HS704_ARATH
ID HS704_ARATH Reviewed; 650 AA.
AC Q9LHA8; Q9ZS55;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Heat shock 70 kDa protein 4 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Heat shock cognate 70 kDa protein 4 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock cognate protein 70-4 {ECO:0000303|PubMed:11402207};
DE Short=AtHsc70-4 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock protein 70-4 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-4 {ECO:0000303|PubMed:11599561};
GN Name=HSP70-4 {ECO:0000303|PubMed:11599561};
GN Synonyms=HSC70-4 {ECO:0000303|PubMed:11402207}, HSP70,
GN MED37_2 {ECO:0000303|PubMed:22021418}, MED37C;
GN OrderedLocusNames=At3g12580 {ECO:0000312|Araport:AT3G12580};
GN ORFNames=T16H11.7 {ECO:0000312|EMBL:BAB02269.1},
GN T2E22.11 {ECO:0000312|EMBL:AAG51030.1};
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].
RC STRAIN=cv. Columbia; TISSUE=Silique;
RA Hinderhofer K., Praendl R., Schoeffl F.;
RT "Seed-maturation-induced subset of heat shock protein mRNAs and heat-shock-
RT element-binding protein complexes are dependent on ABI3 in Arabidopsis
RT thaliana.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
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 [8]
RP INTERACTION WITH HSFA1A/HSF1.
RX PubMed=11807141; DOI=10.1093/jexbot/53.367.371;
RA Kim B.H., Schoeffl F.;
RT "Interaction between Arabidopsis heat shock transcription factor 1 and 70
RT kDa heat shock proteins.";
RL J. Exp. Bot. 53:371-375(2002).
RN [9]
RP INDUCTION.
RX PubMed=15805473; DOI=10.1104/pp.104.058958;
RA Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
RT "Virus induction of heat shock protein 70 reflects a general response to
RT protein accumulation in the plant cytosol.";
RL Plant Physiol. 138:529-536(2005).
RN [10]
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 [11]
RP INDUCTION BY PATHOGEN.
RX PubMed=18065690; DOI=10.1105/tpc.107.051896;
RA Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
RA Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
RT "Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates
RT Arabidopsis immune responses.";
RL Plant Cell 19:4061-4076(2007).
RN [12]
RP INDUCTION.
RX PubMed=19704521; DOI=10.4161/psb.3.10.6021;
RA Scarpeci T.E., Zanor M.I., Valle E.M.;
RT "Investigating the role of plant heat shock proteins during oxidative
RT stress.";
RL Plant Signal. Behav. 3:856-857(2008).
RN [13]
RP FUNCTION, INTERACTION WITH CHIP, AND DISRUPTION PHENOTYPE.
RX PubMed=20028838; DOI=10.1105/tpc.109.071548;
RA Lee S., Lee D.W., Lee Y., Mayer U., Stierhof Y.D., Lee S., Jurgens G.,
RA Hwang I.;
RT "Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate
RT plastid-destined precursor degradation through the ubiquitin-26S proteasome
RT system in Arabidopsis.";
RL Plant Cell 21:3984-4001(2009).
RN [14]
RP NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [15]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28004282; DOI=10.1007/s10265-016-0900-6;
RA Leng L., Liang Q., Jiang J., Zhang C., Hao Y., Wang X., Su W.;
RT "A subclass of HSP70s regulate development and abiotic stress responses in
RT Arabidopsis thaliana.";
RL J. Plant Res. 130:349-363(2017).
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 (Probable). ATP-dependent molecular chaperone that assists folding of
CC unfolded or misfolded proteins under stress conditions. Mediates
CC plastid precursor degradation to prevent cytosolic precursor
CC accumulation, together with the E3 ubiquitin-protein ligase CHIP.
CC Recognizes specific sequence motifs in transit peptides and thereby led
CC to precursor degradation through the ubiquitin-proteasome system. Plays
CC a critical role in embryogenesis. {ECO:0000269|PubMed:20028838,
CC ECO:0000305|PubMed:11402207}.
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 CHIP (PubMed:20028838). Interacts with
CC HSFA1A/HSF1 (PubMed:11807141). {ECO:0000269|PubMed:11807141,
CC ECO:0000269|PubMed:20028838}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28004282}.
CC Nucleus {ECO:0000269|PubMed:28004282}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves, stems, vascular
CC bundles, roots, stigmas and anthers. {ECO:0000269|PubMed:28004282}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during seed maturation.
CC {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: Induced by heat shock and cold (PubMed:11402207). Induced by
CC high light treatment and oxidative stress (PubMed:19704521). Up-
CC regulated by viral infection (PubMed:15805473). Induced by infection
CC with the bacterial pathogen Pseudomonas syringae (PubMed:18065690).
CC Induced by abscisic acid (ABA), salt stress, osmotic shock,
CC brassinosteroid, cytokinin and auxin (PubMed:28004282).
CC {ECO:0000269|PubMed:11402207, ECO:0000269|PubMed:15805473,
CC ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19704521,
CC ECO:0000269|PubMed:28004282}.
CC -!- DISRUPTION PHENOTYPE: Abnormal embryogenesis. Defective seedlings with
CC high levels of reactive oxygen species and monoubiquitinated LHCB4
CC precursors (PubMed:20028838). No visible phenotype under normal growth
CC conditions (PubMed:28004282). {ECO:0000269|PubMed:20028838,
CC ECO:0000269|PubMed:28004282}.
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; AJ002551; CAA05547.1; -; mRNA.
DR EMBL; AP002055; BAB02269.1; -; Genomic_DNA.
DR EMBL; AC069474; AAG51030.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75218.1; -; Genomic_DNA.
DR EMBL; AY054183; AAL06844.1; -; mRNA.
DR EMBL; AY054190; AAL06851.1; -; mRNA.
DR EMBL; AY059885; AAL24367.1; -; mRNA.
DR PIR; JA0171; JA0171.
DR RefSeq; NP_187864.1; NM_112093.3.
DR AlphaFoldDB; Q9LHA8; -.
DR SMR; Q9LHA8; -.
DR BioGRID; 5772; 29.
DR IntAct; Q9LHA8; 9.
DR MINT; Q9LHA8; -.
DR STRING; 3702.AT3G12580.1; -.
DR iPTMnet; Q9LHA8; -.
DR MetOSite; Q9LHA8; -.
DR PaxDb; Q9LHA8; -.
DR PRIDE; Q9LHA8; -.
DR ProteomicsDB; 238330; -.
DR EnsemblPlants; AT3G12580.1; AT3G12580.1; AT3G12580.
DR GeneID; 820438; -.
DR Gramene; AT3G12580.1; AT3G12580.1; AT3G12580.
DR KEGG; ath:AT3G12580; -.
DR Araport; AT3G12580; -.
DR TAIR; locus:2101222; AT3G12580.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; Q9LHA8; -.
DR OMA; GCKVQNA; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q9LHA8; -.
DR PRO; PR:Q9LHA8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHA8; baseline and differential.
DR Genevisible; Q9LHA8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
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:0016567; P:protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; 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 InterPro; IPR043129; ATPase_NBD.
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 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; Nucleotide-binding; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation pathway.
FT CHAIN 1..650
FT /note="Heat shock 70 kDa protein 4"
FT /id="PRO_0000397045"
FT REGION 620..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 126
FT /note="M -> I (in Ref. 1; CAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="T -> I (in Ref. 1; CAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> G (in Ref. 1; CAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> V (in Ref. 1; CAA05547)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="L -> V (in Ref. 1; CAA05547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 71101 MW; 33381E896461C5B9 CRC64;
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPTNTV FDAKRLIGRR YSDPSVQADK SHWPFKVVSG PGEKPMIVVN HKGEEKQFSA
EEISSMVLIK MREIAEAFLG SPVKNAVVTV PAYFNDSQRQ ATKDAGVISG LNVMRIINEP
TAAAIAYGLD KKASSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKNKKDIT GNPRALRRLR TACERAKRTL SSTAQTTIEI DSLFEGIDFY
TTITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSSVHDV VLVGGSTRIP KVQQLLQDFF
NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTVLI
PRNTTIPTKK EQIFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKEE IEKMVQEAEK YKAEDEEHKK
KVDAKNALEN YAYNMRNTIK DEKIASKLDA ADKKKIEDAI DQAIEWLDGN QLAEADEFED
KMKELESLCN PIIARMYQGA GPDMGGAGGM DDDTPAGGSG GAGPKIEEVD
