UniProt functional annotation for P18418



	UniProt functional annotation for P18418

UniProt code: P18418.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity). {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.

Subunit: Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with GABARAP, NR3C1 and TRIM21. Interacts with PPIB and SPACA9. Interacts (via P-domain) with PDIA5 (By similarity). Interacts with PDIA3/ERp57 (PubMed:11842220). Interacts with CLCC1 (By similarity). {ECO:0000250|UniProtKB:P14211, ECO:0000250|UniProtKB:P27797, ECO:0000269|PubMed:11842220}.

Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12782144}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule {ECO:0000250|UniProtKB:P27797}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.

Tissue specificity: Predentin and odontoblast. {ECO:0000269|PubMed:12782144}.

Domain: Can be divided into a N-terminal globular domain, a proline- rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity). {ECO:0000250}.

Domain: The interaction with glycans occurs through a binding site in the globular lectin domain. {ECO:0000250}.

Domain: The zinc binding sites are localized to the N-domain. {ECO:0000250}.

Domain: Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

Similarity: Belongs to the calreticulin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity). {ECO:0000250\|UniProtKB:P27797, ECO:0000250\|UniProtKB:P28491, ECO:0000250\|UniProtKB:Q8K3H7}.


Subunit:		Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with GABARAP, NR3C1 and TRIM21. Interacts with PPIB and SPACA9. Interacts (via P-domain) with PDIA5 (By similarity). Interacts with PDIA3/ERp57 (PubMed:11842220). Interacts with CLCC1 (By similarity). {ECO:0000250\|UniProtKB:P14211, ECO:0000250\|UniProtKB:P27797, ECO:0000269\|PubMed:11842220}.
Subcellular location:		Endoplasmic reticulum lumen {ECO:0000269\|PubMed:12782144}. Cytoplasm, cytosol {ECO:0000250\|UniProtKB:P27797}. Secreted, extracellular space, extracellular matrix {ECO:0000250\|UniProtKB:P27797}. Cell surface {ECO:0000250\|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250\|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250\|UniProtKB:Q8K3H7}. Cytolytic granule {ECO:0000250\|UniProtKB:P27797}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250\|UniProtKB:P27797, ECO:0000250\|UniProtKB:P28491, ECO:0000250\|UniProtKB:Q8K3H7}.
Tissue specificity:		Predentin and odontoblast. {ECO:0000269\|PubMed:12782144}.
Domain:		Can be divided into a N-terminal globular domain, a proline- rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity). {ECO:0000250}.
Domain:		The interaction with glycans occurs through a binding site in the globular lectin domain. {ECO:0000250}.
Domain:		The zinc binding sites are localized to the N-domain. {ECO:0000250}.
Domain:		Associates with PDIA3 through the tip of the extended arm formed by the P-domain.
Similarity:		Belongs to the calreticulin family. {ECO:0000305}.