HS904_ARATH
ID HS904_ARATH Reviewed; 699 AA.
AC O03986;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Heat shock protein 90-4 {ECO:0000305};
DE Short=AtHSP90.4 {ECO:0000305};
DE Short=AtHsp90-4 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 81-4 {ECO:0000305};
DE Short=Hsp81-4 {ECO:0000303|PubMed:11599565};
GN Name=HSP90-4 {ECO:0000303|PubMed:11599565};
GN Synonyms=HSP81-4 {ECO:0000303|PubMed:11599565};
GN OrderedLocusNames=At5g56000; ORFNames=MDA7.4;
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. 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 [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;
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 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 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).
CC -!- FUNCTION: Molecular chaperone which stabilizes unfolding protein
CC intermediates and functions as a folding molecular chaperone that
CC assists the non-covalent folding of proteins in an ATP-dependent
CC manner. {ECO:0000250|UniProtKB:P27323}.
CC -!- SUBUNIT: Homodimer. Interacts with OEP61, OEP64 and OM64.
CC {ECO:0000269|PubMed:24036116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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}.
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DR EMBL; Y11828; CAA72514.1; -; Genomic_DNA.
DR EMBL; AB011476; BAB09282.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96708.1; -; Genomic_DNA.
DR EMBL; AK227254; BAE99287.1; -; mRNA.
DR RefSeq; NP_200411.1; NM_124982.3.
DR PDB; 6HPG; X-ray; 2.00 A; a/b/c/d/e/f=692-699.
DR PDB; 6Q3Q; X-ray; 2.00 A; a/b=692-699.
DR PDBsum; 6HPG; -.
DR PDBsum; 6Q3Q; -.
DR AlphaFoldDB; O03986; -.
DR SMR; O03986; -.
DR BioGRID; 20942; 34.
DR STRING; 3702.AT5G56000.1; -.
DR iPTMnet; O03986; -.
DR MetOSite; O03986; -.
DR PaxDb; O03986; -.
DR PRIDE; O03986; -.
DR ProteomicsDB; 230148; -.
DR EnsemblPlants; AT5G56000.1; AT5G56000.1; AT5G56000.
DR GeneID; 835698; -.
DR Gramene; AT5G56000.1; AT5G56000.1; AT5G56000.
DR KEGG; ath:AT5G56000; -.
DR Araport; AT5G56000; -.
DR TAIR; locus:2161775; AT5G56000.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; O03986; -.
DR OMA; AHDQPME; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; O03986; -.
DR PRO; PR:O03986; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O03986; baseline and differential.
DR Genevisible; O03986; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0003729; F:mRNA binding; IDA:TAIR.
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: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 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..699
FT /note="Heat shock protein 90-4"
FT /id="PRO_0000403651"
FT REGION 219..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..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"
SQ SEQUENCE 699 AA; 80141 MW; 28332C54455E0C3E CRC64;
MADAETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KTNNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VADKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGEALGR GTKMILYLKE
DQMEYIEERR LKDLVKKHSE FISYPISLWI EKTIEKEISD DEEEEEKKDE EGKVEEIDEE
KEKEEKKKKK IKEVTHEWDL VNKQKPIWMR KPEEINKEEY AAFYKSLSND WEEHLAVKHF
SVEGQLEFKA ILFVPKRAPF DLFDTKKKPN NIKLYVRRVF IMDNCEDIIP DYLGFVKGIV
DSEDLPLNIS RETLQQNKIL KVIRKNLVKK CLELFFEIAE NKEDYNKFYE AFSKNLKLGI
HEDSQNRTKI AELLRYHSTK SGDELTSLKD YVTRMKEGQN EIFYITGESK KAVENSPFLE
KLKKKGYEVL YMVDAIDEYA IGQLKEFEGK KLVSATKEGL KLEETDDEKK KKEELKEKFE
GLCKVIKDVL GDKVEKVIVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL KDSNTGGYMS
SKKTMEINPE NSIMDELRKR AEADKNDKSV KDLVLLLFET ALLTSGFSLD EPNTFGSRIH
RMLKLGLSIE EDDAVEADAE MPPLEDDADA EGSKMEEVD
