A4L9L5 · A4L9L5_CAVPO

Function

function

Crystallins are the dominant structural components of the vertebrate eye lens.

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
Molecular Functionstructural constituent of eye lens
Biological Processlens development in camera-type eye
Biological Processvisual perception

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Beta-crystallin B3
  • Alternative names
    • Beta-B3 crystallin

Gene names

    • Name
      Crybb3
    • Synonyms
      CRYBB3

Organism names

  • Taxonomic identifier
  • Strain
    • 2N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia

Accessions

  • Primary accession
    A4L9L5

Proteomes

Organism-specific databases

Expression

Gene expression databases

Interaction

Subunit

Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain24-63Beta/gamma crystallin 'Greek key'
Domain64-108Beta/gamma crystallin 'Greek key'
Domain114-155Beta/gamma crystallin 'Greek key'
Domain156-198Beta/gamma crystallin 'Greek key'

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    211
  • Mass (Da)
    23,981
  • Last updated
    2007-05-01 v1
  • Checksum
    0227AE13AE9DF840
MAEQHGAPEQAAAGKSHGGLGGGYKVTVYELENFQGKRCELSAECPNLTDGLLEKVGSIQVESGPWLAFERRAFRGEQFVLEKGDYPRWDAWSSSRHSDSLLSLRPLQVDGPDHKLHLFESPSFTGRKMEIVDDDVPSLWAHGFQDRVASVRAINGTWVGYEFPGYRGRQFAFERGEYRHWNEWAAGQPQLQSVRRVRDQKWHKRGCFLSS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A286XVE5A0A286XVE5_CAVPOCRYBB3118

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAKN02007338
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
EF457997
EMBL· GenBank· DDBJ
ABO39215.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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