HSP81_ORYSJ
ID HSP81_ORYSJ Reviewed; 699 AA.
AC Q0J4P2; P33126; Q6ZK13;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Heat shock protein 81-1;
DE Short=HSP81-1;
DE AltName: Full=Heat shock protein 82;
GN Name=HSP81-1; Synonyms=HSP82;
GN OrderedLocusNames=Os08g0500700, LOC_Os08g39140;
GN ORFNames=OJ1118_A06.20-1, OJ1345_D02.4-1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF24073.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003873; BAD08818.1; -; Genomic_DNA.
DR EMBL; AP003892; BAD08897.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24073.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015649678.1; XM_015794192.1.
DR AlphaFoldDB; Q0J4P2; -.
DR SMR; Q0J4P2; -.
DR STRING; 39947.Q0J4P2; -.
DR PaxDb; Q0J4P2; -.
DR PRIDE; Q0J4P2; -.
DR GeneID; 4345951; -.
DR KEGG; osa:4345951; -.
DR InParanoid; Q0J4P2; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q0J4P2; OS.
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: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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..699
FT /note="Heat shock protein 81-1"
FT /id="PRO_0000062951"
FT REGION 215..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 695..699
FT /note="TPR repeat-binding"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 699 AA; 80194 MW; 5381D14B572B3BCE CRC64;
MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA
QPELFIHIVP DKASNTLSII DSGIGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG
QFGVGFYSAY LVAERVVVTT KHNDDEQYVW ESQAGGSFTV TRDTSGEQLG RGTKITLYLK
DDQLEYLEER RLKDLIKKHS EFISYPISLW TEKTTEKEIS DDEDEEEKKD AEEGKVEDVD
EEKEEKEKKK KKIKEVSHEW SLVNKQKPIW MRKPEEITKE EYAAFYKSLT NDWEEHLAVK
HFSVEGQLEF KAVLFVPKRA PFDLFDTRKK LNNIKLYVRR VFIMDNCEEL IPEWLSFVKG
IVDSEDLPLN ISREMLQQNK ILKVIRKNLV KKCVELFFEI AENKEDYNKF YEAFSKNLKL
GIHEDSTNRN KIAELLRYHS TKSGDELTSL KDYVTRMKEG QNDIYYITGE SKKAVENSPF
LEKLKKKGYE VLYMVDAIDE YAVGQLKEFE GKKLVSATKE GLKLDESEDE KKRKEELKEK
FEGLCKVIKE VLGDKVEKVV VSDRVVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMAGY
MSSKKTMEIN PENAIMEELR KRADADKNDK SVKDLVLLLF ETALLTSGFS LDDPNTFGSR
IHRMLKLGLS IDEDETAEAD TDMPPLEDDA GESKMEEVD
