P02525 · CRBA1_MOUSE
- ProteinBeta-crystallin A1
- GeneCryba1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids198 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Crystallins are the dominant structural components of the vertebrate eye lens.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | identical protein binding | |
Molecular Function | structural constituent of eye lens | |
Biological Process | camera-type eye development | |
Biological Process | lens development in camera-type eye | |
Biological Process | negative regulation of cytokine production | |
Biological Process | negative regulation of ERK1 and ERK2 cascade | |
Biological Process | negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | |
Biological Process | negative regulation of TOR signaling | |
Biological Process | phagocytosis | |
Biological Process | positive regulation of anoikis | |
Biological Process | regulation of autophagy | |
Biological Process | visual perception |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameBeta-crystallin A1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP02525
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057534 | 1-198 | Beta-crystallin A1 | |||
Sequence: MLYLVLFLVPFNSIQITIYDQENFQGKRMEFTSSCPNVSERNFDNVRSLKVECGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKITIFEKENFIGRQWEICDDYPSLQAMGWFNNEVGSMKIQCGAWVCYQYPGYRGYQYILECDHHGGDYKHWPEWGSHAQTSQIQSIRRIQQ | ||||||
Modified residue | 65 | S-glutathionyl cysteine; alternate | ||||
Sequence: C | ||||||
Modified residue | 65 | S-methylcysteine; alternate | ||||
Sequence: C | ||||||
Modified residue | 100 | S-glutathionyl cysteine; alternate | ||||
Sequence: C | ||||||
Modified residue | 100 | S-methylcysteine; alternate | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-13 | N-terminal arm | ||||
Sequence: MLYLVLFLVPFNS | ||||||
Domain | 14-53 | Beta/gamma crystallin 'Greek key' 1 | ||||
Sequence: IQITIYDQENFQGKRMEFTSSCPNVSERNFDNVRSLKVEC | ||||||
Domain | 54-100 | Beta/gamma crystallin 'Greek key' 2 | ||||
Sequence: GAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPIC | ||||||
Region | 101-106 | Connecting peptide | ||||
Sequence: SANHKE | ||||||
Domain | 107-148 | Beta/gamma crystallin 'Greek key' 3 | ||||
Sequence: SKITIFEKENFIGRQWEICDDYPSLQAMGWFNNEVGSMKIQC | ||||||
Domain | 149-197 | Beta/gamma crystallin 'Greek key' 4 | ||||
Sequence: GAWVCYQYPGYRGYQYILECDHHGGDYKHWPEWGSHAQTSQIQSIRRIQ |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)23,401
- Last updated2012-10-03 v2
- ChecksumF7EBDD750402FEC5
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q9QXC6 | Q9QXC6_MOUSE | Cryba1 | 215 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 111 | in Ref. 3; CAA24106/AAA51629 | ||||
Sequence: I → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL591136 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
V00729 EMBL· GenBank· DDBJ | CAA24107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
V00728 EMBL· GenBank· DDBJ | CAA24106.1 EMBL· GenBank· DDBJ | mRNA | ||
J00378 EMBL· GenBank· DDBJ | AAA51629.1 EMBL· GenBank· DDBJ | mRNA |