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.
|
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:
- 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:
- 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)
|
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
|