HSP7J_ARATH
ID HSP7J_ARATH Reviewed; 682 AA.
AC Q9LDZ0;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Heat shock 70 kDa protein 10, mitochondrial {ECO:0000305};
DE AltName: Full=Chaperone protein HscA homolog 2 {ECO:0000303|PubMed:19865480};
DE Short=AtHscA2 {ECO:0000303|PubMed:19865480};
DE AltName: Full=Heat shock protein 70-10 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-10 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Mitochondrial heat shock protein 70-2 {ECO:0000303|PubMed:11402207};
DE Short=mtHsc70-2 {ECO:0000303|PubMed:11402207};
DE Flags: Precursor;
GN Name=HSP70-10 {ECO:0000303|PubMed:11599561};
GN Synonyms=HSC70-5 {ECO:0000312|EMBL:AAF27638.1},
GN HSCA2 {ECO:0000303|PubMed:19865480},
GN MTHSC70-2 {ECO:0000303|PubMed:11402207};
GN OrderedLocusNames=At5g09590 {ECO:0000312|Araport:AT5G09590};
GN ORFNames=F17I14_220 {ECO:0000312|EMBL:CAB89371.1};
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], 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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19865480; DOI=10.1371/journal.pone.0007662;
RA Xu X.M., Lin H., Latijnhouwers M., Moeller S.G.;
RT "Dual localized AtHscB involved in iron sulfur protein biogenesis in
RT Arabidopsis.";
RL PLoS ONE 4:E7662-E7662(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-50.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur [Fe-S]
CC cluster-containing proteins. Has a low intrinsic ATPase activity which
CC is markedly stimulated by HSCB and ISU1 (By similarity). In cooperation
CC with other chaperones, Hsp70s are key components that facilitate
CC folding of de novo synthesized proteins, assist translocation of
CC precursor proteins into organelles, and are responsible for degradation
CC of damaged protein under stress conditions (Probable).
CC {ECO:0000250|UniProtKB:Q8GUM2, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:19865480,
CC ECO:0000305|PubMed:25732537}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during seed maturation.
CC {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11402207}.
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; AF217458; AAF27638.1; -; mRNA.
DR EMBL; AL353994; CAB89371.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91413.1; -; Genomic_DNA.
DR EMBL; BT046197; ACI49796.1; -; mRNA.
DR PIR; T49939; T49939.
DR RefSeq; NP_196521.1; NM_120996.4.
DR AlphaFoldDB; Q9LDZ0; -.
DR SMR; Q9LDZ0; -.
DR BioGRID; 16096; 12.
DR IntAct; Q9LDZ0; 1.
DR MINT; Q9LDZ0; -.
DR STRING; 3702.AT5G09590.1; -.
DR iPTMnet; Q9LDZ0; -.
DR MetOSite; Q9LDZ0; -.
DR SwissPalm; Q9LDZ0; -.
DR PaxDb; Q9LDZ0; -.
DR PRIDE; Q9LDZ0; -.
DR ProteomicsDB; 232136; -.
DR EnsemblPlants; AT5G09590.1; AT5G09590.1; AT5G09590.
DR GeneID; 830818; -.
DR Gramene; AT5G09590.1; AT5G09590.1; AT5G09590.
DR KEGG; ath:AT5G09590; -.
DR Araport; AT5G09590; -.
DR TAIR; locus:2144801; AT5G09590.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q9LDZ0; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9LDZ0; -.
DR PRO; PR:Q9LDZ0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LDZ0; baseline and differential.
DR Genevisible; Q9LDZ0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009615; P:response to virus; 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; 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; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 51..682
FT /note="Heat shock 70 kDa protein 10, mitochondrial"
FT /id="PRO_0000415429"
FT REGION 646..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 72991 MW; 3BB193B42A4A3C89 CRC64;
MATAALLRSI RRREVVSSPF SAYRCLSSSG KASLNSSYLG QNFRSFSRAF SSKPAGNDVI
GIDLGTTNSC VAVMEGKNPK VIENAEGART TPSVVAFNTK GELLVGTPAK RQAVTNPTNT
VSGTKRLIGR KFDDPQTQKE MKMVPYKIVR APNGDAWVEA NGQQYSPSQI GAFILTKMKE
TAEAYLGKSV TKAVVTVPAY FNDAQRQATK DAGRIAGLDV ERIINEPTAA ALSYGMTNKE
GLIAVFDLGG GTFDVSVLEI SNGVFEVKAT NGDTFLGGED FDNALLDFLV NEFKTTEGID
LAKDRLALQR LREAAEKAKI ELSSTSQTEI NLPFITADAS GAKHFNITLT RSRFETLVNH
LIERTRDPCK NCLKDAGISA KEVDEVLLVG GMTRVPKVQS IVAEIFGKSP SKGVNPDEAV
AMGAALQGGI LRGDVKELLL LDVTPLSLGI ETLGGVFTRL ITRNTTIPTK KSQVFSTAAD
NQTQVGIRVL QGEREMATDN KLLGEFDLVG IPPSPRGVPQ IEVTFDIDAN GIVTVSAKDK
TTGKVQQITI RSSGGLSEDD IQKMVREAEL HAQKDKERKE LIDTKNTADT TIYSIEKSLG
EYREKIPSEI AKEIEDAVAD LRSASSGDDL NEIKAKIEAA NKAVSKIGEH MSGGSGGGSA
PGGGSEGGSD QAPEAEYEEV KK
