DP00142: Heat shock protein beta-1FASTA viewXML view

General information
DisProt:DP00142
Name:Heat shock protein beta-1
Synonym(s):HSPB1_MOUSE
HspB1
Heat shock 27 kDa protein
HSP 27
Growth-related 25 kDa protein
P25
HSP25
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P14602
UniGene:Mm.13849
SwissProt: HSPB1_MOUSE
TrEMBL:  
NCBI (GI): 547679
Source organism:Mus musculus (Mouse)
Sequence length:209
Percent disordered:9%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP - 60
AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG - 120
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS - 180
AEITIPVTFE ARAQIGGPEA GKSEQSGAK



Functional narrative    

Under conditions of cellular stress, small heat shock proteins, e.g. Hsp25, stabilize unfolding proteins and prevent their precipitation from solution. Hsp25 has a short, flexible and solvent-exposed C-terminal extension which protrudes from the domain core of the molecule. This extension adopts a statistically disordered conformation and it is is essential for complete chaperone activity and stability of Hsp25.

Region 1: 192-209

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:C-terminal extension
Location:192 - 209
Length:18
Region sequence:

RAQIGGPEAGKSEQSGAK

Modification type: Native
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Chaperones
Functional subclasses:  
Detection methods:
  1. Nuclear magnetic resonance (NMR)

References:
  1. Carver JA, Esposito G, Schwedersky G, Gaestel M. "1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids." FEBS Lett. 1995; 369(2-3): 305-10. PubMed: 7649277

Comments:
 



References

  1. Lindner RA, Carver JA, Ehrnsperger M, Buchner J, Esposito G, Behlke J, Lutsch G, Kotlyarov A, Gaestel M. "Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action." Eur J Biochem. 2000; 267(7): 1923-32. PubMed: 10727931


If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us.


Disprot-footer
Contact us