DP00445: Alpha-crystallin B chainFASTA viewXML view

General information
DisProt:DP00445
Name:Alpha-crystallin B chain
Synonym(s):CRYAB_HUMAN
Alpha(B)-crystallin
Rosenthal fiber component
Heat shock protein beta-5
HspB5
Renal carcinoma antigen NY-REN-27
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P02511
UniGene: 
SwissProt: CRYAB_HUMAN
TrEMBL:  
NCBI (GI): 117385
Source organism:Homo sapiens (Human)
Sequence length:175
Percent disordered:16%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW - 60
FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR - 120
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK



Functional narrative    

Alpha-crystallins are evolutionarily well conserved from bacteria to humans and belong to the family of the ubiquitous small heat shock proteins. Alpha A- and alpha B-crystallins are multimeric proteins having a subunit molecular mass of ~20 kDa. They are abundantly present in the eye lens as dynamic, heteromultimeric complexes and are encoded by two different genes. Both subunits can also form stable homomultimers. Alpha-crystallin prevents the aggregation of other lens crystallins and proteins that have become unfolded by "trapping" the protein in these high molecular weight complexes. Alpha B-crystallin is also expressed in sufficient amounts in other non-lenticular tissues such as the brain, heart, and kidney. Levels of alpha B-crystallin are seen to increase dramatically in response to heat shock, ischemia, oxidation, infection, and various disease conditions. May contribute to the transparency and refractive index of the lens.

Region 1: 148-175

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:148 - 175
Length:28
Region sequence:

PRKQVSGPERTIPITREEKPAVTAAPKK

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

References:
  1. Carver JA, Lindner RA. "NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins." Int J Biol Macromol. 1998; 22(3-4): 197-209. PubMed: 9650074

  2. Pasta SY, Raman B, Ramakrishna T, Rao ChM. "Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity." J Biol Chem. 2002; 277(48): 45821-8. PubMed: 12235146

Comments:
 



References

  1. Augusteyn RC. "alpha-crystallin: a review of its structure and function." Clin Exp Optom. 2004; 87(6): 356-66. PubMed: 15575808


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