HSP7I_ARATH
ID HSP7I_ARATH Reviewed; 682 AA.
AC Q8GUM2; Q56WU4; Q9SZJ3;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Heat shock 70 kDa protein 9, mitochondrial {ECO:0000305};
DE AltName: Full=Chaperone protein HscA homolog 1 {ECO:0000303|PubMed:19865480};
DE Short=AtHscA1 {ECO:0000303|PubMed:19865480};
DE AltName: Full=Heat shock protein 70-9 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-9 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Mitochondrial heat shock protein 70-1 {ECO:0000303|PubMed:11402207};
DE Short=mtHsc70-1 {ECO:0000303|PubMed:11402207};
DE Flags: Precursor;
GN Name=HSP70-9 {ECO:0000303|PubMed:11599561};
GN Synonyms=HSCA1 {ECO:0000303|PubMed:19865480},
GN MTHSC70-1 {ECO:0000303|PubMed:11402207};
GN OrderedLocusNames=At4g37910 {ECO:0000312|Araport:AT4G37910};
GN ORFNames=F20D10.30 {ECO:0000312|EMBL:CAB37531.1};
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-682.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) 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 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 [7]
RP FUNCTION, INTERACTION WITH HSCB, AND 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 CYS-46.
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 (PubMed:19865480). In
CC cooperation with other chaperones, Hsp70s are key components that
CC facilitate folding of de novo synthesized proteins, assist
CC translocation of precursor proteins into organelles, and are
CC responsible for degradation of damaged protein under stress conditions
CC (Probable). {ECO:0000269|PubMed:19865480, ECO:0000305}.
CC -!- SUBUNIT: Interacts with HSCB. {ECO:0000269|PubMed:19865480}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19865480,
CC ECO:0000305|PubMed:25732537}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19865480}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL035538; CAB37531.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161592; CAB80456.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86852.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66081.1; -; Genomic_DNA.
DR EMBL; BT002390; AAO00750.1; -; mRNA.
DR EMBL; BT008430; AAP37789.1; -; mRNA.
DR EMBL; AK221937; BAD94381.1; -; mRNA.
DR PIR; T05618; T05618.
DR RefSeq; NP_001328002.1; NM_001342461.1.
DR RefSeq; NP_195504.2; NM_119952.4.
DR AlphaFoldDB; Q8GUM2; -.
DR SMR; Q8GUM2; -.
DR BioGRID; 15228; 2.
DR IntAct; Q8GUM2; 1.
DR MINT; Q8GUM2; -.
DR STRING; 3702.AT4G37910.1; -.
DR iPTMnet; Q8GUM2; -.
DR MetOSite; Q8GUM2; -.
DR SwissPalm; Q8GUM2; -.
DR PaxDb; Q8GUM2; -.
DR PRIDE; Q8GUM2; -.
DR ProteomicsDB; 232119; -.
DR EnsemblPlants; AT4G37910.1; AT4G37910.1; AT4G37910.
DR EnsemblPlants; AT4G37910.2; AT4G37910.2; AT4G37910.
DR GeneID; 829947; -.
DR Gramene; AT4G37910.1; AT4G37910.1; AT4G37910.
DR Gramene; AT4G37910.2; AT4G37910.2; AT4G37910.
DR KEGG; ath:AT4G37910; -.
DR Araport; AT4G37910; -.
DR TAIR; locus:2121022; AT4G37910.
DR eggNOG; KOG0102; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; Q8GUM2; -.
DR OMA; YLARPFC; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q8GUM2; -.
DR PRO; PR:Q8GUM2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUM2; baseline and differential.
DR Genevisible; Q8GUM2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0008270; F:zinc ion binding; HDA:TAIR.
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 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; Cytoplasm; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 47..682
FT /note="Heat shock 70 kDa protein 9, mitochondrial"
FT /id="PRO_0000415428"
FT REGION 640..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 414
FT /note="A -> V (in Ref. 4; BAD94381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 73075 MW; BE8EC435202E7234 CRC64;
MASVALLRSF RRREVQMASV SAFKSVSANG KNSMFGKLGY LARPFCSRPV GNDVIGIDLG
TTNSCVSVME GKTARVIENA EGSRTTPSVV AMNQKGELLV GTPAKRQAVT NPTNTIFGSK
RLIGRRFDDP QTQKEMKMVP YKIVKAPNGD AWVEANGQKF SPSQIGANVL TKMKETAEAY
LGKSINKAVV TVPAYFNDAQ RQATKDAGKI AGLDVQRIIN EPTAAALSYG MNNKEGVIAV
FDLGGGTFDV SILEISSGVF EVKATNGDTF LGGEDFDNTL LEYLVNEFKR SDNIDLTKDN
LALQRLREAA EKAKIELSST TQTEINLPFI TADASGAKHL NITLTRSKFE GLVGKLIERT
RSPCQNCLKD AGVTIKEVDE VLLVGGMTRV PKVQEIVSEI FGKSPCKGVN PDEAVAMGAA
IQGGILRGDV KDLLLLDVVP LSLGIETLGA VFTKLIPRNT TIPTKKSQVF STAADNQMQV
GIKVLQGERE MAADNKVLGE FDLVGIPPAP RGMPQIEVTF DIDANGITTV SAKDKATGKE
QNITIRSSGG LSDDEINRMV KEAELNAQKD QEKKQLIDLR NSADTTIYSV EKSLSEYREK
IPAEIASEIE TAVSDLRTAM AGEDVEDIKA KVEAANKAVS KIGEHMSKGS GSSGSDGSSG
EGTSGTEQTP EAEFEEASGS RK
