HSP7G_ARATH
ID HSP7G_ARATH Reviewed; 718 AA.
AC Q9LTX9; Q8RXD1; Q9M637;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Heat shock 70 kDa protein 7, chloroplastic;
DE AltName: Full=Chloroplast heat shock protein 70-2;
DE Short=cpHsc70-2;
DE AltName: Full=Heat shock protein 70-7;
DE Short=AtHsp70-7;
DE Flags: Precursor;
GN Name=HSP70-7; Synonyms=CPHSC70-2, HSC70-7; OrderedLocusNames=At5g49910;
GN ORFNames=K9P8.5;
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] (ISOFORM 1), DNAK GENE SUBFAMILY, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORMS 1 AND 2).
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 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 [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.
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, 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).
CC -!- FUNCTION: Acts redundantly with HSP70-6 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LTX9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LTX9-2; Sequence=VSP_042242, VSP_042243;
CC -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC regulated during germination. {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11402207}.
CC -!- DISRUPTION PHENOTYPE: Defective in protein import into chloroplasts
CC during early developmental stages. {ECO:0000269|PubMed:20484004}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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; AF217459; AAF27639.1; -; mRNA.
DR EMBL; AB024032; BAA97012.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95870.1; -; Genomic_DNA.
DR EMBL; BT000919; AAN41319.1; -; mRNA.
DR EMBL; AY081331; AAL91220.1; -; mRNA.
DR EMBL; BT008452; AAP37811.1; -; mRNA.
DR RefSeq; NP_199802.1; NM_124369.4. [Q9LTX9-1]
DR AlphaFoldDB; Q9LTX9; -.
DR SMR; Q9LTX9; -.
DR BioGRID; 20300; 35.
DR IntAct; Q9LTX9; 1.
DR MINT; Q9LTX9; -.
DR STRING; 3702.AT5G49910.1; -.
DR iPTMnet; Q9LTX9; -.
DR World-2DPAGE; 0003:Q9LTX9; -.
DR PaxDb; Q9LTX9; -.
DR PRIDE; Q9LTX9; -.
DR ProteomicsDB; 230253; -. [Q9LTX9-1]
DR EnsemblPlants; AT5G49910.1; AT5G49910.1; AT5G49910. [Q9LTX9-1]
DR GeneID; 835054; -.
DR Gramene; AT5G49910.1; AT5G49910.1; AT5G49910. [Q9LTX9-1]
DR KEGG; ath:AT5G49910; -.
DR Araport; AT5G49910; -.
DR TAIR; locus:2158834; AT5G49910.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_4_1; -.
DR InParanoid; Q9LTX9; -.
DR OMA; QIHILGG; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9LTX9; -.
DR PRO; PR:Q9LTX9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTX9; baseline and differential.
DR Genevisible; Q9LTX9; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chaperone; Chloroplast;
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 7, chloroplastic"
FT /id="PRO_0000415426"
FT REGION 668..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 353..371
FT /note="SLPFITATADGPKHIETTL -> RFTFPSQIYLPRSHWYVGY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042242"
FT VAR_SEQ 372..718
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_042243"
FT CONFLICT 18..21
FT /note="TSSS -> NSFC (in Ref. 1; AAF27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="T -> S (in Ref. 1; AAF27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="L -> F (in Ref. 1; AAF27639)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> Q (in Ref. 1; AAF27639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 76997 MW; FFD96CC29E3A463B CRC64;
MASSAAQIHI LGGIGFPTSS SSSSTKNLDN KTNSIPRSVF FGNRTSPFTT PTSAFLRMGR
RNNNASRYTV GPVRVVNEKV VGIDLGTTNS AVAAMEGGKP TIVTNAEGQR TTPSVVAYTK
SKDRLVGQIA KRQAVVNPEN TFFSVKRFIG RRMNEVAEES KQVSYRVIKD ENGNVKLDCP
AIGKQFAAEE ISAQVLRKLV DDASRFLNDK VTKAVITVPA YFNDSQRTAT KDAGRIAGLE
VLRIINEPTA ASLAYGFERK SNETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG
DDFDKRVVDW LASTFKKDEG IDLLKDKQAL QRLTEAAEKA KIELSSLTQT NMSLPFITAT
ADGPKHIETT LTRGKFEELC SDLLDRVRTP VENSLRDAKL SFKDIDEVIL VGGSTRIPAV
QDLVRKLTGK EPNVSVNPDE VVALGAAVQA GVLSGDVSDI VLLDVTPLSL GLETLGGVMT
KIIPRNTTLP TSKSEVFSTA ADGQTSVEIN VLQGEREFVR DNKSIGSFRL DGIPPAPRGV
PQIEVKFDID ANGILSVSAS DKGTGKKQDI TITGASTLPK DEVDTMVQEA ERFAKEDKEK
RDAIDTKNQA DSVVYQTEKQ LKELGEKIPG PVKEKVEAKL QELKEKIASG STQEIKDTMA
ALNQEVMQIG QSLYNQPQPG GADSPPGGEA SSSSDTSSSA KGGDNGGDVI DADFTDSN