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Heat shock protein 90-3 (AtHSP90.3) (AtHsp90-3) (HSP81.2) (Heat shock protein 81-3) (Hsp81-3) (Protein MUTANT SNC1-ENHANCING 10)

 HS903_ARATH             Reviewed;         699 AA.
P51818; O03985; Q8VYT8; Q94A60; Q9FKU5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
06-DEC-2002, sequence version 2.
05-DEC-2018, entry version 149.
RecName: Full=Heat shock protein 90-3 {ECO:0000305};
Short=AtHSP90.3 {ECO:0000305};
Short=AtHsp90-3 {ECO:0000303|PubMed:11599565};
AltName: Full=HSP81.2;
AltName: Full=Heat shock protein 81-3 {ECO:0000305};
Short=Hsp81-3 {ECO:0000303|PubMed:11599565};
AltName: Full=Protein MUTANT SNC1-ENHANCING 10 {ECO:0000303|PubMed:24889324};
Name=HSP90-3 {ECO:0000303|PubMed:11599565};
Synonyms=HSP81-3 {ECO:0000303|PubMed:11599565}, HSP81.2,
MUSE10 {ECO:0000303|PubMed:24889324}; OrderedLocusNames=At5g56010;
ORFNames=MDA7.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=7697294;
Yabe N., Takahashi T., Komeda Y.;
"Analysis of tissue-specific expression of Arabidopsis thaliana HSP90-
family gene HSP81.";
Plant Cell Physiol. 35:1207-1219(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Landsberg erecta;
PubMed=9426614; DOI=10.1023/A:1005874521528;
Milioni D., Hatzopoulos P.;
"Genomic organization of hsp90 gene family in Arabidopsis.";
Plant Mol. Biol. 35:955-961(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599565; DOI=10.1379/1466-1268(2001)006<0238:THFOPI>2.0.CO;2;
Krishna P., Gloor G.;
"The Hsp90 family of proteins in Arabidopsis thaliana.";
Cell Stress Chaperones 6:238-246(2001).
[7]
DEVELOPMENTAL STAGE.
PubMed=15582930; DOI=10.1093/jxb/eri035;
Prasinos C., Krampis K., Samakovli D., Hatzopoulos P.;
"Tight regulation of expression of two Arabidopsis cytosolic Hsp90
genes during embryo development.";
J. Exp. Bot. 56:633-644(2005).
[8]
HOMODIMERIZATION, AND INTERACTION WITH OEP61; OEP64 AND OM64.
PubMed=24036116; DOI=10.1074/jbc.M113.493015;
Schweiger R., Soll J., Jung K., Heermann R., Schwenkert S.;
"Quantification of interaction strengths between chaperones and
tetratricopeptide repeat domain-containing membrane proteins.";
J. Biol. Chem. 288:30614-30625(2013).
[9]
FUNCTION.
PubMed=23827697; DOI=10.1016/j.plaphy.2013.05.039;
Cha J.Y., Ahn G., Kim J.Y., Kang S.B., Kim M.R., Su'udi M., Kim W.Y.,
Son D.;
"Structural and functional differences of cytosolic 90-kDa heat-shock
proteins (Hsp90s) in Arabidopsis thaliana.";
Plant Physiol. Biochem. 70:368-373(2013).
[10]
FUNCTION.
PubMed=24611624; DOI=10.1111/nph.12760;
Bao F., Huang X., Zhu C., Zhang X., Li X., Yang S.;
"Arabidopsis HSP90 protein modulates RPP4-mediated temperature-
dependent cell death and defense responses.";
New Phytol. 202:1320-1334(2014).
[11]
FUNCTION, INTERACTION WITH SNC1, AND MUTAGENESIS OF SER-100.
PubMed=24889324; DOI=10.1111/tpj.12573;
Huang S., Monaghan J., Zhong X., Lin L., Sun T., Dong O.X., Li X.;
"HSP90s are required for NLR immune receptor accumulation in
Arabidopsis.";
Plant J. 79:427-439(2014).
-!- FUNCTION: Functions as a holding molecular chaperone (holdase)
which stabilizes unfolding protein intermediates and rapidly
releases them in an active form once stress has abated. Functions
as a folding molecular chaperone (foldase) that assists the non-
covalent folding of proteins in an ATP-dependent manner
(PubMed:23827697). Regulates RPP4-mediated temperature-dependent
cell death and defense responses (PubMed:24611624). May assist
SGT1B in the formation of SCF E3 ubiquitin ligase complexes that
target the immune receptors SNC1, RPS2 and RPS4 for degradation,
to regulate receptor levels and avoid autoimmunity
(PubMed:24889324). {ECO:0000269|PubMed:23827697,
ECO:0000269|PubMed:24611624, ECO:0000269|PubMed:24889324}.
-!- SUBUNIT: Homodimer. Interacts with OEP61, OEP64 and OM64
(PubMed:24036116). Interacts with SNC1 (PubMed:24889324).
{ECO:0000269|PubMed:24036116, ECO:0000269|PubMed:24889324}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- TISSUE SPECIFICITY: Present in all tissues. Most abundantly
expressed in roots and floral bud clusters followed by flowers,
young fruits and rosette leaves.
-!- DEVELOPMENTAL STAGE: Expressed in pollen during pollen
development, germination and tube growth. Expressed during embryo
development and young seedling growth.
{ECO:0000269|PubMed:15582930}.
-!- INDUCTION: In contrast to other major heat shock proteins, this
one is also expressed at normal growth temperatures. Levels
increase only slightly after heat shock. Also increase after salt
treatment.
-!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
repeat-containing proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the heat shock protein 90 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB33937.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; S77849; AAB33937.1; ALT_SEQ; Genomic_DNA.
EMBL; Y11827; CAA72513.1; -; Genomic_DNA.
EMBL; AB011476; BAB09283.1; -; Genomic_DNA.
EMBL; CP002688; AED96709.1; -; Genomic_DNA.
EMBL; AY062832; AAL32910.1; -; mRNA.
EMBL; AY081302; AAL91191.1; -; mRNA.
EMBL; AY070031; AAL49788.1; -; mRNA.
EMBL; AY050349; AAK91366.1; -; mRNA.
RefSeq; NP_200412.1; NM_124983.4.
UniGene; At.45945; -.
UniGene; At.47215; -.
ProteinModelPortal; P51818; -.
SMR; P51818; -.
BioGrid; 20943; 7.
STRING; 3702.AT5G56010.1; -.
iPTMnet; P51818; -.
PaxDb; P51818; -.
PRIDE; P51818; -.
EnsemblPlants; AT5G56010.1; AT5G56010.1; AT5G56010.
GeneID; 835699; -.
Gramene; AT5G56010.1; AT5G56010.1; AT5G56010.
KEGG; ath:AT5G56010; -.
Araport; AT5G56010; -.
TAIR; locus:2161790; AT5G56010.
eggNOG; KOG0019; Eukaryota.
eggNOG; COG0326; LUCA.
HOGENOM; HOG000031988; -.
InParanoid; P51818; -.
KO; K04079; -.
OMA; VKRHSEF; -.
OrthoDB; EOG093604DD; -.
PhylomeDB; P51818; -.
Reactome; R-ATH-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-844456; The NLRP3 inflammasome.
PRO; PR:P51818; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; P51818; baseline and differential.
Genevisible; P51818; AT.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0071277; P:cellular response to calcium ion; IMP:TAIR.
GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:TAIR.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:0009408; P:response to heat; IMP:TAIR.
CDD; cd00075; HATPase_c; 1.
Gene3D; 1.20.120.790; -; 1.
Gene3D; 3.30.565.10; -; 1.
HAMAP; MF_00505; HSP90; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR019805; Heat_shock_protein_90_CS.
InterPro; IPR037196; HSP90_C.
InterPro; IPR001404; Hsp90_fam.
InterPro; IPR020575; Hsp90_N.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR11528; PTHR11528; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00183; HSP90; 1.
PIRSF; PIRSF002583; Hsp90; 1.
PRINTS; PR00775; HEATSHOCK90.
SMART; SM00387; HATPase_c; 1.
SUPFAM; SSF110942; SSF110942; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS00298; HSP90; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Nucleotide-binding; Phosphoprotein; Plant defense;
Reference proteome; Stress response.
CHAIN 1 699 Heat shock protein 90-3.
/FTId=PRO_0000062948.
NP_BIND 100 101 ATP. {ECO:0000250|UniProtKB:P02829}.
NP_BIND 120 125 ATP. {ECO:0000250|UniProtKB:P02829}.
MOTIF 695 699 TPR repeat-binding.
COMPBIAS 222 226 Poly-Glu.
COMPBIAS 246 252 Poly-Lys.
COMPBIAS 529 532 Poly-Lys.
BINDING 34 34 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 38 38 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 80 80 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 85 85 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 93 93 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 99 99 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 172 172 ATP. {ECO:0000250|UniProtKB:P02829}.
BINDING 371 371 ATP. {ECO:0000250|UniProtKB:P02829}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:P27323}.
MUTAGEN 100 100 S->F: In muse10; enhances snc1-mediated
autoimmune phenotypes.
{ECO:0000269|PubMed:24889324}.
CONFLICT 28 28 K -> L (in Ref. 2; CAA72513).
{ECO:0000305}.
CONFLICT 92 92 N -> K (in Ref. 2; CAA72513).
{ECO:0000305}.
CONFLICT 482 482 L -> F (in Ref. 5; AAL49788).
{ECO:0000305}.
CONFLICT 498 498 E -> G (in Ref. 2; CAA72513).
{ECO:0000305}.
CONFLICT 549 549 V -> L (in Ref. 2; CAA72513).
{ECO:0000305}.
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


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