HS901_ARATH
ID HS901_ARATH Reviewed; 700 AA.
AC P27323; Q03930; Q8H0Z5; Q96268; Q9LTF3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Heat shock protein 90-1 {ECO:0000305};
DE Short=AtHSP90.1 {ECO:0000305};
DE Short=AtHsp90-1 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 81-1 {ECO:0000305};
DE Short=Hsp81-1 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 83;
GN Name=HSP90-1 {ECO:0000303|PubMed:11599565};
GN Synonyms=HSP81-1 {ECO:0000303|PubMed:11599565}, HSP83;
GN OrderedLocusNames=At5g52640; ORFNames=F6N7.13;
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=Leaf;
RX PubMed=16667903; DOI=10.1104/pp.94.4.1689;
RA Conner T.W., Lafayette P.R., Nagao R.T., Key J.L.;
RT "Sequence and expression of a HSP83 from Arabidopsis thaliana.";
RL Plant Physiol. 94:1689-1695(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Seed;
RX PubMed=7697294; DOI=10.1093/oxfordjournals.pcp.a078715;
RA Yabe N., Takahashi T., Komeda Y.;
RT "Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-
RT family gene HSP81.";
RL Plant Cell Physiol. 35:1207-1219(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9426614; DOI=10.1023/a:1005874521528;
RA Milioni D., Hatzopoulos P.;
RT "Genomic organization of hsp90 gene family in Arabidopsis.";
RL Plant Mol. Biol. 35:955-961(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, INTERACTION WITH RAR1, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14504384; DOI=10.1073/pnas.2033934100;
RA Takahashi A., Casais C., Ichimura K., Shirasu K.;
RT "HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated
RT disease resistance in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11777-11782(2003).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=15582930; DOI=10.1093/jxb/eri035;
RA Prasinos C., Krampis K., Samakovli D., Hatzopoulos P.;
RT "Tight regulation of expression of two Arabidopsis cytosolic Hsp90 genes
RT during embryo development.";
RL J. Exp. Bot. 56:633-644(2005).
RN [10]
RP INTERACTION WITH RAR1.
RX PubMed=17148606; DOI=10.1073/pnas.0607279103;
RA Shang Y., Li X., Cui H., He P., Thilmony R., Chintamanani S.,
RA Zwiesler-Vollick J., Gopalan S., Tang X., Zhou J.M.;
RT "RAR1, a central player in plant immunity, is targeted by Pseudomonas
RT syringae effector AvrB.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19200-19205(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [14]
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 [15]
RP FUNCTION.
RX PubMed=23827697; DOI=10.1016/j.plaphy.2013.05.039;
RA Cha J.Y., Ahn G., Kim J.Y., Kang S.B., Kim M.R., Su'udi M., Kim W.Y.,
RA Son D.;
RT "Structural and functional differences of cytosolic 90-kDa heat-shock
RT proteins (Hsp90s) in Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 70:368-373(2013).
RN [16]
RP INTERACTION WITH HTD1.
RX PubMed=25358503; DOI=10.14348/molcells.2014.0224;
RA Kim S.-H., Lee J.-H., Seo K.-I., Ryu B., Sung Y., Chung T., Deng X.W.,
RA Lee J.-H.;
RT "Characterization of a novel DWD protein that participates in heat stress
RT response in Arabidopsis.";
RL Mol. Cells 37:833-840(2014).
RN [17]
RP INTERACTION WITH POLL.
RX PubMed=26230318; DOI=10.1371/journal.pone.0133843;
RA Roy S., Banerjee V., Das K.P.;
RT "Understanding the physical and molecular basis of stability of Arabidopsis
RT DNA Pol lambda under UV-B and high NaCl stress.";
RL PLoS ONE 10:E0133843-E0133843(2015).
CC -!- FUNCTION: Functions as a holding molecular chaperone (holdase) which
CC stabilizes unfolding protein intermediates and rapidly releases them in
CC an active form once stress has abated. Functions as a folding molecular
CC chaperone (foldase) that assists the non-covalent folding of proteins
CC in an ATP-dependent manner (PubMed:23827697). Molecular chaperone
CC involved in R gene-mediated disease resistance. Required for full RPS2-
CC mediated resistance through interaction with RAR1. Possesses probably
CC ATPase activity (PubMed:14504384). {ECO:0000269|PubMed:14504384,
CC ECO:0000269|PubMed:23827697}.
CC -!- SUBUNIT: Homodimer (PubMed:24036116). Interacts with RAR1
CC (PubMed:14504384, PubMed:17148606). Interacts with OEP61, OEP64 and
CC OM64 (PubMed:24036116). Interacts with POLL (PubMed:26230318).
CC Interacts with HTD1 (PubMed:25358503). {ECO:0000269|PubMed:14504384,
CC ECO:0000269|PubMed:17148606, ECO:0000269|PubMed:24036116,
CC ECO:0000269|PubMed:25358503, ECO:0000269|PubMed:26230318}.
CC -!- INTERACTION:
CC P27323; Q38931: FKBP62; NbExp=4; IntAct=EBI-1778266, EBI-2409351;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots only. After heat
CC treatment, expressed in most tissues. Levels also increase after heavy
CC metal treatment.
CC -!- DEVELOPMENTAL STAGE: Expressed in pollen during pollen development,
CC germination and tube growth. Expressed during embryo development and
CC young seedling growth. {ECO:0000269|PubMed:15582930}.
CC -!- INDUCTION: By heat shock and infection by avirulent and virulent
CC bacterial pathogens (P.syringae). {ECO:0000269|PubMed:14504384}.
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 RPS2-mediated
CC disease resistance. {ECO:0000269|PubMed:14504384}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32822.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM91104.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN46890.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA98082.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA68885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M62984; AAA32822.1; ALT_INIT; mRNA.
DR EMBL; D00710; BAA00615.1; -; Genomic_DNA.
DR EMBL; Y07613; CAA68885.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB025606; BAA98082.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED96244.2; -; Genomic_DNA.
DR EMBL; AY128296; AAM91104.1; ALT_INIT; mRNA.
DR EMBL; BT001091; AAN46890.1; ALT_INIT; mRNA.
DR PIR; A45508; A45508.
DR RefSeq; NP_200076.2; NM_124642.4.
DR AlphaFoldDB; P27323; -.
DR SMR; P27323; -.
DR BioGRID; 20586; 44.
DR DIP; DIP-47087N; -.
DR IntAct; P27323; 5.
DR STRING; 3702.AT5G52640.1; -.
DR iPTMnet; P27323; -.
DR MetOSite; P27323; -.
DR PaxDb; P27323; -.
DR PRIDE; P27323; -.
DR ProteomicsDB; 232102; -.
DR EnsemblPlants; AT5G52640.1; AT5G52640.1; AT5G52640.
DR GeneID; 835341; -.
DR Gramene; AT5G52640.1; AT5G52640.1; AT5G52640.
DR KEGG; ath:AT5G52640; -.
DR Araport; AT5G52640; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P27323; -.
DR OMA; TRMKAEQ; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P27323; -.
DR PRO; PR:P27323; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P27323; baseline and differential.
DR Genevisible; P27323; 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; IEA:InterPro.
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 ATP-binding; Chaperone; Cytoplasm; Immunity; Innate immunity;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Stress response.
FT CHAIN 1..700
FT /note="Heat shock protein 90-1"
FT /id="PRO_0000062946"
FT REGION 215..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 696..700
FT /note="TPR repeat-binding"
FT COMPBIAS 217..239
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 372
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:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT CONFLICT 72
FT /note="S -> A (in Ref. 1; AAA32822)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="S -> P (in Ref. 3; CAA68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="T -> S (in Ref. 1; AAA32822 and 3; CAA68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="T -> I (in Ref. 2; BAA00615)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="E -> K (in Ref. 3; CAA68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Y -> S (in Ref. 1; AAA32822)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="Missing (in Ref. 3; CAA68885)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="E -> D (in Ref. 3; CAA68885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 80635 MW; 5B379E915757EC7B CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIRLVPD KSNKTLSIID SGIGMTKADL VNNLGTIARS GTKEFMEALQ AGADVSMIGQ
FGVGFYSAYL VAEKVVVTTK HNDDEQYVWE SQAGGSFTVT RDVDGEPLGR GTKITLFLKD
DQLEYLEERR LKDLVKKHSE FISYPIYLWT EKTTEKEISD DEDEDEPKKE NEGEVEEVDE
EKEKDGKKKK KIKEVSHEWE LINKQKPIWL RKPEEITKEE YAAFYKSLTN DWEDHLAVKH
FSVEGQLEFK AILFVPKRAP FDLFDTRKKL NNIKLYVRRV FIMDNCEELI PEYLSFVKGV
VDSDDLPLNI SRETLQQNKI LKVIRKNLVK KCIEMFNEIA ENKEDYTKFY EAFSKNLKLG
IHEDSQNRGK IADLLRYHST KSGDEMTSFK DYVTRMKEGQ KDIFYITGES KKAVENSPFL
ERLKKRGYEV LYMVDAIDEY AVGQLKEYDG KKLVSATKEG LKLEDETEEE KKKREEKKKS
FENLCKTIKE ILGDKVEKVV VSDRIVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMSGY
MSSKKTMEIN PDNGIMEELR KRAEADKNDK SVKDLVMLLY ETALLTSGFS LDEPNTFAAR
IHRMLKLGLS IDEDENVEED GDMPELEEDA AEESKMEEVD
