calreticulin-3 (calreticulin-2, CALR3, CRT2)

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 a) 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 b) proline-rich P-domain forming an elongated arm-like structure - binds one Ca⁺² with high affinity c) C-terminal acidic domain - binds multiple Ca⁺² with low affinity Compartment: endoplasmic reticulum lumen Expression: testis specific

General

Ca+2 binding protein lectin testis-specific protein

Properties

SIZE: MW = 45 kD entity length = 384 aa COMPARTMENT: endoplasmic reticulum MOTIF: signal sequence {1-19} N-domain {20-197} MOTIF: N-glycosylation site {N42} cysteine residue {C105} MODIFICATION: cysteine residue {C137} cysteine residue {C137} MODIFICATION: cysteine residue {C105} consensus repeat {191-202} P-domain {198-294} MOTIF: N-glycosylation site {N201} consensus repeat {208-219} consensus repeat {221-230} consensus repeat {234-245} consensus repeat {249-259} consensus repeat {263-271} consensus repeat {273-283} C-domain {295-384} MOTIF: lysine-rich region {337-362} MOTIF: lysine residue (SEVERAL) Prevents secretion from ER {381-384}

Database Correlations

UniProt Q96L12 Pfam PF00262

References

UniProt :accession Q96L12