CRYGA
Gamma-crystallin A
Also known as: CRGA_HUMAN, CRY-g-A, CRYG1, CRYG5
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P11844
- Gene
- CRYGA
- Ensembl
- ENSG00000168582
- Chromosome
- 2
- Canonical length
- 174 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Vesicles,Cytosol
OverviewNCBI Gene
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
174 residues, UniProt reviewed canonical sequence.
>P11844|CRYGA
1 MGKITFYEDR DFQGRCYNCI SDCPNLRVYF SRCNSIRVDS GCWMLYERPN YQGHQYFLRR
61 GKYPDYQHWM GLSDSVQSCR IIPHTSSHKL RLYERDDYRG LMSELTDDCA CVPELFRLPE
121 IYSLHVLEGC WVLYEMPNYR GRQYLLRPGD YRRYHDWGGA DAKVGSLRRV TDLYLocalizationUniProt · AlphaFold · HPA
Whether an antibody against CRYGA can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Unknown
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.25
- Highest tissue expression
- 0.4 nTPM
Expression across tissuesHPA
Tissue
- basal ganglia: 0.4 nTPM
- cerebral cortex: 0.3 nTPM
- amygdala: 0.2 nTPM
- hippocampal formation: 0.2 nTPM
- hypothalamus: 0.2 nTPM
- choroid plexus: 0.1 nTPM
Single-cell type
- megakaryocyte progenitors: 3.6 nCPM
- oligodendrocyte progenitor cells: 1.3 nCPM
- brain inhibitory neurons: 0.7 nCPM
- brain excitatory neurons: 0.6 nCPM
- other brain neurons: 0.4 nCPM
- undifferentiated spermatogonia: 0.4 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebral cortex: 0.9 nTPM
- hypothalamus: 0.7 nTPM
- amygdala: 0.6 nTPM
- basal ganglia: 0.6 nTPM
- hippocampal formation: 0.5 nTPM
- midbrain: 0.3 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.82
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.65
- DepMap mean gene effect
- -0.04
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 2% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads CRYGA as an antibody target. Whether an autoantibody or antibody against CRYGA could matter depends on whether native CRYGA is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
CRYGA is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label CRYGA as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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