※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||||||||||
Theoretical PI | 4.97 | ||||||||||||||||||||||||||||||||||||||||||
Molecular Weight | 80183.98 | ||||||||||||||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||||||||||||||
Protein Name | Heat shock protein 81-3; HSP81-3; Gravity-specific protein GSC 381 | ||||||||||||||||||||||||||||||||||||||||||
Gene Name | HSP81-3; Os09g0482300; Os09g0482400; LOC_Os09g30438; P0463D04.35 | ||||||||||||||||||||||||||||||||||||||||||
Created Date | 1996-10-01 | ||||||||||||||||||||||||||||||||||||||||||
Organism | Oryza sativa subsp. japonica(Rice) | ||||||||||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 39947 | ||||||||||||||||||||||||||||||||||||||||||
Phosphorylation Sites |
Functional Description Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Sequence Annotation chain 1 699 Heat shock protein 81-3 short sequence motif 695 699 TPR repeat-binding binding site 39 ATP binding site 81 ATP binding site 126 ATP; via amide nitrogen binding site 373 ATP Keyword ATP-binding,Chaperone,Complete proteome,Cytoplasm,Nucleotide-binding,Reference proteome,Stress response Sequence Source UniProt Protein Sequence MASETETFAF QAEINQLLSL IINTFYSNKE IFLRELISNS SDALDKIRFE SLTDKSKLDA 60 QPELFIHIVP DKASNTLSII DSGVGMTKSD LVNNLGTIAR SGTKEFMEAL AAGADVSMIG 120 QFGVGFYSAY LVAERVVVTT KHNDDEQYVW ESQAGGSFTV TRDTSGEQLG RGTKITLYLK 180 DDQLEYLEER RLKDLVKKHS EFISYPISLW TEKTTEKEIS DDEDEEEKKD AEEGKVEDVD 240 EEKEEKEKKK KKIKEVSHEW NVMNKQKPIW LRKPEEITKE EYAAFYKSLT NDWEEHLAVK 300 HFSVEGQLEF KAILFVPKRA PFDLFDTRKK QNNIKLYVRR VFIMDNCEEL IPEWLSFVKG 360 IVDSEDLPLN ISREMLQQNK ILKVIRKNLV KKCVELFFEI AENKEDYNKF YEAFSKNLKL 420 GIHEDSTNRT KIAELLRYHS TKSGDELTSL KDYVTRMKEG QSEIYYITGE SKKAVENSPF 480 LEKLKKKGYE VLYMVDAIDE YAVGQLKEFE GKKLVSATKE GLKLDESEDE KKRQEELKEK 540 FEGLCKVIKE VLGDKVEKVV VSDRVVDSPC CLVTGEYGWT ANMERIMKAQ ALRDSSMAGY 600 MSSKKTMEIN PENAIMDELR KRADADKNDK SVKDLVMLLF ETALLTSGFS LEDPNTFGTR 660 IHRMLKLGLS IDEDESAEAD ADMPPLEDDA GESKMEEVD 699 Gene Ontology GO:0048046; C: apoplast; IEA: EnsemblPlants/Gramene GO:0005618; C: cell wall; IEA: EnsemblPlants/Gramene GO:0009570; C: chloroplast stroma; IEA: EnsemblPlants/Gramene GO:0005829; C: cytosol; IEA: EnsemblPlants/Gramene GO:0005794; C: Golgi apparatus; IEA: EnsemblPlants/Gramene GO:0005634; C: nucleus; IEA: EnsemblPlants/Gramene GO:0005886; C: plasma membrane; IEA: EnsemblPlants/Gramene GO:0005774; C: vacuolar membrane; IEA: EnsemblPlants/Gramene GO:0005524; F: ATP binding; IEA: UniProtKB-KW GO:0006457; P: protein folding; IEA: InterPro GO:0006950; P: response to stress; IEA: UniProtKB-KW Interpro Pfam Pfam; PF00183; HSP90 SMART SMART; SM00387; HATPase_c PROSITE PS00298; HSP90 PRINTS PR00775; HEATSHOCK90 |