HS702_ARATH
ID HS702_ARATH Reviewed; 653 AA.
AC P22954; O04293; Q0WUQ6; Q56WH2; Q9LZ53;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Heat shock 70 kDa protein 2 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Heat shock cognate 70 kDa protein 2 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock cognate protein 70-2 {ECO:0000303|PubMed:11402207};
DE Short=AtHsc70-2 {ECO:0000303|PubMed:11402207};
DE AltName: Full=Heat shock protein 70-2 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-2 {ECO:0000303|PubMed:11599561};
GN Name=HSP70-2 {ECO:0000303|PubMed:11599561};
GN Synonyms=HSC70-2 {ECO:0000303|PubMed:11402207},
GN HSC70-G8 {ECO:0000312|EMBL:CAA70105.1},
GN MED37_3 {ECO:0000303|PubMed:22021418}, MED37D;
GN OrderedLocusNames=At5g02490 {ECO:0000312|Araport:AT5G02490};
GN ORFNames=T22P11.80 {ECO:0000312|EMBL:CAB85986.1};
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=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 [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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
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 1-98.
RC STRAIN=cv. Ostwestfalen; TISSUE=Leaf;
RA King K.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 550-653.
RC STRAIN=cv. Columbia; TISSUE=Silique;
RA Wang Y.C., Lee S.P., Shieh K., Hu S.M., Wang C., Lin B.L.;
RT "Specific Hsp70s are expressed and accumulated during silique development
RT in Arabidopsis.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
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 [10]
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 [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 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 [13]
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 [14]
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 [15]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY CYTOKININ, AND
RP 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 {ECO:0000305|PubMed:11402207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21418353}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:28004282}. Nucleus
CC {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: Down-regulated during seed maturation.
CC {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: Induced by heat shock and cold (PubMed:11402207). Up-
CC regulated by viral infection (PubMed:15805473). Induced by infection
CC with the bacterial pathogen Pseudomonas syringae (PubMed:18065690).
CC Induced by cytokinin (PubMed:28004282). {ECO:0000269|PubMed:11402207,
CC ECO:0000269|PubMed:15805473, ECO:0000269|PubMed:18065690,
CC ECO:0000269|PubMed:28004282}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, under normal growth
CC conditions. {ECO:0000269|PubMed:21418353, ECO:0000269|PubMed:26408532,
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; AL162971; CAB85986.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90479.1; -; Genomic_DNA.
DR EMBL; AY093152; AAM13151.1; -; mRNA.
DR EMBL; BT008411; AAP37770.1; -; mRNA.
DR EMBL; AK222068; BAD94888.1; -; mRNA.
DR EMBL; AK227090; BAE99142.1; -; mRNA.
DR EMBL; AH001335; AAA32820.1; -; Genomic_DNA.
DR EMBL; X77199; CAA54420.1; -; Genomic_DNA.
DR EMBL; Y08892; CAA70105.1; -; mRNA.
DR PIR; JA0170; JA0170.
DR PIR; T48270; T48270.
DR RefSeq; NP_195869.1; NM_120327.5.
DR AlphaFoldDB; P22954; -.
DR SMR; P22954; -.
DR BioGRID; 17132; 20.
DR IntAct; P22954; 3.
DR STRING; 3702.AT5G02490.1; -.
DR iPTMnet; P22954; -.
DR MetOSite; P22954; -.
DR PaxDb; P22954; -.
DR PRIDE; P22954; -.
DR ProteomicsDB; 250836; -.
DR EnsemblPlants; AT5G02490.1; AT5G02490.1; AT5G02490.
DR GeneID; 831856; -.
DR Gramene; AT5G02490.1; AT5G02490.1; AT5G02490.
DR KEGG; ath:AT5G02490; -.
DR Araport; AT5G02490; -.
DR TAIR; locus:2181818; AT5G02490.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P22954; -.
DR OMA; NSITHAQ; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P22954; -.
DR BRENDA; 3.6.4.10; 399.
DR PRO; PR:P22954; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P22954; baseline and differential.
DR Genevisible; P22954; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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: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:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
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.
FT CHAIN 1..653
FT /note="Heat shock 70 kDa protein 2"
FT /id="PRO_0000078345"
FT REGION 617..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 6
FT /note="E -> K (in Ref. 6; CAA54420)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..102
FT /note="GTA -> ELQ (in Ref. 5; AAA32820)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="A -> G (in Ref. 4; BAD94888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 71387 MW; EDEC254DB06D9966 CRC64;
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPVNTV FDAKRLIGRR FSDASVQSDR QLWPFTIISG TAEKPMIVVE YKGEEKQFAA
EEISSMVLIK MREIAEAFLG TTVKNAVVTV PAYFNDSQRQ ATKDAGVIAG LNVLRIINEP
TAAAIAYGLD KKATSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKNKQDIT GQPRALRRLR TACERAKRTL SSTAQTTIEI DSLYGGADFY
SPITRARFEE MNMDLFRKCM EPVEKCLRDA KMDKSTVHEI VLVGGSTRIP KVQQLLQDFF
NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTTLI
QRNTTIPTKK EQVFSTYSDN QPGVLIQVFE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGKKNKITIT NDKGRLSKED IEKMVQEAEK YKSEDEEHKK
KVEAKNALEN YAYNMRNTIR DEKIGEKLPA ADKKKVEDSI EEAIQWLDGN QLGEADEFED
KMKELESVCN PIIAKMYQGG AGGEAGGPGA SGMDEDEAPP ASGGAGPKIE EVD
