DP00676: 18.1 kDa class I heat shock proteinFASTA viewXML view

General information
DisProt:DP00676
Name:18.1 kDa class I heat shock protein
Synonym(s):HSP 18.1
HSP11_PEA
First appeared in release:Release 5.5 (11/17/2010)
UniProt:P19243
UniGene: 
SwissProt: HSP11_PEA
TrEMBL:  
NCBI (GI): 123555
Source organism:Pisum sativum (Garden pea)
Sequence length:158
Percent disordered:34%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSLIPSFFSG RRSNVFDPFS LDVWDPLKDF PFSNSSPSAS FPRENPAFVS TRVDWKETPE - 60
AHVFKADLPG LKKEEVKVEV EDDRVLQISG ERSVEKEDKN DEWHRVERSS GKFLRRFRLP - 120
ENAKMDKVKA SMENGVLTVT VPKEEIKKAE VKSIEISG



Functional narrative    

Chaperone that confers thermal protection to other proteins. Homooligomer of 12 subunits (dodecamer). It is donut shaped or disc shaped. Belongs to the small heat shock protein (HSP20) family.

Region 1: 1-53

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:N-terminal
Location:1 - 53
Length:53
Region sequence:

MSLIPSFFSGRRSNVFDPFSLDVWDPLKDFPFSNSSPSASFPRENPAFVSTRV

Modification type: Mutant
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Chaperones
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Size exclusion/gel filtration chromatography (pH: 7.4; flow rate 1 mL/min; KCl 150 mM; protein (sample) 100 uL; protein concentration 12 uM; sodium phosphate 25 mM; TSKgel G5000PWxL (column (Tosoh Biosciences) ))

References:
  1. Jaya N, Garcia V, Vierling E. "Substrate binding site flexibility of the small heat shock protein molecular chaperones." Proc Natl Acad Sci U S A. 2009; 106(37): 15604-9. PubMed: 19717454

Comments:
 



Comments


The protein used in this paper is a single-site variant of PsHsp18.1 in which the phenylalanine (Phe) analog, Bpa (26), was incorporated at specific positions throughout the protein.



AV 11-7-2010 (PubMed: 19717454)


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