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Cryaa crystallin, alpha A [ Rattus norvegicus (Norway rat) ]

Gene ID: 24273, updated on 8-May-2016
Official Symbol
Cryaaprovided by RGD
Official Full Name
crystallin, alpha Aprovided by RGD
Primary source
RGD:2413
See related
Ensembl:ENSRNOG00000047175
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Rattus norvegicus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus
Also known as
Crya1; Acry-1
Summary
This gene encodes subunit a, one of two subunits of alpha-crystallin, which is a high molecular weight, soluble aggregate and is a member of the small heat shock protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. It acts as a molecular chaperone and is the major protein in the eye lens, maintaining the transparency and refractive index of the lens. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Orthologs
Location:
chromosome: 20
Exon count:
4
Annotation release Status Assembly Chr Location
105 current Rnor_6.0 (GCF_000001895.5) 20 NC_005119.4 (10438037..10442189)
104 previous assembly Rnor_5.0 (GCF_000001895.4) 20 NC_005119.3 (12621549..12625628)

Chromosome 20 - NC_005119.4Genomic Context describing neighboring genes Neighboring gene cystathionine beta synthase Neighboring gene U2 small nuclear RNA auxiliary factor 1 Neighboring gene uncharacterized LOC103694395 Neighboring gene similar to Eukaryotic translation initiation factor 3 subunit 2 (eIF-3 beta) (eIF3 p36) (eIF3i) (TGF-beta receptor-interacting protein 1) (TRIP-1)

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

  • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Gene Ontology Provided by RGD

Function Evidence Code Pubs
identical protein binding IDA
Inferred from Direct Assay
more info
PubMed 
identical protein binding ISO
Inferred from Sequence Orthology
more info
 
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
structural constituent of eye lens TAS
Traceable Author Statement
more info
PubMed 
unfolded protein binding ISO
Inferred from Sequence Orthology
more info
 
Process Evidence Code Pubs
actin filament organization IEA
Inferred from Electronic Annotation
more info
 
actin filament organization ISO
Inferred from Sequence Orthology
more info
 
apoptotic process ISO
Inferred from Sequence Orthology
more info
 
apoptotic process involved in morphogenesis IEA
Inferred from Electronic Annotation
more info
 
apoptotic process involved in morphogenesis ISO
Inferred from Sequence Orthology
more info
 
camera-type eye development ISO
Inferred from Sequence Orthology
more info
 
embryonic camera-type eye morphogenesis IEA
Inferred from Electronic Annotation
more info
 
embryonic camera-type eye morphogenesis ISO
Inferred from Sequence Orthology
more info
 
lens development in camera-type eye IEP
Inferred from Expression Pattern
more info
PubMed 
lens development in camera-type eye ISO
Inferred from Sequence Orthology
more info
 
lens fiber cell morphogenesis IEA
Inferred from Electronic Annotation
more info
 
lens fiber cell morphogenesis ISO
Inferred from Sequence Orthology
more info
 
lens morphogenesis in camera-type eye ISO
Inferred from Sequence Orthology
more info
 
microtubule-based process IEA
Inferred from Electronic Annotation
more info
 
microtubule-based process ISO
Inferred from Sequence Orthology
more info
 
mitochondrion organization IEA
Inferred from Electronic Annotation
more info
 
mitochondrion organization ISO
Inferred from Sequence Orthology
more info
 
negative regulation of apoptotic process ISO
Inferred from Sequence Orthology
more info
 
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process IEA
Inferred from Electronic Annotation
more info
 
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process ISO
Inferred from Sequence Orthology
more info
 
negative regulation of gene expression IEA
Inferred from Electronic Annotation
more info
 
negative regulation of gene expression ISO
Inferred from Sequence Orthology
more info
 
negative regulation of intracellular transport ISO
Inferred from Sequence Orthology
more info
 
positive regulation of cell growth IEA
Inferred from Electronic Annotation
more info
 
positive regulation of cell growth ISO
Inferred from Sequence Orthology
more info
 
positive regulation of protein phosphorylation IEA
Inferred from Electronic Annotation
more info
 
positive regulation of protein phosphorylation ISO
Inferred from Sequence Orthology
more info
 
protein folding IDA
Inferred from Direct Assay
more info
PubMed 
protein homooligomerization IDA
Inferred from Direct Assay
more info
PubMed 
protein homooligomerization ISO
Inferred from Sequence Orthology
more info
 
response to UV-A IEA
Inferred from Electronic Annotation
more info
 
response to UV-A ISO
Inferred from Sequence Orthology
more info
 
response to drug IEP
Inferred from Expression Pattern
more info
PubMed 
response to glucocorticoid IEP
Inferred from Expression Pattern
more info
PubMed 
response to hydrogen peroxide IDA
Inferred from Direct Assay
more info
PubMed 
response to hydrogen peroxide ISO
Inferred from Sequence Orthology
more info
 
response to hypoxia IEA
Inferred from Electronic Annotation
more info
 
response to hypoxia ISO
Inferred from Sequence Orthology
more info
 
response to lead ion IEP
Inferred from Expression Pattern
more info
PubMed 
tubulin complex assembly IEA
Inferred from Electronic Annotation
more info
 
tubulin complex assembly ISO
Inferred from Sequence Orthology
more info
 
visual perception ISO
Inferred from Sequence Orthology
more info
 
Component Evidence Code Pubs
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm ISO
Inferred from Sequence Orthology
more info
 
extracellular exosome ISO
Inferred from Sequence Orthology
more info
 
nucleus ISO
Inferred from Sequence Orthology
more info
 
nucleus ISS
Inferred from Sequence or Structural Similarity
more info
 
Preferred Names
alpha-crystallin A chain
Names
Crystallin, alpha polypeptide A

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001289737.1NP_001276666.1  alpha-crystallin A chain isoform 2

    See identical proteins and their annotated locations for NP_001276666.1

    Status: VALIDATED

    Description
    Transcript Variant: This variant (2) includes an alternate in-frame exon in the central coding region, compared to variant 1. The encoded isoform (2, also known as alpha Ains-crystallin) is longer, compared to isoform 1.
    Source sequence(s)
    U47921
    UniProtKB/Swiss-Prot
    P24623
    Related
    ENSRNOP00000065714, ENSRNOT00000075545
    Conserved Domains (3) summary
    COG0071
    Location:87168
    IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
    pfam00525
    Location:154
    Crystallin; Alpha crystallin A chain, N terminal
    cl00175
    Location:86168
    alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
  2. NM_012534.4NP_036666.2  alpha-crystallin A chain isoform 1

    See identical proteins and their annotated locations for NP_036666.2

    Status: VALIDATED

    Description
    Transcript Variant: This variant (1) encodes the shorter isoform (1).
    Source sequence(s)
    BC126082
    UniProtKB/Swiss-Prot
    P24623
    UniProtKB/TrEMBL
    A0JN13
    Related
    ENSRNOP00000067332, ENSRNOT00000071248
    Conserved Domains (3) summary
    cd06497
    Location:60145
    ACD_alphaA-crystallin_HspB4; Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers ...
    COG0071
    Location:63145
    IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
    pfam00525
    Location:154
    Crystallin; Alpha crystallin A chain, N terminal

RefSeqs of Annotated Genomes: Rattus norvegicus Annotation Release 105 details...

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Rnor_6.0 Primary Assembly

Genomic

  1. NC_005119.4 Reference Rnor_6.0 Primary Assembly

    Range
    10438037..10442189
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_008772796.1XP_008771018.1  

    Conserved Domains (3) summary
    COG0071
    Location:93174
    IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
    pfam00525
    Location:154
    Crystallin; Alpha crystallin A chain, N terminal
    cl00175
    Location:90174
    alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.

Alternate Rn_Celera

Genomic

  1. AC_000088.1 Alternate Rn_Celera

    Range
    11297259..11301004
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)