P27797 · CALR_HUMAN
- ProteinCalreticulin
- GeneCALR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids417 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:7876246).
Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926).
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).
Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926).
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).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 62 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 64 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 109 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 111 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 128 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 135 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 317 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 328 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCalreticulin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP27797
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038).
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).
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).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 440 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue, disulfide bond, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-17 | UniProt | |||||
Sequence: MLLSVPLLLGLLGLAVA | |||||||
Chain | PRO_0000004173 | 18-417 | UniProt | Calreticulin | |||
Sequence: EPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | |||||||
Modified residue | 48 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 64 | UniProt | N6-(2-hydroxyisobutyryl)lysine | ||||
Sequence: K | |||||||
Disulfide bond | 105↔137 | UniProt | |||||
Sequence: CGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDIC | |||||||
Modified residue | 159 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 209 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Glycosylation | 344 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and SPACA9 (By similarity).
Interacts with TRIM21 (PubMed:8666824).
Interacts with NR3C1 (PubMed:11149926).
Interacts with PPIB (PubMed:20801878).
Interacts (via P-domain) with PDIA5 (PubMed:23614004).
Interacts with GABARAP (PubMed:19154346).
Interacts with HLA-E-B2M and HLA-G-B2M complexes (PubMed:9427624, PubMed:9640257).
Interacts with HLA-F (PubMed:10605026).
Interacts with CLCC1 (PubMed:30157172).
Interacts with TRIM21 (PubMed:8666824).
Interacts with NR3C1 (PubMed:11149926).
Interacts with PPIB (PubMed:20801878).
Interacts (via P-domain) with PDIA5 (PubMed:23614004).
Interacts with GABARAP (PubMed:19154346).
Interacts with HLA-E-B2M and HLA-G-B2M complexes (PubMed:9427624, PubMed:9640257).
Interacts with HLA-F (PubMed:10605026).
Interacts with CLCC1 (PubMed:30157172).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 18-197 | N-domain | ||||
Sequence: EPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLE | ||||||
Repeat | 191-202 | 1-1 | ||||
Sequence: VESGSLEDDWDF | ||||||
Region | 191-255 | 4 X approximate repeats | ||||
Sequence: VESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDE | ||||||
Region | 193-278 | Disordered | ||||
Sequence: SGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPR | ||||||
Region | 198-308 | P-domain | ||||
Sequence: DDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAY | ||||||
Compositional bias | 199-254 | Basic and acidic residues | ||||
Sequence: DWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWD | ||||||
Repeat | 210-221 | 1-2 | ||||
Sequence: DPDASKPEDWDE | ||||||
Repeat | 227-238 | 1-3 | ||||
Sequence: DPTDSKPEDWDK | ||||||
Region | 237-270 | Interaction with PPIB | ||||
Sequence: DKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPE | ||||||
Repeat | 244-255 | 1-4 | ||||
Sequence: DPDAKKPEDWDE | ||||||
Repeat | 259-269 | 2-1 | ||||
Sequence: GEWEPPVIQNP | ||||||
Region | 259-297 | 3 X approximate repeats | ||||
Sequence: GEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNP | ||||||
Repeat | 273-283 | 2-2 | ||||
Sequence: GEWKPRQIDNP | ||||||
Repeat | 287-297 | 2-3 | ||||
Sequence: GTWIHPEIDNP | ||||||
Region | 309-417 | C-domain | ||||
Sequence: DNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | ||||||
Region | 350-417 | Disordered | ||||
Sequence: TKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | ||||||
Compositional bias | 352-381 | Basic and acidic residues | ||||
Sequence: AAEKQMKDKQDEEQRLKEEEEDKKRKEEEE | ||||||
Compositional bias | 382-417 | Acidic residues | ||||
Sequence: AEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL | ||||||
Motif | 414-417 | Prevents secretion from ER | ||||
Sequence: KDEL |
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.
The interaction with glycans occurs through a binding site in the globular lectin domain.
The zinc binding sites are localized to the N-domain.
Associates with PDIA3 through the tip of the extended arm formed by the P-domain.
Sequence similarities
Belongs to the calreticulin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length417
- Mass (Da)48,142
- Last updated1992-08-01 v1
- ChecksumBC37C3C0F1054FB2
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7EJB9 | K7EJB9_HUMAN | CALR | 349 | ||
A0A7P0T861 | A0A7P0T861_HUMAN | CALR | 356 | ||
K7ELE2 | K7ELE2_HUMAN | CALR | 13 | ||
K7EL50 | K7EL50_HUMAN | CALR | 378 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 199-254 | Basic and acidic residues | ||||
Sequence: DWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWD | ||||||
Compositional bias | 352-381 | Basic and acidic residues | ||||
Sequence: AAEKQMKDKQDEEQRLKEEEEDKKRKEEEE | ||||||
Compositional bias | 382-417 | Acidic residues | ||||
Sequence: AEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M32294 EMBL· GenBank· DDBJ | AAA36582.1 EMBL· GenBank· DDBJ | mRNA | ||
M84739 EMBL· GenBank· DDBJ | AAA51916.1 EMBL· GenBank· DDBJ | mRNA | ||
AY047586 EMBL· GenBank· DDBJ | AAL13126.1 EMBL· GenBank· DDBJ | mRNA | ||
AB451408 EMBL· GenBank· DDBJ | BAG70222.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007448 EMBL· GenBank· DDBJ | AAP36116.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457070 EMBL· GenBank· DDBJ | CAG33351.1 EMBL· GenBank· DDBJ | mRNA | ||
AD000092 EMBL· GenBank· DDBJ | AAB51176.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471106 EMBL· GenBank· DDBJ | EAW84331.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002500 EMBL· GenBank· DDBJ | AAH02500.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007911 EMBL· GenBank· DDBJ | AAH07911.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020493 EMBL· GenBank· DDBJ | AAH20493.1 EMBL· GenBank· DDBJ | mRNA |