HSP7C_ARATH
ID HSP7C_ARATH Reviewed; 649 AA.
AC O65719; Q42345; Q56WH5; Q96267;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Heat shock 70 kDa protein 3 {ECO:0000303|PubMed:11599561, ECO:0000303|Ref.7};
DE Short=AtHsp70-3 {ECO:0000303|PubMed:11599561, ECO:0000303|Ref.7};
DE Short=Heat shock protein 70-3 {ECO:0000303|PubMed:11599561, ECO:0000303|Ref.7};
DE AltName: Full=Heat shock cognate 70 kDa protein 3 {ECO:0000303|Ref.1};
DE Short=AtHsc70-3 {ECO:0000303|Ref.1};
DE Short=Heat shock cognate protein 70-3 {ECO:0000303|Ref.1};
GN Name=HSP70-3 {ECO:0000303|PubMed:11599561, ECO:0000303|Ref.7};
GN Synonyms=HSC70-3 {ECO:0000303|Ref.1}, HSC70-G7;
GN OrderedLocusNames=At3g09440 {ECO:0000312|Araport:AT3G09440};
GN ORFNames=F11F8 {ECO:0000312|EMBL:AAF23276.1},
GN F3L24.33 {ECO:0000312|EMBL:AAF14038.1};
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].
RC STRAIN=cv. Columbia;
RA Hsieh K., Wang Y.-C., Lin B.-L.;
RT "At-hsc70-3 encodes a cytosolic Hsp70 in Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-139(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-117.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-649.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 550-649.
RC STRAIN=cv. Columbia;
RA Wang Y.C., Lee S.P., Shieh K., Hu S.M., Wang C., Lin B.L.;
RT "Specific Hsp70s are expressed and accumulated during silique development
RT in Arabidopsis.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:gaoths>2.0.co;2;
RA Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.;
RT "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
RL Cell Stress Chaperones 6:201-208(2001).
RN [9]
RP DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11402207; DOI=10.1104/pp.126.2.789;
RA Sung D.Y., Vierling E., Guy C.L.;
RT "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene
RT family.";
RL Plant Physiol. 126:789-800(2001).
RN [10]
RP SUBUNIT.
RX PubMed=11752432; DOI=10.1073/pnas.011578198;
RA Wolucka B.A., Persiau G., Van Doorsselaere J., Davey M.W., Demol H.,
RA Vandekerckhove J., Van Montagu M., Zabeau M., Boerjan W.;
RT "Partial purification and identification of GDP-mannose 3',5'-epimerase of
RT Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14843-14848(2001).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12954627; DOI=10.1074/jbc.m309135200;
RA Wolucka B.A., Van Montagu M.;
RT "GDP-mannose 3',5'-epimerase forms GDP-L-gulose, a putative intermediate
RT for the de novo biosynthesis of vitamin C in plants.";
RL J. Biol. Chem. 278:47483-47490(2003).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=14505352; DOI=10.1002/jcb.10624;
RA Calikowski T.T., Meulia T., Meier I.;
RT "A proteomic study of the Arabidopsis nuclear matrix.";
RL J. Cell. Biochem. 90:361-378(2003).
RN [13]
RP INDUCTION.
RX PubMed=15805473; DOI=10.1104/pp.104.058958;
RA Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
RT "Virus induction of heat shock protein 70 reflects a general response to
RT protein accumulation in the plant cytosol.";
RL Plant Physiol. 138:529-536(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [15]
RP INTERACTION WITH SGT1B.
RX PubMed=18065690; DOI=10.1105/tpc.107.051896;
RA Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
RA Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
RT "Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates
RT Arabidopsis immune responses.";
RL Plant Cell 19:4061-4076(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [17]
RP INTERACTION WITH WPP1.
RX PubMed=19617588; DOI=10.1104/pp.109.143404;
RA Brkljacic J., Zhao Q., Meier I.;
RT "WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
RT preventing mistargeting of RanGAP1-anchoring protein WIT1.";
RL Plant Physiol. 151:142-154(2009).
RN [18]
RP INTERACTION WITH AMSH3.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
RN [19]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s are key
CC components that facilitate folding of de novo synthesized proteins,
CC assist translocation of precursor proteins into organelles, and are
CC responsible for degradation of damaged protein under stress conditions.
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts with GDP-mannose 3,5-epimerase and SGT1B (via SGS
CC domain). Binds to the deubiquitinating enzyme AMSH3. Interacts with
CC WPP1. Interacts with DEK3 (PubMed:25387881).
CC {ECO:0000269|PubMed:11752432, ECO:0000269|PubMed:18065690,
CC ECO:0000269|PubMed:19617588, ECO:0000269|PubMed:20543027,
CC ECO:0000269|PubMed:25387881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14505352}. Nucleus
CC matrix {ECO:0000269|PubMed:14505352}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC regulated during germination. {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: By heat shock and by cold. Up-regulated by virus infection.
CC {ECO:0000269|PubMed:11402207, ECO:0000269|PubMed:15805473}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
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DR EMBL; Y17053; CAA76606.1; -; mRNA.
DR EMBL; AC011436; AAF14038.1; -; Genomic_DNA.
DR EMBL; AC016661; AAF23276.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74767.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74768.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64320.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64321.1; -; Genomic_DNA.
DR EMBL; AY050896; AAK92833.1; -; mRNA.
DR EMBL; AY096676; AAM20310.1; -; mRNA.
DR EMBL; AY102116; AAM26685.1; -; mRNA.
DR EMBL; BT001066; AAN46823.1; -; mRNA.
DR EMBL; F20026; CAA23383.1; -; mRNA.
DR EMBL; AK222065; BAD94875.1; -; mRNA.
DR EMBL; Y08903; CAA70111.1; -; mRNA.
DR RefSeq; NP_001189847.1; NM_001202918.1.
DR RefSeq; NP_001319509.1; NM_001337819.1.
DR RefSeq; NP_001319510.1; NM_001337820.1.
DR RefSeq; NP_187555.1; NM_111778.4.
DR AlphaFoldDB; O65719; -.
DR SMR; O65719; -.
DR BioGRID; 5436; 29.
DR IntAct; O65719; 4.
DR STRING; 3702.AT3G09440.1; -.
DR iPTMnet; O65719; -.
DR MetOSite; O65719; -.
DR SwissPalm; O65719; -.
DR SWISS-2DPAGE; O65719; -.
DR World-2DPAGE; 0003:O65719; -.
DR PaxDb; O65719; -.
DR PRIDE; O65719; -.
DR ProteomicsDB; 230157; -.
DR EnsemblPlants; AT3G09440.1; AT3G09440.1; AT3G09440.
DR EnsemblPlants; AT3G09440.2; AT3G09440.2; AT3G09440.
DR EnsemblPlants; AT3G09440.3; AT3G09440.3; AT3G09440.
DR EnsemblPlants; AT3G09440.4; AT3G09440.4; AT3G09440.
DR GeneID; 820102; -.
DR Gramene; AT3G09440.1; AT3G09440.1; AT3G09440.
DR Gramene; AT3G09440.2; AT3G09440.2; AT3G09440.
DR Gramene; AT3G09440.3; AT3G09440.3; AT3G09440.
DR Gramene; AT3G09440.4; AT3G09440.4; AT3G09440.
DR KEGG; ath:AT3G09440; -.
DR Araport; AT3G09440; -.
DR TAIR; locus:2074984; AT3G09440.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; O65719; -.
DR OMA; NCGQHAG; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; O65719; -.
DR PRO; PR:O65719; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O65719; baseline and differential.
DR Genevisible; O65719; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Nucleus;
KW Reference proteome; Stress response.
FT CHAIN 1..649
FT /note="Heat shock 70 kDa protein 3"
FT /id="PRO_0000078346"
FT REGION 619..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 113..117
FT /note="GEDKE -> EKIKS (in Ref. 5; CAA23383)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="R -> T (in Ref. 7; CAA70111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 649 AA; 71148 MW; 453268ED6E60E152 CRC64;
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPINTV FDAKRLIGRR FTDSSVQSDI KLWPFTLKSG PAEKPMIVVN YKGEDKEFSA
EEISSMILIK MREIAEAYLG TTIKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP
TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKNKKDIS GNPRALRRLR TACERAKRTL SSTAQTTIEI DSLFDGIDFY
APITRARFEE LNIDLFRKCM EPVEKCLRDA KMDKNSIDDV VLVGGSTRIP KVQQLLVDFF
NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTVLI
QRNTTIPTKK EQVFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKDE IEKMVQEAEK YKSEDEEHKK
KVDAKNALEN YAYNMRNTIR DEKIGEKLAG DDKKKIEDSI EAAIEWLEAN QLAECDEFED
KMKELESICN PIIAKMYQGG EAGGPAAGGM DEDVPPSAGG AGPKIEEVD
