Search results for CALR

Showing 15 results out of 16

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Types

Compartments

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Protein (5 results from a total of 6)

Identifier: R-HSA-195905
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Primary external reference: UniProt: CALR: P27797
Identifier: R-HSA-985502
Species: Homo sapiens
Compartment: integral component of lumenal side of endoplasmic reticulum membrane
Primary external reference: UniProt: CALR: P27797
Identifier: R-HSA-2197641
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: CALR: P27797
Identifier: R-HSA-8863866
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane
Primary external reference: UniProt: P27797
Identifier: R-HSA-1236879
Species: Homo sapiens
Compartment: phagocytic vesicle membrane
Primary external reference: UniProt: P27797

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-5642250
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000179218

Set (1 results from a total of 1)

Identifier: R-HSA-901048
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen

Reaction (4 results from a total of 4)

Identifier: R-HSA-8951595
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane, phagocytic vesicle membrane
The interaction between the two compartments involves either direct fusion of ER stacks to phagosomes (Phgs) or vesicular intermediates. In both cases, a fusion event between the ER or ER-derived membrane vesicles and Phgs must occur. The SNARE SEC22B localizes to the ER-Golgi intermediate compartment (ERGIC) and interacts with SNARE syntaxin 4 (STX4) on phagosomes (Phgs), mediating the recruitment of subset of ER components including transporter associated with antigen processing (TAP), to phagosomes (Cebrian et al. 2011).
Identifier: R-HSA-8863858
Species: Homo sapiens
Compartment: endoplasmic reticulum-Golgi intermediate compartment membrane, phagocytic vesicle membrane
The interaction between the two compartments could involve either direct fusion of ER stacks to phagosomes (Phgs) or vesicular intermediates. In both cases, a fusion event between the ER or ER-derived membrane vesicles and Phgs must occur. The SNARE SEC22B localizes to the ER-Golgi intermediate compartment (ERGIC) and interacts with SNARE syntaxin 4 (STX4) on phagosomes (Phgs), mediating the recruitment of subset of ER components including transporter associated with antigen processing (TAP), to phagosomes (Cebrian et al. 2011).
Identifier: R-HSA-1791082
Species: Homo sapiens
Compartment: nucleoplasm, endoplasmic reticulum lumen
The Calreticulin gene is transcribed to yield mRNA and the mRNA is translated to yield protein.
Identifier: R-HSA-535717
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Calnexin (membrane protein) and calreticulin (soluble in ER) are two lectins (proteins that can bind a glycan) which recognize the mono-glucosylated form of the N-glycan and mediate the folding of the glycoproteins to which they are attached to (Ou WJ et al, 1993; Nauseef Wm et al, 1995). Calmegin is another chaperone with the same role expressed only in testis (van Lith M et al, 2007). These lectins act as chaperons, providing a protected environment where the unfolded glycoprotein can fold without forming interactions with other proteins or components in the ER. The unfolded protein can loop between these two steps multiple time, therefore this process is called the 'calnexin/calreticulin cycle'. If the protein achieves correct folding, it is modified by Mannosidase I and then moved to the cis-Golgi where the glycan is further processed.

Complex (2 results from a total of 2)

Identifier: R-HSA-548862
Species: Homo sapiens
Compartment: endoplasmic reticulum lumen
Identifier: R-HSA-8951594
Species: Homo sapiens
Compartment: phagocytic vesicle membrane

Pathway (2 results from a total of 2)

Identifier: R-HSA-901042
Species: Homo sapiens
The unfolded protein is recognized by a chaperon protein (calnexin or calreticulin) and the folding process starts. The binding of these protein requires a mono-glucosylated glycan (Caramelo JJ and Parodi AJ, 2008), but in certain cases can occur even in the absence of glycosylation (Ireland BS et al, 2008).
Identifier: R-HSA-532668
Species: Homo sapiens
After being synthesized in the ER membrane the 14-sugars lipid-linked oligosaccharide is co-translationally transferred to an unfolded protein, as described in the previous steps. After this point the N-glycan is progressively trimmed of the three glucoses and some of the mannoses before the protein is transported to the cis-Golgi. The role of these trimming reactions is that the N-glycan attached to an unfolded glycoprotein in the ER assume the role of 'tags' that direct the interactions of the glycoprotein with different elements that mediate its folding. The removal of the two outer glucoses leads to an N-glycan with only one glucose, which is a signal for the binding of either one of two chaperone proteins, calnexin (CNX) and calreticulin (CRT). These chaperones provide an environment where the protein can fold more easily. The interaction with these proteins is not transient and is terminated by the trimming of the last remaining glucose, after which the glycoprotein is released from CNX or CRT and directed to the ER Quality Control compartment (ERQC) if it still has folding defects, or transported to the Golgi if the folding is correct. The involvement of N-glycans in the folding quality control of proteins in the ER explains why this form of glycosylation is so important, and why defects in the enzymes involved in these reactions are frequently associated with congenital diseases. However, there are many unknown points in this process, as it is known that even proteins without N-glycosylation sites can be folded properly (Caramelo JJ and Parodi AJ, 2008).
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