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Heat shock 70 kDa protein 3 (Heat shock cognate 70 kDa protein 3) (Heat shock cognate protein 70-3) (AtHsc70-3) (Heat shock protein 70-3) (AtHsp70-3)

 HSP7C_ARATH             Reviewed;         649 AA.
O65719; Q42345; Q56WH5; Q96267;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 143.
RecName: Full=Heat shock 70 kDa protein 3;
AltName: Full=Heat shock cognate 70 kDa protein 3;
AltName: Full=Heat shock cognate protein 70-3;
Short=AtHsc70-3;
AltName: Full=Heat shock protein 70-3;
Short=AtHsp70-3;
Name=HSP70-3; Synonyms=HSC70-3, HSC70-G7; OrderedLocusNames=At3g09440;
ORFNames=F11F8, F3L24.33;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Hsieh K., Wang Y.-C., Lin B.-L.;
"At-hsc70-3 encodes a cytosolic Hsp70 in Arabidopsis thaliana.";
(er) Plant Gene Register PGR98-139(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-117.
STRAIN=cv. Columbia;
PubMed=8580968; DOI=10.1046/j.1365-313X.1996.09010101.x;
Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y.,
Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
Hoefte H.;
"Further progress towards a catalogue of all Arabidopsis genes:
analysis of a set of 5000 non-redundant ESTs.";
Plant J. 9:101-124(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-649.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 550-649.
STRAIN=cv. Columbia;
Wang Y.C., Lee S.P., Shieh K., Hu S.M., Wang C., Lin B.L.;
"Specific Hsp70s are expressed and accumulated during silique
development in Arabidopsis.";
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:GAOTHS>2.0.CO;2;
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A.,
Delseny M.;
"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
Cell Stress Chaperones 6:201-208(2001).
[9]
DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
PubMed=11402207; DOI=10.1104/pp.126.2.789;
Sung D.Y., Vierling E., Guy C.L.;
"Comprehensive expression profile analysis of the Arabidopsis Hsp70
gene family.";
Plant Physiol. 126:789-800(2001).
[10]
SUBUNIT.
PubMed=11752432; DOI=10.1073/pnas.011578198;
Wolucka B.A., Persiau G., Van Doorsselaere J., Davey M.W., Demol H.,
Vandekerckhove J., Van Montagu M., Zabeau M., Boerjan W.;
"Partial purification and identification of GDP-mannose 3',5'-
epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C
pathway.";
Proc. Natl. Acad. Sci. U.S.A. 98:14843-14848(2001).
[11]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12954627; DOI=10.1074/jbc.M309135200;
Wolucka B.A., Van Montagu M.;
"GDP-mannose 3',5'-epimerase forms GDP-L-gulose, a putative
intermediate for the de novo biosynthesis of vitamin C in plants.";
J. Biol. Chem. 278:47483-47490(2003).
[12]
SUBCELLULAR LOCATION.
PubMed=14505352; DOI=10.1002/jcb.10624;
Calikowski T.T., Meulia T., Meier I.;
"A proteomic study of the Arabidopsis nuclear matrix.";
J. Cell. Biochem. 90:361-378(2003).
[13]
INDUCTION.
PubMed=15805473; DOI=10.1104/pp.104.058958;
Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
"Virus induction of heat shock protein 70 reflects a general response
to protein accumulation in the plant cytosol.";
Plant Physiol. 138:529-536(2005).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[15]
INTERACTION WITH SGT1B.
PubMed=18065690; DOI=10.1105/tpc.107.051896;
Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
"Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones
regulates Arabidopsis immune responses.";
Plant Cell 19:4061-4076(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[17]
INTERACTION WITH WPP1.
PubMed=19617588; DOI=10.1104/pp.109.143404;
Brkljacic J., Zhao Q., Meier I.;
"WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
preventing mistargeting of RanGAP1-anchoring protein WIT1.";
Plant Physiol. 151:142-154(2009).
[18]
INTERACTION WITH AMSH3.
PubMed=20543027; DOI=10.1105/tpc.110.075952;
Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F.,
Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.;
"The deubiquitinating enzyme AMSH3 is required for intracellular
trafficking and vacuole biogenesis in Arabidopsis thaliana.";
Plant Cell 22:1826-1837(2010).
-!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
preexistent proteins against aggregation and mediate the folding
of newly translated polypeptides in the cytosol as well as within
organelles. These chaperones participate in all these processes
through their ability to recognize nonnative conformations of
other proteins. They bind extended peptide segments with a net
hydrophobic character exposed by polypeptides during translation
and membrane translocation, or following stress-induced damage (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with GDP-mannose 3,5-epimerase and SGT1B (via
SGS domain). Binds to the deubiquitinating enzyme AMSH3. Interacts
with WPP1. {ECO:0000269|PubMed:11752432,
ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19617588,
ECO:0000269|PubMed:20543027}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14505352}.
Nucleus matrix {ECO:0000269|PubMed:14505352}.
-!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
regulated during germination. {ECO:0000269|PubMed:11402207}.
-!- INDUCTION: By heat shock and by cold. Up-regulated by virus
infection. {ECO:0000269|PubMed:11402207,
ECO:0000269|PubMed:15805473}.
-!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33)
family. DnaK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y17053; CAA76606.1; -; mRNA.
EMBL; AC011436; AAF14038.1; -; Genomic_DNA.
EMBL; AC016661; AAF23276.1; -; Genomic_DNA.
EMBL; CP002686; AEE74767.1; -; Genomic_DNA.
EMBL; CP002686; AEE74768.1; -; Genomic_DNA.
EMBL; CP002686; ANM64320.1; -; Genomic_DNA.
EMBL; CP002686; ANM64321.1; -; Genomic_DNA.
EMBL; AY050896; AAK92833.1; -; mRNA.
EMBL; AY096676; AAM20310.1; -; mRNA.
EMBL; AY102116; AAM26685.1; -; mRNA.
EMBL; BT001066; AAN46823.1; -; mRNA.
EMBL; F20026; CAA23383.1; -; mRNA.
EMBL; AK222065; BAD94875.1; -; mRNA.
EMBL; Y08903; CAA70111.1; -; mRNA.
RefSeq; NP_001189847.1; NM_001202918.1.
RefSeq; NP_001319509.1; NM_001337819.1.
RefSeq; NP_001319510.1; NM_001337820.1.
RefSeq; NP_187555.1; NM_111778.4.
UniGene; At.22293; -.
ProteinModelPortal; O65719; -.
SMR; O65719; -.
BioGrid; 5436; 17.
IntAct; O65719; 3.
STRING; 3702.AT3G09440.1; -.
iPTMnet; O65719; -.
SwissPalm; O65719; -.
SWISS-2DPAGE; O65719; -.
World-2DPAGE; 0003:O65719; -.
PaxDb; O65719; -.
PRIDE; O65719; -.
EnsemblPlants; AT3G09440.1; AT3G09440.1; AT3G09440.
EnsemblPlants; AT3G09440.2; AT3G09440.2; AT3G09440.
EnsemblPlants; AT3G09440.3; AT3G09440.3; AT3G09440.
EnsemblPlants; AT3G09440.4; AT3G09440.4; AT3G09440.
GeneID; 820102; -.
Gramene; AT3G09440.1; AT3G09440.1; AT3G09440.
Gramene; AT3G09440.2; AT3G09440.2; AT3G09440.
Gramene; AT3G09440.3; AT3G09440.3; AT3G09440.
Gramene; AT3G09440.4; AT3G09440.4; AT3G09440.
KEGG; ath:AT3G09440; -.
Araport; AT3G09440; -.
TAIR; locus:2074984; AT3G09440.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228135; -.
InParanoid; O65719; -.
KO; K03283; -.
OMA; MILIKMR; -.
OrthoDB; EOG093604KP; -.
PhylomeDB; O65719; -.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-ATH-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-ATH-3371568; Attenuation phase.
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-8876725; Protein methylation.
PRO; PR:O65719; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; O65719; baseline and differential.
Genevisible; O65719; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0022626; C:cytosolic ribosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009408; P:response to heat; IEP:UniProtKB.
GO; GO:0080167; P:response to karrikin; IEP:TAIR.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Reference proteome; Stress response.
CHAIN 1 649 Heat shock 70 kDa protein 3.
/FTId=PRO_0000078346.
CONFLICT 113 117 GEDKE -> EKIKS (in Ref. 5; CAA23383).
{ECO:0000305}.
CONFLICT 556 556 R -> T (in Ref. 7; CAA70111).
{ECO:0000305}.
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


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