ID HS906_ARATH Reviewed; 799 AA.
AC F4JFN3; A0A1I9LN11; Q0WRS4; Q9S7E7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Heat shock protein 90-6, mitochondrial {ECO:0000305};
DE Short=AtHSP90.6 {ECO:0000305};
DE Short=AtHsp90-6 {ECO:0000303|PubMed:11599565};
DE AltName: Full=Heat shock protein 89-1 {ECO:0000305};
DE Short=Hsp89-1 {ECO:0000303|PubMed:11599565};
DE Flags: Precursor;
GN Name=HSP90-6 {ECO:0000303|PubMed:11599565};
GN Synonyms=HSP89-1 {ECO:0000303|PubMed:11599565};
GN OrderedLocusNames=At3g07770 {ECO:0000312|Araport:AT3G07770};
GN ORFNames=F17A17.11 {ECO:0000312|EMBL:AAF21187.1},
GN MLP3.22 {ECO:0000312|EMBL:AAF13098.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH P23-1.
RX PubMed=20493581; DOI=10.1016/j.jplph.2010.03.016;
RA Song H., Fan P., Shi W., Zhao R., Li Y.;
RT "Expression of five AtHsp90 genes in Saccharomyces cerevisiae reveals
RT functional differences of AtHsp90s under abiotic stresses.";
RL J. Plant Physiol. 167:1172-1178(2010).
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: Interacts with P23-1. {ECO:0000269|PubMed:20493581}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13098.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF21187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009176; AAF13098.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013483; AAF21187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74602.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63969.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63970.1; -; Genomic_DNA.
DR EMBL; AK228225; BAF00175.1; -; mRNA.
DR RefSeq; NP_001319498.1; NM_001337742.1.
DR RefSeq; NP_001326027.1; NM_001337743.1.
DR RefSeq; NP_187434.2; NM_111656.4.
DR AlphaFoldDB; F4JFN3; -.
DR SMR; F4JFN3; -.
DR STRING; 3702.F4JFN3; -.
DR iPTMnet; F4JFN3; -.
DR MetOSite; F4JFN3; -.
DR PaxDb; 3702-AT3G07770-1; -.
DR ProteomicsDB; 228809; -.
DR EnsemblPlants; AT3G07770.1; AT3G07770.1; AT3G07770.
DR EnsemblPlants; AT3G07770.2; AT3G07770.2; AT3G07770.
DR EnsemblPlants; AT3G07770.3; AT3G07770.3; AT3G07770.
DR GeneID; 819968; -.
DR Gramene; AT3G07770.1; AT3G07770.1; AT3G07770.
DR Gramene; AT3G07770.2; AT3G07770.2; AT3G07770.
DR Gramene; AT3G07770.3; AT3G07770.3; AT3G07770.
DR KEGG; ath:AT3G07770; -.
DR Araport; AT3G07770; -.
DR TAIR; AT3G07770; HSP89.1.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; F4JFN3; -.
DR OMA; KWKLMNE; -.
DR OrthoDB; 547579at2759; -.
DR PRO; PR:F4JFN3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JFN3; baseline and differential.
DR Genevisible; F4JFN3; AT.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PANTHER; PTHR11528:SF41; HEAT SHOCK PROTEIN 90-6, MITOCHONDRIAL; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..799
FT /note="Heat shock protein 90-6, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434019"
FT REGION 23..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 190..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 214..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT CONFLICT 250
FT /note="S -> L (in Ref. 3; BAF00175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 90567 MW; 2B3E70F97FE9BC14 CRC64;
MIRLSKRSVS TLLRSGNQSF RIAAAASTSR SSPSATDVKR SDTESRWYSS LTNGQSKNSG
SFAQLNMKTN WFMGYRNESS AAASDSSSQA PPPAEKFEYQ AEVSRLMDLI VNSLYSNKEV
FLRELISNAS DALDKLRYLS VTNPELSKDA PDLDIRIYAD KENGIITLTD SGIGMTRQEL
VDCLGTIAQS GTAKFMKALK DSKDAGGDNN LIGQFGVGFY SAFLVADRVI VSTKSPKSDK
QYVWEGEANS SSFTIQEDTD PQSLIPRGTR ITLHLKQEAK NFADPERIQK LVKNYSQFVS
FPIYTWQEKG YTKEVEVEDD PTETKKDDQD DQTEKKKKTK KVVERYWDWE LTNETQPIWL
RNPKEVTTAE YNEFYRKAFN EYLDPLASSH FTTEGEVEFR SILYVPPVSP SGKDDIVNQK
TKNIRLYVKR VFISDDFDGE LFPRYLSFVK GVVDSHDLPL NVSREILQES RIVRIMKKRL
VRKAFDMILG ISLSENREDY EKFWDNFGKH LKLGCIEDRE NHKRIAPLLR FFSSQSENDM
ISLDEYVENM KPEQKAIYFI ASDSITSAKN APFLEKMLEK GLEVLYLVEP IDEVAVQSLK
AYKEKDFVDI SKEDLDLGDK NEEKEAAVKK EFGQTCDWIK KRLGDKVASV QISNRLSSSP
CVLVSGKFGW SANMERLMKA QSTGDTISLD YMKGRRVFEI NPDHSIIKNI NAAYNSNPND
EDAMRAIDLM YDAALVSSGF TPDNPAELGG KIYEMMDVAL SGKWSSPEVQ PQQQQMAHSH
DAETFEAEVV EPVEVDGKK
//
