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
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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.
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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: | 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:
- Nuclear magnetic resonance (NMR)
| References:
- 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
- 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:
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References |
- 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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