P06504 · CRYGS_BOVIN
- ProteinGamma-crystallin S
- GeneCRYGS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids178 (go to sequence)
- Protein existenceEvidence at protein 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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Molecular Function | structural constituent of eye lens | |
Biological Process | lens development in camera-type eye | |
Biological Process | visual perception |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameGamma-crystallin S
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP06504
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000057564 | 2-178 | Gamma-crystallin S | |||
Sequence: SKAGTKITFFEDKNFQGRHYDSDCDCADFHMYLSRCNSIRVEGGTWAVYERPNFAGYMYILPRGEYPEYQHWMGLNDRLSSCRAVHLSSGGQYKLQIFEKGDFNGQMHETTEDCPSIMEQFHMREVHSCKVLEGAWIFYELPNYRGRQYLLDKKEYRKPVDWGAASPAVQSFRRIVE |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 2-5 | N-terminal arm | ||||
Sequence: SKAG | ||||||
Domain | 6-44 | Beta/gamma crystallin 'Greek key' 1 | ||||
Sequence: TKITFFEDKNFQGRHYDSDCDCADFHMYLSRCNSIRVEG | ||||||
Domain | 45-87 | Beta/gamma crystallin 'Greek key' 2 | ||||
Sequence: GTWAVYERPNFAGYMYILPRGEYPEYQHWMGLNDRLSSCRAVH | ||||||
Region | 88-93 | Connecting peptide | ||||
Sequence: LSSGGQ | ||||||
Domain | 94-134 | Beta/gamma crystallin 'Greek key' 3 | ||||
Sequence: YKLQIFEKGDFNGQMHETTEDCPSIMEQFHMREVHSCKVLE | ||||||
Domain | 135-177 | Beta/gamma crystallin 'Greek key' 4 | ||||
Sequence: GAWIFYELPNYRGRQYLLDKKEYRKPVDWGAASPAVQSFRRIV |
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
- Length178
- Mass (Da)20,928
- Last updated2007-01-23 v2
- Checksum03953B5627186F1D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X03006 EMBL· GenBank· DDBJ | CAA26791.1 EMBL· GenBank· DDBJ | mRNA | ||
M21095 EMBL· GenBank· DDBJ | AAA30477.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M21094 EMBL· GenBank· DDBJ | AAA30477.1 EMBL· GenBank· DDBJ | Genomic DNA |