Detail Information for IndEnz0002005507
IED ID IndEnz0002005507
Enzyme Type ID protease005507
Protein Name Beta-crystallin B1
Beta-B1 crystallin

Cleaved into: Beta-crystallin B1B
Gene Name Crybb1
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MSQVAKAAATTAVNPGPDGKGKGTPSTGTAPAPGPTPVPASVPRPAAKVGELPPGSYRLVVFEQENFQGRRVEFSGECLNLGDRGFDRVRSLIVLSGPWVAFEQSAFRGEMFVLEKGEYPRWDTWTSSYRSDRLMSFRPIRMDSQEHKICLFEGANFKGNTMEIQEDDVPSLWVYGFCDRVGSITVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQAVRRLRDRQWHQEGCFPVLTAEPPK
Enzyme Length 250
Uniprot Accession Number P02523
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (2); Domain (4); Initiator methionine (1); Modified residue (1); Region (4); Sequence conflict (2)
Keywords Acetylation;Direct protein sequencing;Eye lens protein;Methylation;Reference proteome;Repeat
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000269|PubMed:11773034
Post Translational Modification PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 28,093
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda