HS903_ARATH
ID HS903_ARATH Reviewed; 699 AA.
AC P51818; O03985; Q8VYT8; Q94A60; Q9FKU5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Heat shock protein 90-3 {ECO:0000305};
DE Short=AtHSP90.3 {ECO:0000305};
DE Short=AtHsp90-3 {ECO:0000303|PubMed:11599565};
DE AltName: Full=HSP81.2;
DE AltName: Full=Heat shock protein 81-3 {ECO:0000305};
DE Short=Hsp81-3 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Protein MUTANT SNC1-ENHANCING 10 {ECO:0000303|PubMed:24889324};
GN Name=HSP90-3 {ECO:0000303|PubMed:11599565};
GN Synonyms=HSP81-3 {ECO:0000303|PubMed:11599565}, HSP81.2,
GN MUSE10 {ECO:0000303|PubMed:24889324}; OrderedLocusNames=At5g56010;
GN ORFNames=MDA7.5;
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;
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 [2]
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 [3]
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 [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=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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, INTERACTION WITH SNC1, AND MUTAGENESIS OF SER-100.
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: 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). 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:23827697,
CC ECO:0000269|PubMed:24611624, ECO:0000269|PubMed:24889324}.
CC -!- SUBUNIT: Homodimer. Interacts with OEP61, OEP64 and OM64
CC (PubMed:24036116). Interacts with SNC1 (PubMed:24889324).
CC {ECO:0000269|PubMed:24036116, ECO:0000269|PubMed:24889324}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Present in all tissues. Most abundantly expressed
CC in roots and floral bud clusters followed by flowers, young fruits and
CC rosette leaves.
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: 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 and also increase after salt treatment.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB33937.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; S77849; AAB33937.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y11827; CAA72513.1; -; Genomic_DNA.
DR EMBL; AB011476; BAB09283.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96709.1; -; Genomic_DNA.
DR EMBL; AY062832; AAL32910.1; -; mRNA.
DR EMBL; AY081302; AAL91191.1; -; mRNA.
DR EMBL; AY070031; AAL49788.1; -; mRNA.
DR EMBL; AY050349; AAK91366.1; -; mRNA.
DR RefSeq; NP_200412.1; NM_124983.4.
DR AlphaFoldDB; P51818; -.
DR SMR; P51818; -.
DR BioGRID; 20943; 35.
DR STRING; 3702.AT5G56010.1; -.
DR iPTMnet; P51818; -.
DR PaxDb; P51818; -.
DR PRIDE; P51818; -.
DR ProteomicsDB; 230249; -.
DR EnsemblPlants; AT5G56010.1; AT5G56010.1; AT5G56010.
DR GeneID; 835699; -.
DR Gramene; AT5G56010.1; AT5G56010.1; AT5G56010.
DR KEGG; ath:AT5G56010; -.
DR Araport; AT5G56010; -.
DR TAIR; locus:2161790; AT5G56010.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P51818; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P51818; -.
DR PRO; PR:P51818; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P51818; baseline and differential.
DR Genevisible; P51818; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:TAIR.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:TAIR.
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 GO; GO:0009408; P:response to heat; IMP:TAIR.
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..699
FT /note="Heat shock protein 90-3"
FT /id="PRO_0000062948"
FT REGION 219..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..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 100
FT /note="S->F: In muse10; enhances snc1-mediated autoimmune
FT phenotypes."
FT /evidence="ECO:0000269|PubMed:24889324"
FT CONFLICT 28
FT /note="K -> L (in Ref. 2; CAA72513)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="N -> K (in Ref. 2; CAA72513)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="L -> F (in Ref. 5; AAL49788)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="E -> G (in Ref. 2; CAA72513)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="V -> L (in Ref. 2; CAA72513)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 80052 MW; 1DC8044D787665B6 CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VADKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGEALGR GTKMVLYLKE
DQMEYIEERR 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 RDSSMGGYMS
SKKTMEINPE NSIMDELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGSRIH
RMLKLGLSID DDDVVEADAD MPPLEDDADA EGSKMEEVD
