Cryaa crystallin, alpha A [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Cryaaprovided by MGI
Official Full Name: crystallin, alpha Aprovided by MGI
Primary source: MGI:MGI:88515
See related: Ensembl:ENSMUSG00000024041 AllianceGenome:MGI:88515
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Crya1; lop18; Acry-1; Crya-1; DAcry-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 (sHSP) 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. In mouse, deficiency in this gene is associated with smaller lenses and eyes and with increasing lens opacity with age. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Expression: Biased expression in placenta adult (RPKM 1.1), lung adult (RPKM 1.0) and 8 other tissues See more
Orthologs: human all
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Genomic context

Location:: 17 B1; 17 17.09 cM

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	17	NC_000083.7 (31896905..31900704)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	17	NC_000083.6 (31677931..31681730)

Chromosome 17 - NC_000083.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.
Title: Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.
We show that many crystallins are upregulated in a murine model of RD and that alphaA-crystallin shows the highest level of expression both on the transcriptional and translational levels. We further found a significant upregulation of alphaA-crystallin in vitreous samples of human pseudophakic RD patients
Title: Significant upregulation of small heat shock protein αA-crystallin in retinal detachment.
alpha-Crystallin isolated from SIRT3 and SIRT5 KO lenses displayed a higher surface hydrophobicity and higher chaperone activity than the protein isolated from WT lenses. Thus, SIRTs regulate the acetylation levels of crystallins in mouse lenses, and acetylation in lenses enhances the chaperone activity of alpha-crystallin.
Title: The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of α-crystallin in mouse lenses.
Study using mouse streptozotocin diabetes model demonstrated the neuroprotective role of alphaA-crystallin during diabetes and its regulation by its phosphorylation on residue 148 and further characterized the dual role of alphaA-crystallin in neurons and glia, its essential role for neuronal survival, and its direct dependence on phosphorylation on this residue.
Title: A specific phosphorylation regulates the protective role of αA-crystallin in diabetes.
findings offer additional insight into the early transcriptional changes caused by Cryaa and Cryab mutations associated with autosomal dominant cataracts, and indicate that the transcript levels of certain genes are affected by the expression of mutant alpha-crystallin in vivo
Title: Probing the changes in gene expression due to α-crystallin mutations in mouse models of hereditary human cataract.
Collectively, these studies show that FGF signaling up-regulates expression of alphaA-crystallin both directly and indirectly via up-regulation of c-Maf.
Title: Regulation of c-Maf and αA-Crystallin in Ocular Lens by Fibroblast Growth Factor Signaling.
Knockout of alphaA-crystallin inhibited pathologic neovascularization through the VEGF and VEGFR2 signaling pathways both in vitro and in vivo.
Title: Knockout of αA-crystallin inhibits ocular neovascularization.
the expression of alphaAN101D transgene results in disruption of lens morphogenesis, which is characterized by defective LEC proliferation, elongation, and lens fiber cell denucleation.
Title: Molecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice.
p53 can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.
Title: p53 directly regulates αA- and βA3/A1-crystallin genes to modulate lens differentiation.
Alpha A crystallin is a moonlighting protein that functions as a heat shock protein as well as a lens crystalline.
Title: Gene sharing in lens and cornea: facts and implications.

Submit: New GeneRIF Correction See all GeneRIFs (29)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Chemically induced (ENU) (2) 1 citation
Endonuclease-mediated (2) 1 citation
Spontaneous (2) 1 citation
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

UniSTS:259595 (e-PCR)
- UniSTS:259595

Cryaa (e-PCR), detects polymorphism
- UniSTS:259595

Cryaa (e-PCR), detects polymorphism
- UniSTS:234013

NoName (e-PCR)
- UniSTS:548146

D17Rua3 (e-PCR), detects polymorphism
- UniSTS:142162

AI323437 (e-PCR)
- UniSTS:160636

J00376 (e-PCR)
- UniSTS:124848

Cryaa (e-PCR), detects polymorphism
- UniSTS:231399

Cryaa (e-PCR), detects polymorphism
- UniSTS:259061

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of eye lens	TAS Traceable Author Statement more info	PubMed
enables structural molecule activity	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within actin filament organization	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within apoptotic process involved in morphogenesis	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within camera-type eye development	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within embryonic camera-type eye morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in lens development in camera-type eye	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within lens development in camera-type eye	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within lens development in camera-type eye	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within lens fiber cell morphogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within lens morphogenesis in camera-type eye	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within microtubule-based process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within mitochondrion organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of apoptotic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within negative regulation of apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of cysteine-type endopeptidase activity	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within negative regulation of gene expression	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of intracellular transport	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of cell growth	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within positive regulation of protein phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	ISO Inferred from Sequence Orthology more info
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to UV-A	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to heat	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within response to hydrogen peroxide	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to hydrogen peroxide	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within response to hypoxia	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within tubulin complex assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in visual perception	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: alpha-crystallin A chain

Names: crystallin, alpha 1; lens opacity 18

NCBI Reference Sequences (RefSeq)

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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)

NM_001278569.1 → NP_001265498.1 alpha-crystallin A chain isoform 1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).

Source sequence(s)

BB371615, BY114969, CA452236, CX734348, EL605017

Consensus CDS

CCDS89060.1

UniProtKB/TrEMBL

A0A494B9Q6

Related

ENSMUSP00000157708.2, ENSMUST00000228089.3

Conserved Domains (3) summary

COG0071
Location:93 → 174

IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]

pfam00525
Location:1 → 50

Crystallin; Alpha crystallin A chain, N terminal

cl00175
Location:90 → 174

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.
NM_001278570.1 → NP_001265499.1 alpha-crystallin A chain isoform 3

See identical proteins and their annotated locations for NP_001265499.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an alternate in-frame exon in the coding region compared to variant 1. It encodes isoform 3 which is shorter compared to isoform 1.

Source sequence(s)

AK143463, BB371615, EL604937

Consensus CDS

CCDS89061.1

UniProtKB/TrEMBL

Q569M7

Related

ENSMUSP00000154747.2, ENSMUST00000228716.3

Conserved Domains (2) summary

cd06497
Location:60 → 145

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 ...

pfam00525
Location:1 → 51

Crystallin; Alpha crystallin A chain, N terminal
NM_013501.3 → NP_038529.1 alpha-crystallin A chain isoform 2

See identical proteins and their annotated locations for NP_038529.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) uses an alternate in-frame splice site in the coding region compared to variant 1. It encodes isoform 2, also known as alpha-A-ins, which is shorter compared to isoform 1.

Source sequence(s)

BB371615, BC085170, EL605017

Consensus CDS

CCDS37551.1

UniProtKB/Swiss-Prot

P24622, Q6LEL4

UniProtKB/TrEMBL

Q546L9

Related

ENSMUSP00000019192.6, ENSMUST00000019192.8

Conserved Domains (3) summary

COG0071
Location:84 → 168

IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]

pfam00525
Location:1 → 50

Crystallin; Alpha crystallin A chain, N terminal

cl00175
Location:86 → 168

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.