HSP83_ORYSJ
ID HSP83_ORYSJ Reviewed; 699 AA.
AC Q07078; Q69QQ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Heat shock protein 81-3;
DE Short=HSP81-3;
DE AltName: Full=Gravity-specific protein GSC 381 {ECO:0000303|PubMed:1363521};
GN Name=HSP81-3; OrderedLocusNames=Os09g0482400 {ECO:0000312|EMBL:BAT08654.1};
GN ORFNames=P0463D04.35 {ECO:0000312|EMBL:BAD33409.1};
GN and
GN OrderedLocusNames=Os09g0482600 {ECO:0000312|EMBL:BAT08658.1},
GN LOC_Os09g30418 {ECO:0000305};
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=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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-463, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RX PubMed=1363521; DOI=10.1266/jjg.67.335;
RA Kwon S., Kikuchi S., Oono K.;
RT "Molecular cloning and characterization of gravity specific cDNA in rice
RT (Oryza sativa L.) suspension callus.";
RL Jpn. J. Genet. 67:335-348(1992).
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. {ECO:0000250|UniProtKB:P07900}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02829}.
CC -!- TISSUE SPECIFICITY: Expressed in callus. {ECO:0000269|PubMed:1363521}.
CC -!- INDUCTION: By gravity stress. {ECO:0000269|PubMed:1363521}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250|UniProtKB:P02829}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01912.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA01912.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAB31515.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB31515.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AP005392; BAD33409.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08654.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08658.1; -; Genomic_DNA.
DR EMBL; D11138; BAA01912.1; ALT_SEQ; mRNA.
DR EMBL; S56878; CAB31515.1; ALT_SEQ; mRNA.
DR PIR; T04311; T04311.
DR RefSeq; XP_015611111.1; XM_015755625.1.
DR RefSeq; XP_015611112.1; XM_015755626.1.
DR RefSeq; XP_015611113.1; XM_015755627.1.
DR PDB; 4X9L; X-ray; 3.10 A; A=1-216.
DR PDBsum; 4X9L; -.
DR AlphaFoldDB; Q07078; -.
DR SMR; Q07078; -.
DR STRING; 4530.OS09T0482400-01; -.
DR iPTMnet; Q07078; -.
DR PRIDE; Q07078; -.
DR EnsemblPlants; Os09t0482400-01; Os09t0482400-01; Os09g0482400.
DR EnsemblPlants; Os09t0482600-01; Os09t0482600-01; Os09g0482600.
DR GeneID; 4347405; -.
DR GeneID; 9267802; -.
DR Gramene; Os09t0482400-01; Os09t0482400-01; Os09g0482400.
DR Gramene; Os09t0482600-01; Os09t0482600-01; Os09g0482600.
DR KEGG; osa:4347405; -.
DR KEGG; osa:9267802; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q07078; -.
DR OMA; AHDQPME; -.
DR OrthoDB; 924636at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR ExpressionAtlas; Q07078; baseline and differential.
DR Genevisible; Q07078; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..699
FT /note="Heat shock protein 81-3"
FT /id="PRO_0000062955"
FT REGION 215..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..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 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 101..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 121..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07900"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P02829"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 31..53
FT /evidence="ECO:0007829|PDB:4X9L"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4X9L"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4X9L"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4X9L"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4X9L"
SQ SEQUENCE 699 AA; 80184 MW; 317B10F0FC81DE89 CRC64;
MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA
QPELFIHIVP DKASNTLSII DSGVGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG
QFGVGFYSAY LVAERVVVTT KHNDDEQYVW ESQAGGSFTV TRDTSGEQLG RGTKITLYLK
DDQLEYLEER RLKDLVKKHS EFISYPISLW TEKTTEKEIS DDEDEEEKKD AEEGKVEDVD
EEKEEKEKKK KKIKEVSHEW NVMNKQKPIW LRKPEEITKE EYAAFYKSLT NDWEEHLAVK
HFSVEGQLEF KAILFVPKRA PFDLFDTRKK QNNIKLYVRR VFIMDNCEEL IPEWLSFVKG
IVDSEDLPLN ISREMLQQNK ILKVIRKNLV KKCVELFFEI AENKEDYNKF YEAFSKNLKL
GIHEDSTNRT KIAELLRYHS TKSGDELTSL KDYVTRMKEG QSEIYYITGE SKKAVENSPF
LEKLKKKGYE VLYMVDAIDE YAVGQLKEFE GKKLVSATKE GLKLDESEDE KKRQEELKEK
FEGLCKVIKE VLGDKVEKVV VSDRVVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMAGY
MSSKKTMEIN PENAIMDELR KRADADKNDK SVKDLVMLLF ETALLTSGFS LEDPNTFGTR
IHRMLKLGLS IDEDESAEAD ADMPPLEDDA GESKMEEVD
