HSP83_IPONI
ID HSP83_IPONI Reviewed; 703 AA.
AC P51819;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Heat shock protein 83;
GN Name=HSP83A;
OS Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=35883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Cotyledon;
RX PubMed=16653195; DOI=10.1104/pp.100.4.1764;
RA Felsheim R.F., Das A.;
RT "Structure and expression of a heat shock protein 83 (hsp83) gene of
RT Pharbitis nil.";
RL Plant Physiol. 100:1764-1771(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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By heat shock and light. This heat shock protein is induced
CC by light only after a prolonged dark period or vice versa.
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; M99431; AAA33748.1; -; Genomic_DNA.
DR RefSeq; XP_019149680.1; XM_019294135.1.
DR AlphaFoldDB; P51819; -.
DR SMR; P51819; -.
DR PRIDE; P51819; -.
DR GeneID; 109146489; -.
DR KEGG; ini:109146489; -.
DR OrthoDB; 924636at2759; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..703
FT /note="Heat shock protein 83"
FT /id="PRO_0000062954"
FT REGION 220..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 699..703
FT /note="TPR repeat-binding"
FT COMPBIAS 222..243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..703
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 703 AA; 80821 MW; C8E5DC10586AB736 CRC64;
MADVQMAEAE TFAFQAEINQ LLSLIINTFY SNKEIFLREL ISNASDALDK IRFESLTDKS
KLDAQPELFI RLVPDKTNKT LSIIDSGVGM AKADLVNNLG TIARSGTKEF MEALQAGADV
SMIGQFGVGF YSAYLVAEKV IVTTKHNDDE QYIWESQAGG SFTVTRDVDG EQLGRGTKIT
LFLKEDQLEY LEERRIKDLV KKHSEFISYP IYLWTEKTTE KEISDDEDDE PKKEEEGDIE
EVDEDKEKEG KKKKKIKEVS HEWQLINKQK PIWLRKPEEI TKEEYASFYK SLTNDWEDHL
AVKHFSVEGQ LEFKAILFVP KRAPFDLFDT RKKMNNIKLY VRRVFIMDNC EELIPEYLGF
VKGVVDSDDL PLNISREMLQ QNKILKVIRK NLVKKCIEMF NEIAENKDDY NKFYEAFSKN
LKLGIHEDSQ NRAKLADLLR YYSTKSGDEL TSLKDYVTRM KEGQKDIYYI TGESKKAVEN
SPFLERLKKK GYEVLFMVDA IDEYAVGQLK EYDGKKLVSA TKEGLKLEDD DEEEKKKREE
KKKSFENLCK IIKDILGDKV EKVVVSDRIV DSPCCLVTGE YGWTANMERI MKAQALRDSS
MSSYMSSKKT MEINPDNGIM EELRKRAEAD KNDKSVKDLV LLLFETALLT SGFSLDDPNT
FGARIHRMLK LGLSIDEEEA GDDADMPALE EEAGEESKME EVD