  42490 MW;  FFD7FD662FB222FC CRC64;
     MASVTFSVPK GFTEFSGLRS SSASLPFGKK LSSDEFVSIV SFQTSAMGSS GGYRKGVTEA
     KLKVAINGFG RIGRNFLRCW HGRKDSPLDI IAINDTGGVK QASHLLKYDS TLGIFDADVK
     PSGETAISVD GKIIQVVSNR NPSLLPWKEL GIDIVIEGTG VFVDREGAGK HIEAGAKKVI
     ITAPGKGDIP TYVVGVNADA YSHDEPIISN ASCTTNCLAP FVKVLDQKFG IIKGTMTTTH
     SYTGDQRLLD ASHRDLRRAR AAALNIVPTS TGAAKAVALV LPNLKGKLNG IALRVPTPNV
     SVVDLVVQVS KKTFAEEVNA AFRDSAEKEL KGILDVCDEP LVSVDFRCSD FSTTIDSSLT
     MVMGDDMVKV IAWYDNEWGY SQRVVDLADI VANNWK
//