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Protein

Heat shock 70 kDa protein 3

Gene

HSP70-3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protease binding Source: UniProtKB

GO - Biological processi

  • response to cadmium ion Source: TAIR
  • response to heat Source: UniProtKB
  • response to karrikin Source: TAIR
  • response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:GQT-199-MONOMER.
ARA:GQT-37-MONOMER.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 3
Alternative name(s):
Heat shock cognate 70 kDa protein 3
Heat shock cognate protein 70-3
Short name:
AtHsc70-3
Heat shock protein 70-3
Short name:
AtHsp70-3
Gene namesi
Name:HSP70-3
Synonyms:HSC70-3, HSC70-G7
Ordered Locus Names:At3g09440
ORF Names:F11F8, F3L24.33
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G09440.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • cytosolic ribosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • nuclear matrix Source: UniProtKB
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuolar membrane Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 649648Heat shock 70 kDa protein 3PRO_0000078346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki457 – 457Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO65719.
PRIDEiO65719.

2D gel databases

SWISS-2DPAGEO65719.
World-2DPAGE0003:O65719.

PTM databases

iPTMnetiO65719.
SwissPalmiO65719.

Expressioni

Developmental stagei

Down-regulated during seed maturation. Up-regulated during germination.1 Publication

Inductioni

By heat shock and by cold. Up-regulated by virus infection.2 Publications

Gene expression databases

GenevisibleiO65719. AT.

Interactioni

Subunit structurei

Interacts with GDP-mannose 3,5-epimerase and SGT1B (via SGS domain). Binds to the deubiquitinating enzyme AMSH3. Interacts with WPP1.4 Publications

GO - Molecular functioni

  • protease binding Source: UniProtKB

Protein-protein interaction databases

BioGridi5436. 15 interactions.
IntActiO65719. 3 interactions.
STRINGi3702.AT3G09440.1.

Structurei

3D structure databases

ProteinModelPortaliO65719.
SMRiO65719. Positions 6-619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiO65719.
KOiK03283.
OMAiDFYAPIT.
PhylomeDBiO65719.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O65719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS
60 70 80 90 100
ERLIGDAAKN QVAMNPINTV FDAKRLIGRR FTDSSVQSDI KLWPFTLKSG
110 120 130 140 150
PAEKPMIVVN YKGEDKEFSA EEISSMILIK MREIAEAYLG TTIKNAVVTV
160 170 180 190 200
PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP TAAAIAYGLD KKATSVGEKN
210 220 230 240 250
VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD NRMVNHFVQE
260 270 280 290 300
FKRKNKKDIS GNPRALRRLR TACERAKRTL SSTAQTTIEI DSLFDGIDFY
310 320 330 340 350
APITRARFEE LNIDLFRKCM EPVEKCLRDA KMDKNSIDDV VLVGGSTRIP
360 370 380 390 400
KVQQLLVDFF NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL
410 420 430 440 450
DVTPLSLGLE TAGGVMTVLI QRNTTIPTKK EQVFSTYSDN QPGVLIQVYE
460 470 480 490 500
GERARTKDNN LLGKFELSGI PPAPRGVPQI TVCFDIDANG ILNVSAEDKT
510 520 530 540 550
TGQKNKITIT NDKGRLSKDE IEKMVQEAEK YKSEDEEHKK KVDAKNALEN
560 570 580 590 600
YAYNMRNTIR DEKIGEKLAG DDKKKIEDSI EAAIEWLEAN QLAECDEFED
610 620 630 640
KMKELESICN PIIAKMYQGG EAGGPAAGGM DEDVPPSAGG AGPKIEEVD
Length:649
Mass (Da):71,148
Last modified:August 1, 1998 - v1
Checksum:i453268ED6E60E152
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1175GEDKE → EKIKS in CAA23383 (PubMed:8580968).Curated
Sequence conflicti556 – 5561R → T in CAA70111 (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17053 mRNA. Translation: CAA76606.1.
AC011436 Genomic DNA. Translation: AAF14038.1.
AC016661 Genomic DNA. Translation: AAF23276.1.
CP002686 Genomic DNA. Translation: AEE74767.1.
CP002686 Genomic DNA. Translation: AEE74768.1.
AY050896 mRNA. Translation: AAK92833.1.
AY096676 mRNA. Translation: AAM20310.1.
AY102116 mRNA. Translation: AAM26685.1.
BT001066 mRNA. Translation: AAN46823.1.
F20026 mRNA. Translation: CAA23383.1.
AK222065 mRNA. Translation: BAD94875.1.
Y08903 mRNA. Translation: CAA70111.1.
RefSeqiNP_001189847.1. NM_001202918.1.
NP_187555.1. NM_111778.3.
UniGeneiAt.22293.

Genome annotation databases

EnsemblPlantsiAT3G09440.1; AT3G09440.1; AT3G09440.
AT3G09440.2; AT3G09440.2; AT3G09440.
GeneIDi820102.
GrameneiAT3G09440.1; AT3G09440.1; AT3G09440.
AT3G09440.2; AT3G09440.2; AT3G09440.
KEGGiath:AT3G09440.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17053 mRNA. Translation: CAA76606.1.
AC011436 Genomic DNA. Translation: AAF14038.1.
AC016661 Genomic DNA. Translation: AAF23276.1.
CP002686 Genomic DNA. Translation: AEE74767.1.
CP002686 Genomic DNA. Translation: AEE74768.1.
AY050896 mRNA. Translation: AAK92833.1.
AY096676 mRNA. Translation: AAM20310.1.
AY102116 mRNA. Translation: AAM26685.1.
BT001066 mRNA. Translation: AAN46823.1.
F20026 mRNA. Translation: CAA23383.1.
AK222065 mRNA. Translation: BAD94875.1.
Y08903 mRNA. Translation: CAA70111.1.
RefSeqiNP_001189847.1. NM_001202918.1.
NP_187555.1. NM_111778.3.
UniGeneiAt.22293.

3D structure databases

ProteinModelPortaliO65719.
SMRiO65719. Positions 6-619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi5436. 15 interactions.
IntActiO65719. 3 interactions.
STRINGi3702.AT3G09440.1.

PTM databases

iPTMnetiO65719.
SwissPalmiO65719.

2D gel databases

SWISS-2DPAGEO65719.
World-2DPAGE0003:O65719.

Proteomic databases

PaxDbiO65719.
PRIDEiO65719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G09440.1; AT3G09440.1; AT3G09440.
AT3G09440.2; AT3G09440.2; AT3G09440.
GeneIDi820102.
GrameneiAT3G09440.1; AT3G09440.1; AT3G09440.
AT3G09440.2; AT3G09440.2; AT3G09440.
KEGGiath:AT3G09440.

Organism-specific databases

TAIRiAT3G09440.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiO65719.
KOiK03283.
OMAiDFYAPIT.
PhylomeDBiO65719.

Enzyme and pathway databases

BioCyciARA:GQT-199-MONOMER.
ARA:GQT-37-MONOMER.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.
R-ATH-3371568. Attenuation phase.
R-ATH-3371571. HSF1-dependent transactivation.
R-ATH-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

PROiO65719.

Gene expression databases

GenevisibleiO65719. AT.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "At-hsc70-3 encodes a cytosolic Hsp70 in Arabidopsis thaliana."
    Hsieh K., Wang Y.-C., Lin B.-L.
    Plant Gene Register PGR98-139
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    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.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-117.
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-649.
    Strain: cv. Columbia.
  7. "Specific Hsp70s are expressed and accumulated during silique development in Arabidopsis."
    Wang Y.C., Lee S.P., Shieh K., Hu S.M., Wang C., Lin B.L.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-649.
    Strain: cv. Columbia.
  8. "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
    Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
    Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family."
    Sung D.Y., Vierling E., Guy C.L.
    Plant Physiol. 126:789-800(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNAK GENE SUBFAMILY, INDUCTION, DEVELOPMENTAL STAGE.
  10. "Partial purification and identification of GDP-mannose 3',5'-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway."
    Wolucka B.A., Persiau G., Van Doorsselaere J., Davey M.W., Demol H., Vandekerckhove J., Van Montagu M., Zabeau M., Boerjan W.
    Proc. Natl. Acad. Sci. U.S.A. 98:14843-14848(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "GDP-mannose 3',5'-epimerase forms GDP-L-gulose, a putative intermediate for the de novo biosynthesis of vitamin C in plants."
    Wolucka B.A., Van Montagu M.
    J. Biol. Chem. 278:47483-47490(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  12. "A proteomic study of the Arabidopsis nuclear matrix."
    Calikowski T.T., Meulia T., Meier I.
    J. Cell. Biochem. 90:361-378(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Virus induction of heat shock protein 70 reflects a general response to protein accumulation in the plant cytosol."
    Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.
    Plant Physiol. 138:529-536(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses."
    Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S., Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.
    Plant Cell 19:4061-4076(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGT1B.
  15. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  16. "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
    Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
    Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-457.
  17. "WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1."
    Brkljacic J., Zhao Q., Meier I.
    Plant Physiol. 151:142-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WPP1.
  18. "The deubiquitinating enzyme AMSH3 is required for intracellular trafficking and vacuole biogenesis in Arabidopsis thaliana."
    Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D., Geldner N., Chory J., Schwechheimer C.
    Plant Cell 22:1826-1837(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMSH3.

Entry informationi

Entry nameiHSP7C_ARATH
AccessioniPrimary (citable) accession number: O65719
Secondary accession number(s): Q42345, Q56WH5, Q96267
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: April 13, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.