Q90497 · CRYAA_EUDEL

Function

function

Contributes to the transparency and refractive index of the lens. May act as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions.

Features

Showing features for binding site.

114920406080100120140
TypeIDPosition(s)Description
Binding site89Zn2+ 1 (UniProtKB | ChEBI)
Binding site91Zn2+ 1 (UniProtKB | ChEBI)
Binding site96Zn2+ 2 (UniProtKB | ChEBI)
Binding site143Zn2+ 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 > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Palaeognathae > Tinamiformes > Tinamidae > Eudromia

Accessions

  • Primary accession
    Q90497

Subcellular Location

Cytoplasm
Nucleus
Note: Translocates to the nucleus during heat shock.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001258951-149Alpha-crystallin A chain

Interaction

Subunit

Heteropolymer composed of three CRYAA and one CRYAB subunits (By similarity).
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-89 and Glu-91 from one molecule are ligands of the zinc ion, and His-96 and His-143 residues from additional molecules complete the site with tetrahedral coordination geometry (By similarity).

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-149sHSP

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    149
  • Mass (Da)
    17,078
  • Last updated
    1996-11-01 v1
  • Checksum
    E444A52044D13E62
RALGPLIPSRLFDQFFGEGLLEYDLLPLFSSTISPYYRQSLFRSVLESGISEVRSDREKFTIMLDVKHFSPEDLSVKIIDDFVEIHGKHSERQDDHGYISREFHRRYRLPSNVDQSAITCSLSSDGMLTFSGPKVQANMDPSHSERPIP

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue149

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L25850
EMBL· GenBank· DDBJ
AAA49254.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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