P04342 · CRGD_MOUSE

  • Protein
    Gamma-crystallin D
  • Gene
    Crygd
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

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

Miscellaneous

There are six different gamma crystallins identified in mouse 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
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionstructural constituent of eye lens
Biological Processeye development
Biological Processlens development in camera-type eye
Biological Processlens fiber cell differentiation
Biological Processvisual perception

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Gamma-crystallin D
  • Alternative names
    • Gamma-D-crystallin
    • Gamma-crystallin 1

Gene names

    • Name
      Crygd

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • 102 X C3H
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P04342
  • Secondary accessions
    • O89027
    • Q6PGI0

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000575981-174Gamma-crystallin D

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in the superior olivary complex of the auditory hindbrain.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain2-40Beta/gamma crystallin 'Greek key' 1
Domain41-83Beta/gamma crystallin 'Greek key' 2
Region84-87Connecting peptide
Domain88-128Beta/gamma crystallin 'Greek key' 3
Domain129-171Beta/gamma crystallin 'Greek key' 4

Domain

Has a two-domain beta-structure, folded into four very similar Greek key motifs.

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    174
  • Mass (Da)
    21,118
  • Last updated
    2012-10-03 v3
  • Checksum
    1AFC29C0269B35A1
MGKITFYEDRGFQGRHYECSTDHSNLQPYFSRCNSVRVDSGCWMLYEQPNFTGCQYFLRRGDYPDYQQWMGFSDSVRSCRLIPHAGSHRIRLYEREEYRGQMIEFTEDCPSLQDRFHFNEIYSLNVLEGCWVLYDMTNYRGRQYLLRPGEYRRYHDWGAMNARVGSLRRVMDFY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F7CUK9F7CUK9_MOUSECrygd110

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict32in Ref. 1; AAA37475
Sequence conflict52in Ref. 1; AAA37475 and 5; CAA11908
Sequence conflict102in Ref. 1; AAA37475 and 5; CAA11908
Sequence conflict163in Ref. 1; AAA37475

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
K02583
EMBL· GenBank· DDBJ
AAA37475.1
EMBL· GenBank· DDBJ
mRNA
AK136286
EMBL· GenBank· DDBJ
BAE22915.1
EMBL· GenBank· DDBJ
mRNA
AC158958
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC057013
EMBL· GenBank· DDBJ
AAH57013.1
EMBL· GenBank· DDBJ
mRNA
BC132116
EMBL· GenBank· DDBJ
AAI32117.1
EMBL· GenBank· DDBJ
mRNA
BC132118
EMBL· GenBank· DDBJ
AAI32119.1
EMBL· GenBank· DDBJ
mRNA
AJ224342
EMBL· GenBank· DDBJ
CAA11908.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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