Q9XF98 · CALR_PRUAR
- ProteinCalreticulin
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 114 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 116 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 133 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 140 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | calcium ion binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | unfolded protein binding | |
Biological Process | protein folding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCalreticulin
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus
Accessions
- Primary accessionQ9XF98
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MAFRVPNSSLLSLILLSLLAIA | ||||||
Chain | PRO_0000004194 | 23-421 | Calreticulin | |||
Sequence: SAKVFFEERFEDGWDKRWVTSEWKKDENLAGEWNYTSGKWNGDPNDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYIKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILNYNNTNNLIKKDVPCETDQLTHVYTFIIRPDATYSILIDNLEKQTGSLYSDWDLLPAKKIKDPEAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGEWKPKKIKNPNFKGKWKAPLIDNPEFKDDPELYVYPNLKYVGIELWQVKSGTLFDNILITDEPEYAKQLAEETWGKQKDAEKAAFEELEKKLQEEESKEDPVDSDAEDDDNEAEDGEESDSESKPDSTEESAETEAEKHDEL | ||||||
Glycosylation | 56 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 110↔142 | |||||
Sequence: CGGGYIKLLSGDVDQKKFGGDTPYSIMFGPDIC | ||||||
Glycosylation | 156 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 196-207 | 1-1 | ||||
Sequence: KQTGSLYSDWDL | ||||||
Region | 196-261 | 4 X approximate repeats | ||||
Sequence: KQTGSLYSDWDLLPAKKIKDPEAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKKPEDWDD | ||||||
Repeat | 215-226 | 1-2 | ||||
Sequence: DPEAKKPEDWED | ||||||
Compositional bias | 217-255 | Basic and acidic residues | ||||
Sequence: EAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKK | ||||||
Region | 217-283 | Disordered | ||||
Sequence: EAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGEWKP | ||||||
Repeat | 232-243 | 1-3 | ||||
Sequence: DPEDKKPEGYDD | ||||||
Repeat | 250-261 | 1-4 | ||||
Sequence: DPDAKKPEDWDD | ||||||
Repeat | 265-275 | 2-1 | ||||
Sequence: GEWTAPTIPNP | ||||||
Region | 265-303 | 3 X approximate repeats | ||||
Sequence: GEWTAPTIPNPEYKGEWKPKKIKNPNFKGKWKAPLIDNP | ||||||
Repeat | 279-289 | 2-2 | ||||
Sequence: GEWKPKKIKNP | ||||||
Repeat | 293-303 | 2-3 | ||||
Sequence: GKWKAPLIDNP | ||||||
Compositional bias | 350-377 | Basic and acidic residues | ||||
Sequence: EETWGKQKDAEKAAFEELEKKLQEEESK | ||||||
Region | 350-421 | Disordered | ||||
Sequence: EETWGKQKDAEKAAFEELEKKLQEEESKEDPVDSDAEDDDNEAEDGEESDSESKPDSTEESAETEAEKHDEL | ||||||
Compositional bias | 378-403 | Acidic residues | ||||
Sequence: EDPVDSDAEDDDNEAEDGEESDSESK | ||||||
Compositional bias | 404-421 | Basic and acidic residues | ||||
Sequence: PDSTEESAETEAEKHDEL | ||||||
Motif | 418-421 | Prevents secretion from ER | ||||
Sequence: HDEL |
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).
The interaction with glycans occurs through a binding site in the globular lectin domain.
The zinc binding sites are localized to the N-domain.
Sequence similarities
Belongs to the calreticulin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length421
- Mass (Da)48,416
- Last updated1999-11-01 v1
- Checksum4F5F94CBAA6C6690
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 217-255 | Basic and acidic residues | ||||
Sequence: EAKKPEDWEDQEYIPDPEDKKPEGYDDIPKEITDPDAKK | ||||||
Compositional bias | 350-377 | Basic and acidic residues | ||||
Sequence: EETWGKQKDAEKAAFEELEKKLQEEESK | ||||||
Compositional bias | 378-403 | Acidic residues | ||||
Sequence: EDPVDSDAEDDDNEAEDGEESDSESK | ||||||
Compositional bias | 404-421 | Basic and acidic residues | ||||
Sequence: PDSTEESAETEAEKHDEL |