| 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
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MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP - 60
AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG - 120
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS - 180
AEITIPVTFE ARAQIGGPEA GKSEQSGAK
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| 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.
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| 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.
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| 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:
- Nuclear magnetic resonance (NMR)
| References:
- 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:
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| References |
- 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
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