P68285 · CRYAA_HIPAM

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.

117320406080100120140160
TypeIDPosition(s)Description
Binding site100Zn2+ 1 (UniProtKB | ChEBI)
Binding site102Zn2+ 1 (UniProtKB | ChEBI)
Binding site107Zn2+ 2 (UniProtKB | ChEBI)
Binding site154Zn2+ 3 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionstructural constituent of eye lens
Molecular Functionunfolded protein binding
Biological Processlens development in camera-type eye
Biological Processnegative regulation of apoptotic process
Biological Processprotein refolding
Biological Processresponse to heat

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-crystallin A chain

Gene names

    • Name
      CRYAA

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Whippomorpha > Ancodonta > Hippopotamidae > Hippopotamus

Accessions

  • Primary accession
    P68285
  • Secondary accessions
    • P02471

Subcellular Location

Cytoplasm
Nucleus
Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.

Keywords

PTM/Processing

Features

Showing features for modified residue, chain, glycosylation.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00001258631-173Alpha-crystallin A chain
Modified residue6Deamidated glutamine; partial
Modified residue45Phosphoserine
Modified residue50Deamidated glutamine; partial
Modified residue70N6-acetyllysine
Modified residue90Deamidated glutamine; partial
Modified residue99N6-acetyllysine
Modified residue101Deamidated asparagine; partial
Modified residue122Phosphoserine
Modified residue123Deamidated asparagine; partial
Glycosylation162O-linked (GlcNAc) serine

Post-translational modification

Acetylation at Lys-70 may increase chaperone activity.
Undergoes age-dependent proteolytical cleavage at the C-terminus.

Keywords

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).

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-63Required for complex formation with BFSP1 and BFSP2
Domain52-162sHSP
Region144-173Disordered

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    173
  • Mass (Da)
    19,760
  • Last updated
    1986-07-21 v1
  • Checksum
    DB312BCCAAF659CE
MDIAIQHPWFKRALGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAIPVSREEKPSSAPSS

Keywords

Sequence databases

Similar Proteins

Disclaimer

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