P68285 · CRYAA_HIPAM
- ProteinAlpha-crystallin A chain
- GeneCRYAA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids173 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | structural constituent of eye lens | |
Molecular Function | unfolded protein binding | |
Biological Process | lens development in camera-type eye | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | protein refolding | |
Biological Process | response to heat |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAlpha-crystallin A chain
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Whippomorpha > Ancodonta > Hippopotamidae > Hippopotamus
Accessions
- Primary accessionP68285
- Secondary accessions
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000125863 | 1-173 | Alpha-crystallin A chain | |||
Sequence: MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAIPVSREEKPSSAPSS | ||||||
Modified residue | 6 | Deamidated glutamine; partial | ||||
Sequence: Q | ||||||
Modified residue | 45 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 50 | Deamidated glutamine; partial | ||||
Sequence: Q | ||||||
Modified residue | 70 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 90 | Deamidated glutamine; partial | ||||
Sequence: Q | ||||||
Modified residue | 99 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 101 | Deamidated asparagine; partial | ||||
Sequence: N | ||||||
Modified residue | 122 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 123 | Deamidated asparagine; partial | ||||
Sequence: N | ||||||
Glycosylation | 162 | O-linked (GlcNAc) serine | ||||
Sequence: S |
Post-translational modification
Acetylation at Lys-70 may increase chaperone activity.
Undergoes age-dependent proteolytical cleavage at the C-terminus.
Keywords
- PTM
PTM databases
Interaction
Subunit
Heteromer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and homotetramers (dimers of dimers) which serve as the building blocks of homooligomers (By similarity).
Within homooligomers, the zinc-binding motif is created from residues of 3 different molecules. His-100 and Glu-102 from one molecule are ligands of the zinc ion, and His-107 and His-154 residues from additional molecules complete the site with tetrahedral coordination geometry (By similarity).
Part of a complex required for lens intermediate filament formation composed of BFSP1, BFSP2 and CRYAA (By similarity).
Within homooligomers, the zinc-binding motif is created from residues of 3 different molecules. His-100 and Glu-102 from one molecule are ligands of the zinc ion, and His-107 and His-154 residues from additional molecules complete the site with tetrahedral coordination geometry (By similarity).
Part of a complex required for lens intermediate filament formation composed of BFSP1, BFSP2 and CRYAA (By similarity).
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-63 | Required for complex formation with BFSP1 and BFSP2 | ||||
Sequence: MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE | ||||||
Domain | 52-162 | sHSP | ||||
Sequence: LFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAIPVS | ||||||
Region | 144-173 | Disordered | ||||
Sequence: PKIPSGVDAGHSERAIPVSREEKPSSAPSS |
Sequence similarities
Belongs to the small heat shock protein (HSP20) family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length173
- Mass (Da)19,760
- Last updated1986-07-21 v1
- ChecksumDB312BCCAAF659CE
Keywords
- Technical term