HSP80_SOLLC
ID HSP80_SOLLC Reviewed; 699 AA.
AC P36181;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heat shock cognate protein 80;
GN Name=HSC80;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. UC82B; TISSUE=Shoot apex;
RX PubMed=16653061; DOI=10.1104/pp.100.2.801;
RA Koning A.J., Rose R., Comai L.;
RT "Developmental expression of tomato heat-shock cognate protein 80.";
RL Plant Physiol. 100:801-811(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 -!- TISSUE SPECIFICITY: Most abundantly expressed in roots and apical
CC shoots. Low expression in mature leaves.
CC -!- DEVELOPMENTAL STAGE: Increasing levels of expression observed in
CC developing ovaries, floral shoots and roots. Levels decrease with
CC maturation.
CC -!- INDUCTION: Heat treatment increases expression 3-fold in mature leaves.
CC Has little effect on developing shoot apices.
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; M96549; AAB01376.1; -; Genomic_DNA.
DR PIR; T07037; T07037.
DR RefSeq; NP_001234439.1; NM_001247510.1.
DR AlphaFoldDB; P36181; -.
DR SMR; P36181; -.
DR STRING; 4081.Solyc07g065840.2.1; -.
DR PaxDb; P36181; -.
DR PRIDE; P36181; -.
DR EnsemblPlants; Solyc07g065840.2.1; Solyc07g065840.2.1; Solyc07g065840.2.
DR GeneID; 543903; -.
DR Gramene; Solyc07g065840.2.1; Solyc07g065840.2.1; Solyc07g065840.2.
DR KEGG; sly:543903; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P36181; -.
DR OMA; ELISNAX; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P36181; -.
DR Proteomes; UP000004994; Chromosome 7.
DR ExpressionAtlas; P36181; baseline.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..699
FT /note="Heat shock cognate protein 80"
FT /id="PRO_0000062949"
FT REGION 219..248
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 219..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 699 AA; 80136 MW; BDF2357946AC6DEF CRC64;
MSDVETFAFQ AEINQLLSLI INTFYSNKEI FLRELISNSS DALDKIRFES LTDKSKLDGQ
PELFIHIIPD KANNTLTIID SGIGMTKADL VNNLGTIARS GTKEFMEALA AGADVSMIGQ
FGVGFYSAYL VAEKVVVTTK HNDDEQYVWE SQAGGSFTVT RDTSGENLGR GTKMVLYLKE
DQLEYLEERR LKDLIKKHSE FISYPISLWV EKTIEKEISD DEEEEEKKDE EGKVEEVDEE
KEKEEKKKKK VKEVSNEWSL VNKQKPIWMR KPEEITKEEY AAFYKSLTND WEEHLAVKHF
SVEGQLEFKA VLFVPKRAPF DLFDTKKKPN NIKLYVRRVF IMDNCDELIP EYLSFVKGIV
DSEDLPLNIS RETLQQNKIL KVIRKNLVKK CVELFFEIAE NKEDYNKFYE AFSKNLKLGI
HEDSQNRAKF AELLRYHSTK SGDEMTSLKD YVTRMKEGQN DIYYITGESK KAVENSPFLE
KLKKKGYEVL YMVDAIDEYS IGQLKEFEGK KLVSATKEGL KLDESEDEKK KQEELKEKFE
GLCKVMKDVL GDKVEKVIVS DRVVDSPCCL VTGEYGWTAN MERIMKAQAL RDSSMAGYMS
SKKTMEINPE NSIMDELRKR ADADKNDKSV KDLVLLLFET ALLTSGFSLE EPNTFGNRIH
RMLKLGLSID EESGDADADM PALEDPEADA EGSKMEEVD
