HS902_ARATH
ID HS902_ARATH Reviewed; 699 AA.
AC P55737; Q8H158;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Heat shock protein 90-2 {ECO:0000305};
DE Short=AtHSP90.2 {ECO:0000305};
DE Short=AtHsp90-2 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 81-2 {ECO:0000305};
DE Short=Hsp81-2 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Protein EARLY-RESPONSIVE TO DEHYDRATION 8;
DE AltName: Full=Protein LOSS OF RECOGNITION OF AVRRPM1 2;
DE AltName: Full=Protein MUTANT SNC1-ENHANCING 12 {ECO:0000303|PubMed:24889324};
GN Name=HSP90-2 {ECO:0000303|PubMed:11599565};
GN Synonyms=ERD8, HSP81-2 {ECO:0000303|PubMed:11599565}, LRA2,
GN MUSE12 {ECO:0000303|PubMed:24889324}; OrderedLocusNames=At5g56030;
GN ORFNames=MDA7.7;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=16668895; DOI=10.1104/pp.99.2.383;
RA Takahashi T., Naito S., Komeda Y.;
RT "Isolation and analysis of the expression of two genes for the 81-
RT kilodalton heat-shock proteins from Arabidopsis.";
RL Plant Physiol. 99:383-390(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:thfopi>2.0.co;2;
RA Krishna P., Gloor G.;
RT "The Hsp90 family of proteins in Arabidopsis thaliana.";
RL Cell Stress Chaperones 6:238-246(2001).
RN [6]
RP FUNCTION, INTERACTION WITH RPM1; RAR1 AND SGT1B, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASP-80; GLY-95 AND SER-100.
RX PubMed=14592967; DOI=10.1093/emboj/cdg547;
RA Hubert D.A., Tornero P., Belkhadir Y., Krishna P., Takahashi A.,
RA Shirasu K., Dangl J.L.;
RT "Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease
RT resistance protein.";
RL EMBO J. 22:5679-5689(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH HSFA1D.
RX PubMed=17965410; DOI=10.1074/jbc.m707168200;
RA Yamada K., Fukao Y., Hayashi M., Fukazawa M., Suzuki I., Nishimura M.;
RT "Cytosolic HSP90 regulates the heat shock response that is responsible for
RT heat acclimation in Arabidopsis thaliana.";
RL J. Biol. Chem. 282:37794-37804(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP FUNCTION, INTERACTION WITH RAR1 AND SGT1B, AND MUTAGENESIS OF ALA-11;
RP ALA-42 AND ARG-337.
RX PubMed=19487680; DOI=10.1073/pnas.0904877106;
RA Hubert D.A., He Y., McNulty B.C., Tornero P., Dangl J.L.;
RT "Specific Arabidopsis HSP90.2 alleles recapitulate RAR1 cochaperone
RT function in plant NB-LRR disease resistance protein regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9556-9563(2009).
RN [10]
RP FUNCTION.
RX PubMed=20147301; DOI=10.1093/pcp/pcq015;
RA Nishizawa-Yokoi A., Tainaka H., Yoshida E., Tamoi M., Yabuta Y.,
RA Shigeoka S.;
RT "The 26S proteasome function and Hsp90 activity involved in the regulation
RT of HsfA2 expression in response to oxidative stress.";
RL Plant Cell Physiol. 51:486-496(2010).
RN [11]
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 [12]
RP HOMODIMERIZATION, AND INTERACTION WITH OEP61; OEP64 AND OM64.
RX PubMed=24036116; DOI=10.1074/jbc.m113.493015;
RA Schweiger R., Soll J., Jung K., Heermann R., Schwenkert S.;
RT "Quantification of interaction strengths between chaperones and
RT tetratricopeptide repeat domain-containing membrane proteins.";
RL J. Biol. Chem. 288:30614-30625(2013).
RN [13]
RP FUNCTION.
RX PubMed=24611624; DOI=10.1111/nph.12760;
RA Bao F., Huang X., Zhu C., Zhang X., Li X., Yang S.;
RT "Arabidopsis HSP90 protein modulates RPP4-mediated temperature-dependent
RT cell death and defense responses.";
RL New Phytol. 202:1320-1334(2014).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF ARG-33 AND ASP-41.
RX PubMed=24889324; DOI=10.1111/tpj.12573;
RA Huang S., Monaghan J., Zhong X., Lin L., Sun T., Dong O.X., Li X.;
RT "HSP90s are required for NLR immune receptor accumulation in Arabidopsis.";
RL Plant J. 79:427-439(2014).
CC -!- FUNCTION: Molecular chaperone. Involved in RPM1-mediated resistance.
CC Component of the RPM1/RAR1/SGT1 complex. May stabilize RPM1 and protect
CC it from SGT1-mediated degradation. Associates with RAR1 which may
CC function as co-chaperone. Possesses ATPase activity (PubMed:14592967,
CC PubMed:19487680). In the absence of heat shock, negatively regulates
CC heat-inducible genes by actively suppressing heat shock transcription
CC factor A1D (HSFA1D) function (PubMed:17965410). Involved in the
CC induction of heat shock transcription factor A2 (HSFA2) expression in
CC response to oxidative stress (PubMed:20147301). Required for stomatal
CC closure and modulates transcriptional and physiological responses to
CC abscisic acid (ABA) (PubMed:21586649). Regulates RPP4-mediated
CC temperature-dependent cell death and defense responses
CC (PubMed:24611624). May assist SGT1B in the formation of SCF E3
CC ubiquitin ligase complexes that target the immune receptors SNC1, RPS2
CC and RPS4 for degradation, to regulate receptor levels and avoid
CC autoimmunity (PubMed:24889324). {ECO:0000269|PubMed:14592967,
CC ECO:0000269|PubMed:17965410, ECO:0000269|PubMed:19487680,
CC ECO:0000269|PubMed:20147301, ECO:0000269|PubMed:21586649,
CC ECO:0000269|PubMed:24611624, ECO:0000269|PubMed:24889324}.
CC -!- SUBUNIT: Homodimer (PubMed:19487680, PubMed:24036116). Interacts with
CC RPM1, RAR1 and SGT1B (PubMed:14592967, PubMed:19487680). Interacts with
CC OEP61, OEP64 and OM64 (PubMed:24036116). Interacts with HSFA1D
CC (PubMed:17965410). {ECO:0000269|PubMed:14592967,
CC ECO:0000269|PubMed:17965410, ECO:0000269|PubMed:19487680,
CC ECO:0000269|PubMed:24036116}.
CC -!- INTERACTION:
CC P55737; P25854: CAM4; NbExp=2; IntAct=EBI-1235834, EBI-1235664;
CC P55737; Q03509: CAM6; NbExp=2; IntAct=EBI-1235834, EBI-1236097;
CC P55737; P59220: CAM7; NbExp=2; IntAct=EBI-1235834, EBI-1236031;
CC P55737; Q9S744: CML9; NbExp=2; IntAct=EBI-1235834, EBI-1236048;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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=P55737-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Present in all tissues. Most abundantly expressed
CC in roots followed by floral bud clusters, flowers and young fruits.
CC -!- INDUCTION: In contrast to other major heat shock proteins, this one is
CC also expressed at normal growth temperatures. Levels increase only
CC slightly after heat shock.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. In case of infection, plants are altered in RPM1-mediated
CC disease resistance. {ECO:0000269|PubMed:14592967}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AB011476; BAB09285.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96711.1; -; Genomic_DNA.
DR EMBL; AY062750; AAL32828.1; -; mRNA.
DR EMBL; AY128805; AAM91205.1; -; mRNA.
DR EMBL; BT000717; AAN31859.1; -; mRNA.
DR EMBL; BT001944; AAN71943.1; -; mRNA.
DR EMBL; BT002535; AAO00895.1; -; mRNA.
DR RefSeq; NP_200414.1; NM_124985.5. [P55737-1]
DR AlphaFoldDB; P55737; -.
DR SMR; P55737; -.
DR BioGRID; 20945; 48.
DR DIP; DIP-51470N; -.
DR IntAct; P55737; 11.
DR iPTMnet; P55737; -.
DR MetOSite; P55737; -.
DR SwissPalm; P55737; -.
DR PRIDE; P55737; -.
DR EnsemblPlants; AT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
DR GeneID; 835701; -.
DR Gramene; AT5G56030.1; AT5G56030.1; AT5G56030. [P55737-1]
DR KEGG; ath:AT5G56030; -.
DR Araport; AT5G56030; -.
DR InParanoid; P55737; -.
DR PhylomeDB; P55737; -.
DR PRO; PR:P55737; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P55737; baseline and differential.
DR Genevisible; P55737; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chaperone; Cytoplasm; Immunity;
KW Innate immunity; Nucleotide-binding; Phosphoprotein; Plant defense;
KW Reference proteome; Stress response.
FT CHAIN 1..699
FT /note="Heat shock protein 90-2"
FT /id="PRO_0000062947"
FT REGION 219..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 695..699
FT /note="TPR repeat-binding"
FT COMPBIAS 219..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 100..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 120..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27323"
FT MUTAGEN 11
FT /note="A->T: In hsp90.2-7; No effect on ATPase activity,
FT dimerization and interaction with RAR1. Decreased
FT interaction with SGT1B."
FT /evidence="ECO:0000269|PubMed:19487680"
FT MUTAGEN 33
FT /note="R->H: In muse12; enhances snc1-mediated autoimmune
FT phenotypes."
FT /evidence="ECO:0000269|PubMed:24889324"
FT MUTAGEN 41
FT /note="D->N: In muse12; enhances snc1-mediated autoimmune
FT phenotypes."
FT /evidence="ECO:0000269|PubMed:24889324"
FT MUTAGEN 42
FT /note="A->T: In hsp90.2-6; Loss of RPM1 function and
FT accumulation. Loss of ATPase activity. Loss of
FT dimerization. Loss of interaction with RAR1 and SGT1B."
FT /evidence="ECO:0000269|PubMed:19487680"
FT MUTAGEN 80
FT /note="D->N: In hsp90.2-3/lra2-3; Loss of RPM1 function and
FT accumulation. Loss of ATPase activity. Loss of
FT dimerization. Loss of interaction with RAR1 and SGT1B."
FT /evidence="ECO:0000269|PubMed:14592967"
FT MUTAGEN 95
FT /note="G->E: In hsp90.2-1/lra2-1; Loss of RPM1 function and
FT accumulation. Loss of ATPase activity. Loss of
FT dimerization. Loss of interaction with RAR1 and SGT1B."
FT /evidence="ECO:0000269|PubMed:14592967"
FT MUTAGEN 100
FT /note="S->F: In hsp90.2-4/lra2-4; Loss of RPM1 function and
FT accumulation. Loss of ATPase activity. Loss of
FT dimerization. Normal interaction with RAR1. Loss of
FT interaction with SGT1B."
FT /evidence="ECO:0000269|PubMed:14592967"
FT MUTAGEN 337
FT /note="R->C: In hsp90.2-6; Decreased dimerization. Loss of
FT ATPase activity and interaction with RAR1 and SGT1B."
FT /evidence="ECO:0000269|PubMed:19487680"
FT CONFLICT 657
FT /note="S -> N (in Ref. 4; AAN31859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 80064 MW; 78A6E490AE48E508 CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VADKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGETLGR GTKMVLYLKE
DQLEYLEERR LKDLVKKHSE FISYPISLWI EKTIEKEISD DEEEEEKKDE EGKVEEVDEE
KEKEEKKKKK IKEVSHEWDL VNKQKPIWMR KPEEINKEEY AAFYKSLSND WEEHLAVKHF
SVEGQLEFKA ILFVPKRAPF DLFDTKKKPN NIKLYVRRVF IMDNCEDIIP EYLGFVKGIV
DSEDLPLNIS RETLQQNKIL KVIRKNLVKK CLELFFEIAE NKEDYNKFYE AFSKNLKLGI
HEDSQNRTKI AELLRYHSTK SGDELTSLKD YVTRMKEGQN DIFYITGESK KAVENSPFLE
KLKKKGIEVL YMVDAIDEYA IGQLKEFEGK KLVSATKEGL KLDETEDEKK KKEELKEKFE
GLCKVIKDVL GDKVEKVIVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS
SKKTMEINPE NSIMDELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGSRIH
RMLKLGLSID DDDAVEADAE MPPLEDDADA EGSKMEEVD
