HS701_ARATH
ID HS701_ARATH Reviewed; 651 AA.
AC P22953; Q93VU6; Q9LZ52;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Heat shock 70 kDa protein 1 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Heat shock cognate 70 kDa protein 1 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock cognate protein 70-1 {ECO:0000303|PubMed:11402207};
DE Short=AtHsc70-1 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock protein 70-1 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-1 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 2 {ECO:0000303|PubMed:8075396};
GN Name=HSP70-1 {ECO:0000303|PubMed:11599561};
GN Synonyms=ERD2 {ECO:0000303|PubMed:8075396},
GN HSC70-1 {ECO:0000303|PubMed:11402207},
GN MED37_4 {ECO:0000303|PubMed:22021418}, MED37E;
GN OrderedLocusNames=At5g02500 {ECO:0000312|Araport:AT5G02500};
GN ORFNames=T22P11.90 {ECO:0000312|EMBL:CAB85987.1};
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8049382; DOI=10.1007/bf00043887;
RA Wu S.H., Wang C., Chen J., Lin B.-L.;
RT "Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed
RT in vegetative tissues of Arabidopsis thaliana.";
RL Plant Mol. Biol. 25:577-583(1994).
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;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120, AND INDUCTION.
RX PubMed=16666375; DOI=10.1104/pp.88.3.731;
RA Wu C.H., Caspar T., Browse J., Lindquist S., Somerville C.R.;
RT "Characterization of an hsp70 cognate gene family in Arabidopsis.";
RL Plant Physiol. 88:731-740(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-651.
RC STRAIN=cv. Ostwestfalen; TISSUE=Leaf;
RA King K.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION BY DEHYDRATION STRESS AND ABA.
RX PubMed=8075396; DOI=10.1007/bf00028874;
RA Kiyosue T., Yamaguchi-shinozaki K., Shinozaki K.;
RT "Cloning of cDNAs for genes that are early-responsive to dehydration stress
RT (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP
RT cognate genes.";
RL Plant Mol. Biol. 25:791-798(1994).
RN [8]
RP INTERACTION WITH TIR.
RC STRAIN=cv. Columbia;
RA Kroczynska B., Ciesielski A., Stachnik K.;
RT "The nucleotide sequence of a cDNA encoding the AtTIR, a TIR-like
RT resistance protein in Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-172(1999).
RN [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION.
RX PubMed=12805626; DOI=10.1104/pp.102.019398;
RA Sung D.Y., Guy C.L.;
RT "Physiological and molecular assessment of altered expression of Hsc70-1 in
RT Arabidopsis. Evidence for pleiotropic consequences.";
RL Plant Physiol. 132:979-987(2003).
RN [13]
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 [14]
RP INTERACTION WITH BAG3 AND BAG5.
RX PubMed=16003391; DOI=10.1038/sj.cdd.4401712;
RA Kang C.H., Jung W.Y., Kang Y.H., Kim J.Y., Kim D.G., Jeong J.C., Baek D.W.,
RA Jin J.B., Lee J.Y., Kim M.O., Chung W.S., Mengiste T., Koiwa H., Kwak S.S.,
RA Bahk J.D., Lee S.Y., Nam J.S., Yun D.J., Cho M.J.;
RT "AtBAG6, a novel calmodulin-binding protein, induces programmed cell death
RT in yeast and plants.";
RL Cell Death Differ. 13:84-95(2006).
RN [15]
RP INTERACTION WITH BAG4.
RX PubMed=16636050; DOI=10.1074/jbc.m511794200;
RA Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J.,
RA Dickman M.B.;
RT "Identification and functional characterization of the BAG protein family
RT in Arabidopsis thaliana.";
RL J. Biol. Chem. 281:18793-18801(2006).
RN [16]
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 [17]
RP FUNCTION, INTERACTION WITH SGT1B, AND SUBCELLULAR LOCATION.
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 [18]
RP INTERACTION WITH WPP1; WPP2 AND WIT1, AND FUNCTION.
RX PubMed=19617588; DOI=10.1104/pp.109.143404;
RA Brkljacic J., Zhao Q., Meier I.;
RT "WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
RT preventing mistargeting of RanGAP1-anchoring protein WIT1.";
RL Plant Physiol. 151:142-154(2009).
RN [19]
RP INTERACTION WITH AMSH3.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
RN [20]
RP INTERACTION WITH OEP61.
RX PubMed=21612577; DOI=10.1042/bj20110448;
RA von Loeffelholz O., Kriechbaumer V., Ewan R.A., Jonczyk R., Lehmann S.,
RA Young J.C., Abell B.M.;
RT "OEP61 is a chaperone receptor at the plastid outer envelope.";
RL Biochem. J. 438:143-153(2011).
RN [21]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21418353; DOI=10.1111/j.1365-313x.2011.04558.x;
RA Jungkunz I., Link K., Vogel F., Voll L.M., Sonnewald S., Sonnewald U.;
RT "AtHsp70-15-deficient Arabidopsis plants are characterized by reduced
RT growth, a constitutive cytosolic protein response and enhanced resistance
RT to TuMV.";
RL Plant J. 66:983-995(2011).
RN [22]
RP FUNCTION.
RX PubMed=21586649; DOI=10.1104/pp.111.174425;
RA Clement M., Leonhardt N., Droillard M.J., Reiter I., Montillet J.L.,
RA Genty B., Lauriere C., Nussaume L., Noel L.D.;
RT "The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important
RT for stomatal closure and modulate abscisic acid-dependent physiological
RT responses in Arabidopsis.";
RL Plant Physiol. 156:1481-1492(2011).
RN [23]
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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [26]
RP INTERACTION WITH BON1, AND DISRUPTION PHENOTYPE.
RX PubMed=26408532; DOI=10.1104/pp.15.00970;
RA Gou M., Zhang Z., Zhang N., Huang Q., Monaghan J., Yang H., Shi Z.,
RA Zipfel C., Hua J.;
RT "Opposing effects on two phases of defense responses from concerted actions
RT of HEAT SHOCK COGNATE70 and BONZAI1 in Arabidopsis.";
RL Plant Physiol. 169:2304-2323(2015).
RN [27]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION 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). Probably involved in defense response. Chaperone involved
CC in protein targeting to chloroplasts. May cooperate with SGT1 and HSP90
CC in R gene-mediated resistance towards the oomycete Hyaloperonospora
CC parasitica (downy mildew). Plays a role with WPP-domain proteins in
CC facilitating WIT1 nuclear envelope targeting (PubMed:12805626,
CC PubMed:18065690, PubMed:19617588). Modulates stomatal aperture in
CC response to various environmental conditions and physiological
CC responses to the hormone abscisic acid (ABA) (PubMed:21586649).
CC {ECO:0000269|PubMed:12805626, ECO:0000269|PubMed:18065690,
CC ECO:0000269|PubMed:19617588, ECO:0000269|PubMed:21586649,
CC ECO:0000305|PubMed:11402207}.
CC -!- SUBUNIT: Binds to the deubiquitinating enzyme AMSH3. Interacts with
CC SGT1B (via SGS domain). Interacts with OEP61. Interacts with
CC HSFA1A/HSF1. Interacts with BAG3, BAG4 and BAG5. Interacts with WPP1,
CC WPP2 and WIT1. Component of a ternary complex composed of WPP1, HSP70-1
CC and WIT1. Binds to TIR. {ECO:0000269|PubMed:11807141,
CC ECO:0000269|PubMed:16003391, ECO:0000269|PubMed:16636050,
CC ECO:0000269|PubMed:18065690, ECO:0000269|PubMed:19617588,
CC ECO:0000269|PubMed:20543027, ECO:0000269|PubMed:21612577,
CC ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC P22953; Q9SUT5: SGT1B; NbExp=3; IntAct=EBI-1238845, EBI-1581364;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28004282}.
CC Nucleus {ECO:0000269|PubMed:28004282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P22953-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at a substantial level during normal
CC growth in root, stem, leaf and flower tissues, but not in siliques
CC (PubMed:8049382). Expressed in cotyledons, leaves, stems, vascular
CC bundles, roots, stigmas and anthers (PubMed:28004282).
CC {ECO:0000269|PubMed:28004282, ECO:0000269|PubMed:8049382}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC regulated during germination. {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: Induced by heat shock and cold (PubMed:11402207). Induced by
CC dehydration stress and abscisic acid (ABA) (PubMed:8075396). Up-
CC regulated by viral infection (PubMed:15805473).
CC {ECO:0000269|PubMed:11402207, ECO:0000269|PubMed:15805473,
CC ECO:0000269|PubMed:8075396}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:21418353, PubMed:28004282, PubMed:26408532). The
CC double mutants hsp70-1 and hsp70-4 exhibit accelerated bolting,
CC flowering, and branching, small round shape and flat leaf blades, thin
CC stems and short siliques (PubMed:28004282). The double mutants hsp70-1
CC and hsp70-4 exhibit reduced tolerance to abiotic stresses, such as
CC heat, cold, salt and osmotic shock (PubMed:28004282).
CC {ECO:0000269|PubMed:21418353, ECO:0000269|PubMed:26408532,
CC ECO:0000269|PubMed:28004282}.
CC -!- MISCELLANEOUS: Plants overexpressing HSP70-1 show disabled immune
CC responses, enhanced tolerance to heat shock and altered plant growth
CC and development (PubMed:12805626). Plants overexpressing HSP70-1 are
CC hypersensitive to abscisic acid (ABA) in seed germination assays, and
CC are compromised in the dark- and ABA-induced stomatal closure
CC (PubMed:21586649). {ECO:0000269|PubMed:12805626,
CC ECO:0000269|PubMed:21586649}.
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; X74604; CAA52684.1; -; mRNA.
DR EMBL; AL162971; CAB85987.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90480.1; -; Genomic_DNA.
DR EMBL; AY035123; AAK59628.2; -; mRNA.
DR EMBL; AY057481; AAL09715.1; -; mRNA.
DR EMBL; AY120747; AAM53305.1; -; mRNA.
DR EMBL; BT002754; AAO22583.1; -; mRNA.
DR EMBL; AH001335; AAA32819.1; -; Genomic_DNA.
DR EMBL; X77199; CAA54419.1; -; Genomic_DNA.
DR PIR; S46302; S46302.
DR PIR; T48271; T48271.
DR RefSeq; NP_195870.1; NM_120328.5. [P22953-1]
DR AlphaFoldDB; P22953; -.
DR SMR; P22953; -.
DR BioGRID; 16298; 44.
DR IntAct; P22953; 10.
DR MINT; P22953; -.
DR STRING; 3702.AT5G02500.1; -.
DR TCDB; 1.A.33.1.1; the cation channel-forming heat shock protein-70 (hsp70) family.
DR iPTMnet; P22953; -.
DR MetOSite; P22953; -.
DR SWISS-2DPAGE; P22953; -.
DR World-2DPAGE; 0003:P22953; -.
DR PaxDb; P22953; -.
DR PRIDE; P22953; -.
DR EnsemblPlants; AT5G02500.1; AT5G02500.1; AT5G02500. [P22953-1]
DR GeneID; 831020; -.
DR Gramene; AT5G02500.1; AT5G02500.1; AT5G02500. [P22953-1]
DR KEGG; ath:AT5G02500; -.
DR Araport; AT5G02500; -.
DR TAIR; locus:2181833; AT5G02500.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P22953; -.
DR OMA; KANPIMM; -.
DR PhylomeDB; P22953; -.
DR BRENDA; 3.6.4.10; 399.
DR PRO; PR:P22953; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P22953; baseline and differential.
DR Genevisible; P22953; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
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:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP: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 Acetylation; Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW Stress response; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..651
FT /note="Heat shock 70 kDa protein 1"
FT /id="PRO_0000078344"
FT REGION 618..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 65
FT /note="N -> S (in Ref. 6; CAA54419)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="S -> R (in Ref. 6; CAA54419)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="S -> T (in Ref. 2; CAA52684)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="D -> V (in Ref. 6; CAA54419)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="A -> V (in Ref. 6; CAA54419)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="I -> V (in Ref. 6; CAA54419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 71358 MW; BD689BA0C936A420 CRC64;
MSGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPVNTV FDAKRLIGRR FSDSSVQSDM KLWPFKIQAG PADKPMIYVE YKGEEKEFAA
EEISSMVLIK MREIAEAYLG VTIKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVMRIINEP
TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKSKKDIT GNPRALRRLR TSCERAKRTL SSTAQTTIEI DSLYEGIDFY
STITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSTVHDV VLVGGSTRIP KVQQLLQDFF
NGKELCKSIN PDEAVAYGAA VQGAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTTLI
PRNTTIPTKK EQVFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKDE IEKMVQEAEK YKSEDEEHKK
KVEAKNALEN YAYNMRNTIQ DEKIGEKLPA ADKKKIEDSI EQAIQWLEGN QLAEADEFED
KMKELESICN PIIAKMYQGA GGEAGGPGAS GMDDDAPPAS GGAGPKIEEV D
