calreticulin-3 (calreticulin-2, CALR3, CRT2)
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Function
- molecular Ca+2 binding chaperone
- promotes folding, oligomeric assembly & quality control in the endoplasmic reticulum via calreticulin/calnexin cycle
- may interact transiently with almost all monoglucosylated glycoproteins synthesized in the ER
Structure
- lectin
- belongs to the calreticulin family
- domains
- N-terminal globular domain
- interaction with glycans occurs through a binding site in the globular lectin domain
- Zn+2 binding sites are localized to the N-domain
- proline-rich P-domain forming an elongated arm-like structure - binds one Ca+2 with high affinity
- C-terminal acidic domain
- binds multiple Ca+2 with low affinity
- N-terminal globular domain
Compartment
Expression
testis specific