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Protein

Heat shock 70 kDa protein 6, chloroplastic

Gene

HSP70-6

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

Functioni

Acts redundantly with HSP70-7 in the thermotolerance of germinating seeds. Plays an important role in the protein precursor import into chloroplasts.3 Publications
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: TAIR

GO - Biological processi

  • protein folding Source: InterPro
  • protein targeting to chloroplast Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to cold Source: TAIR
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction, Protein transport, Stress response, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 6, chloroplastic
Alternative name(s):
Chloroplast heat shock protein 70-1
Short name:
cpHsc70-1
Heat shock protein 70-6
Short name:
AtHsp70-6
Gene namesi
Name:HSP70-6
Synonyms:CPHSC70-1
Ordered Locus Names:At4g24280
ORF Names:T22A6.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G24280.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • mitochondrion Source: TAIR
  • nucleus Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Variegated cotyledons, malformed leaves, growth retardation and impaired root growth. Defective in protein import into chloroplasts during early developmental stages.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 9292ChloroplastSequence analysisAdd
BLAST
Chaini93 – 718626Heat shock 70 kDa protein 6, chloroplasticPRO_0000415425Add
BLAST

Proteomic databases

PaxDbiQ9STW6.
PRIDEiQ9STW6.

PTM databases

iPTMnetiQ9STW6.

Expressioni

Gene expression databases

GenevisibleiQ9STW6. AT.

Interactioni

Subunit structurei

Interacts with geminivirus movement protein (MP).1 Publication

Protein-protein interaction databases

BioGridi13820. 8 interactions.
STRINGi3702.AT4G24280.1.

Structurei

3D structure databases

ProteinModelPortaliQ9STW6.
SMRiQ9STW6. Positions 79-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiQ9STW6.
KOiK03283.
OMAiYSRSRRW.
PhylomeDBiQ9STW6.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. 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.
TIGRFAMsiTIGR02350. prok_dnaK. 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.

Q9STW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSAAQIHV LGGIGFASSS SSKRNLNGKG GTFMPRSAFF GTRTGPFSTP
60 70 80 90 100
TSAFLRMGTR NGGGASRYAV GPVRVVNEKV VGIDLGTTNS AVAAMEGGKP
110 120 130 140 150
TIVTNAEGQR TTPSVVAYTK SGDRLVGQIA KRQAVVNPEN TFFSVKRFIG
160 170 180 190 200
RKMNEVDEES KQVSYRVVRD ENNNVKLECP AINKQFAAEE ISAQVLRKLV
210 220 230 240 250
DDASRFLNDK VTKAVITVPA YFNDSQRTAT KDAGRIAGLE VLRIINEPTA
260 270 280 290 300
ASLAYGFDRK ANETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG
310 320 330 340 350
DDFDKRVVDW LAAEFKKDEG IDLLKDKQAL QRLTEAAEKA KIELSSLTQT
360 370 380 390 400
NMSLPFITAT ADGPKHIETT LTRAKFEELC SDLLDRVRTP VENSLRDAKL
410 420 430 440 450
SFKDIDEVIL VGGSTRIPAV QELVRKVTGK EPNVTVNPDE VVALGAAVQA
460 470 480 490 500
GVLAGDVSDI VLLDVTPLSI GLETLGGVMT KIIPRNTTLP TSKSEVFSTA
510 520 530 540 550
ADGQTSVEIN VLQGEREFVR DNKSLGSFRL DGIPPAPRGV PQIEVKFDID
560 570 580 590 600
ANGILSVSAV DKGTGKKQDI TITGASTLPK DEVDQMVQEA ERFAKDDKEK
610 620 630 640 650
RDAIDTKNQA DSVVYQTEKQ LKELGEKIPG EVKEKVEAKL QELKDKIGSG
660 670 680 690 700
STQEIKDAMA ALNQEVMQIG QSLYNQPGAG GPGAGPSPGG EGASSGDSSS
710
SKGGDGDDVI DADFTDSQ
Length:718
Mass (Da):76,508
Last modified:May 1, 2000 - v1
Checksum:i8723B345C601B8A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078637 Genomic DNA. Translation: CAB45063.1.
AL161561 Genomic DNA. Translation: CAB79338.1.
CP002687 Genomic DNA. Translation: AEE84884.1.
AY072138 mRNA. Translation: AAL59960.1.
BT001950 mRNA. Translation: AAN71949.1.
PIRiT09891.
RefSeqiNP_194159.1. NM_118561.2.
UniGeneiAt.25311.
At.67055.

Genome annotation databases

EnsemblPlantsiAT4G24280.1; AT4G24280.1; AT4G24280.
GeneIDi828531.
GrameneiAT4G24280.1; AT4G24280.1; AT4G24280.
KEGGiath:AT4G24280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078637 Genomic DNA. Translation: CAB45063.1.
AL161561 Genomic DNA. Translation: CAB79338.1.
CP002687 Genomic DNA. Translation: AEE84884.1.
AY072138 mRNA. Translation: AAL59960.1.
BT001950 mRNA. Translation: AAN71949.1.
PIRiT09891.
RefSeqiNP_194159.1. NM_118561.2.
UniGeneiAt.25311.
At.67055.

3D structure databases

ProteinModelPortaliQ9STW6.
SMRiQ9STW6. Positions 79-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13820. 8 interactions.
STRINGi3702.AT4G24280.1.

PTM databases

iPTMnetiQ9STW6.

Proteomic databases

PaxDbiQ9STW6.
PRIDEiQ9STW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G24280.1; AT4G24280.1; AT4G24280.
GeneIDi828531.
GrameneiAT4G24280.1; AT4G24280.1; AT4G24280.
KEGGiath:AT4G24280.

Organism-specific databases

TAIRiAT4G24280.

Phylogenomic databases

eggNOGiKOG0102. Eukaryota.
COG0443. LUCA.
HOGENOMiHOG000228135.
InParanoidiQ9STW6.
KOiK03283.
OMAiYSRSRRW.
PhylomeDBiQ9STW6.

Miscellaneous databases

PROiQ9STW6.

Gene expression databases

GenevisibleiQ9STW6. AT.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
HAMAPiMF_00332. DnaK.
InterProiIPR012725. Chaperone_DnaK.
IPR018181. 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.
TIGRFAMsiTIGR02350. prok_dnaK. 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. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "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.
  4. "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.
  5. "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.
  6. "Alternative processing of Arabidopsis Hsp70 precursors during protein import into chloroplasts."
    Ratnayake R.M., Inoue H., Nonami H., Akita M.
    Biosci. Biotechnol. Biochem. 72:2926-2935(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Arabidopsis stromal 70-kD heat shock proteins are essential for plant development and important for thermotolerance of germinating seeds."
    Su P.H., Li H.M.
    Plant Physiol. 146:1231-1241(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Arabidopsis stromal 70-kDa heat shock proteins are essential for chloroplast development."
    Latijnhouwers M., Xu X.M., Moeller S.G.
    Planta 232:567-578(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  9. "Stromal Hsp70 is important for protein translocation into pea and Arabidopsis chloroplasts."
    Su P.H., Li H.M.
    Plant Cell 22:1516-1531(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "A plastid-targeted heat shock cognate 70kDa protein interacts with the Abutilon mosaic virus movement protein."
    Krenz B., Windeisen V., Wege C., Jeske H., Kleinow T.
    Virology 401:6-17(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GEMINIVIRUS MP.

Entry informationi

Entry nameiHSP7F_ARATH
AccessioniPrimary (citable) accession number: Q9STW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 120 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.