HSP7F_ARATH
ID HSP7F_ARATH Reviewed; 718 AA.
AC Q9STW6;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Heat shock 70 kDa protein 6, chloroplastic;
DE AltName: Full=Chloroplast heat shock protein 70-1;
DE Short=cpHsc70-1;
DE AltName: Full=Heat shock protein 70-6;
DE Short=AtHsp70-6;
DE Flags: Precursor;
GN Name=HSP70-6; Synonyms=CPHSC70-1; OrderedLocusNames=At4g24280;
GN ORFNames=T22A6.110;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [5]
RP DNAK GENE SUBFAMILY.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18997426; DOI=10.1271/bbb.80408;
RA Ratnayake R.M., Inoue H., Nonami H., Akita M.;
RT "Alternative processing of Arabidopsis Hsp70 precursors during protein
RT import into chloroplasts.";
RL Biosci. Biotechnol. Biochem. 72:2926-2935(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18192441; DOI=10.1104/pp.107.114496;
RA Su P.H., Li H.M.;
RT "Arabidopsis stromal 70-kD heat shock proteins are essential for plant
RT development and important for thermotolerance of germinating seeds.";
RL Plant Physiol. 146:1231-1241(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=20506024; DOI=10.1007/s00425-010-1192-z;
RA Latijnhouwers M., Xu X.M., Moeller S.G.;
RT "Arabidopsis stromal 70-kDa heat shock proteins are essential for
RT chloroplast development.";
RL Planta 232:567-578(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20484004; DOI=10.1105/tpc.109.071415;
RA Su P.H., Li H.M.;
RT "Stromal Hsp70 is important for protein translocation into pea and
RT Arabidopsis chloroplasts.";
RL Plant Cell 22:1516-1531(2010).
RN [10]
RP INTERACTION WITH GEMINIVIRUS MP.
RX PubMed=20193958; DOI=10.1016/j.virol.2010.02.011;
RA Krenz B., Windeisen V., Wege C., Jeske H., Kleinow T.;
RT "A plastid-targeted heat shock cognate 70kDa protein interacts with the
RT Abutilon mosaic virus movement protein.";
RL Virology 401:6-17(2010).
CC -!- FUNCTION: Acts redundantly with HSP70-7 in the thermotolerance of
CC germinating seeds. Plays an important role in the protein precursor
CC import into chloroplasts. {ECO:0000269|PubMed:18192441,
CC ECO:0000269|PubMed:20484004, ECO:0000269|PubMed:20506024}.
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 geminivirus movement protein (MP).
CC {ECO:0000269|PubMed:20193958}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
CC -!- DISRUPTION PHENOTYPE: Variegated cotyledons, malformed leaves, growth
CC retardation and impaired root growth. Defective in protein import into
CC chloroplasts during early developmental stages.
CC {ECO:0000269|PubMed:18192441, ECO:0000269|PubMed:20484004,
CC ECO:0000269|PubMed:20506024}.
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; AL078637; CAB45063.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79338.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84884.1; -; Genomic_DNA.
DR EMBL; AY072138; AAL59960.1; -; mRNA.
DR EMBL; BT001950; AAN71949.1; -; mRNA.
DR PIR; T09891; T09891.
DR RefSeq; NP_194159.1; NM_118561.3.
DR AlphaFoldDB; Q9STW6; -.
DR SMR; Q9STW6; -.
DR BioGRID; 13820; 25.
DR IntAct; Q9STW6; 1.
DR STRING; 3702.AT4G24280.1; -.
DR iPTMnet; Q9STW6; -.
DR MetOSite; Q9STW6; -.
DR PaxDb; Q9STW6; -.
DR PRIDE; Q9STW6; -.
DR ProteomicsDB; 230156; -.
DR EnsemblPlants; AT4G24280.1; AT4G24280.1; AT4G24280.
DR GeneID; 828531; -.
DR Gramene; AT4G24280.1; AT4G24280.1; AT4G24280.
DR KEGG; ath:AT4G24280; -.
DR Araport; AT4G24280; -.
DR TAIR; locus:2135897; AT4G24280.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q9STW6; -.
DR OMA; SAAQINC; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9STW6; -.
DR PRO; PR:Q9STW6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STW6; baseline and differential.
DR Genevisible; Q9STW6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 TIGRFAMs; TIGR02350; prok_dnaK; 1.
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; Chloroplast; Host-virus interaction;
KW Nucleotide-binding; Plastid; Protein transport; Reference proteome;
KW Stress response; Transit peptide; Transport.
FT TRANSIT 1..92
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 93..718
FT /note="Heat shock 70 kDa protein 6, chloroplastic"
FT /id="PRO_0000415425"
FT REGION 671..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 76508 MW; 8723B345C601B8A1 CRC64;
MASSAAQIHV LGGIGFASSS SSKRNLNGKG GTFMPRSAFF GTRTGPFSTP TSAFLRMGTR
NGGGASRYAV GPVRVVNEKV VGIDLGTTNS AVAAMEGGKP TIVTNAEGQR TTPSVVAYTK
SGDRLVGQIA KRQAVVNPEN TFFSVKRFIG RKMNEVDEES KQVSYRVVRD ENNNVKLECP
AINKQFAAEE ISAQVLRKLV DDASRFLNDK VTKAVITVPA YFNDSQRTAT KDAGRIAGLE
VLRIINEPTA ASLAYGFDRK ANETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG
DDFDKRVVDW LAAEFKKDEG IDLLKDKQAL QRLTEAAEKA KIELSSLTQT NMSLPFITAT
ADGPKHIETT LTRAKFEELC SDLLDRVRTP VENSLRDAKL SFKDIDEVIL VGGSTRIPAV
QELVRKVTGK EPNVTVNPDE VVALGAAVQA GVLAGDVSDI VLLDVTPLSI GLETLGGVMT
KIIPRNTTLP TSKSEVFSTA ADGQTSVEIN VLQGEREFVR DNKSLGSFRL DGIPPAPRGV
PQIEVKFDID ANGILSVSAV DKGTGKKQDI TITGASTLPK DEVDQMVQEA ERFAKDDKEK
RDAIDTKNQA DSVVYQTEKQ LKELGEKIPG EVKEKVEAKL QELKDKIGSG STQEIKDAMA
ALNQEVMQIG QSLYNQPGAG GPGAGPSPGG EGASSGDSSS SKGGDGDDVI DADFTDSQ
