P29413 · CALR_DROME
- ProteinCalreticulin
- GeneCalr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids406 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | 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 |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endomembrane system | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | extracellular space | |
Cellular Component | fusome | |
Molecular Function | calcium ion binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | unfolded protein binding | |
Biological Process | ERAD pathway | |
Biological Process | olfactory behavior | |
Biological Process | protein folding | |
Biological Process | sleep |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCalreticulin
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP29413
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MMWCKTVIVLLATVGFI | ||||||
Chain | PRO_0000004182 | 18-406 | Calreticulin | |||
Sequence: SAEVYLKENFDNENWEDTWIYSKHPGKEFGKFVLTPGTFYNDAEADKGIQTSQDARFYAASRKFDGFSNEDKPLVVQFSVKHEQNIDCGGGYVKLFDCSLDQTDMHGESPYEIMFGPDICGPGTKKVHVIFSYKGKNHLISKDIRCKDDVYTHFYTLIVRPDNTYEVLIDNEKVESGNLEDDWDFLAPKKIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDATKPEDWDDEMDGEWEPPMIDNPEFKGEWQPKQLDNPNYKGAWEHPEIANPEYVPDDKLYLRKEICTLGFDLWQVKSGTIFDNVLITDDVELAAKAAAEVKNTQAGEKKMKEAQDEVQRKKDEEEAKKASDKDDEDEDDDDEEKDDESKQDKDQSEHDEL | ||||||
Disulfide bond | 105↔137 | |||||
Sequence: CGGGYVKLFDCSLDQTDMHGESPYEIMFGPDIC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 191-202 | 1-1 | ||||
Sequence: VESGNLEDDWDF | ||||||
Region | 191-255 | 4 X approximate repeats | ||||
Sequence: VESGNLEDDWDFLAPKKIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDATKPEDWDD | ||||||
Compositional bias | 207-248 | Basic and acidic residues | ||||
Sequence: KIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDAT | ||||||
Region | 207-259 | Disordered | ||||
Sequence: KIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDATKPEDWDDEMDG | ||||||
Repeat | 210-221 | 1-2 | ||||
Sequence: DPTATKPEDWDD | ||||||
Repeat | 227-238 | 1-3 | ||||
Sequence: DPDDKKPEDWDK | ||||||
Repeat | 244-255 | 1-4 | ||||
Sequence: DPDATKPEDWDD | ||||||
Repeat | 259-269 | 2-1 | ||||
Sequence: GEWEPPMIDNP | ||||||
Region | 259-297 | 3 X approximate repeats | ||||
Sequence: GEWEPPMIDNPEFKGEWQPKQLDNPNYKGAWEHPEIANP | ||||||
Repeat | 273-283 | 2-2 | ||||
Sequence: GEWQPKQLDNP | ||||||
Repeat | 287-297 | 2-3 | ||||
Sequence: GAWEHPEIANP | ||||||
Region | 347-406 | Disordered | ||||
Sequence: KNTQAGEKKMKEAQDEVQRKKDEEEAKKASDKDDEDEDDDDEEKDDESKQDKDQSEHDEL | ||||||
Compositional bias | 348-374 | Basic and acidic residues | ||||
Sequence: NTQAGEKKMKEAQDEVQRKKDEEEAKK | ||||||
Compositional bias | 375-393 | Acidic residues | ||||
Sequence: ASDKDDEDEDDDDEEKDDE |
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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length406
- Mass (Da)46,808
- Last updated1993-10-01 v2
- Checksum65D72C69D0BEC427
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q53YH3 | Q53YH3_DROME | Calr | 406 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 107 | in Ref. 4; AA sequence | ||||
Sequence: G → A | ||||||
Sequence conflict | 184 | in Ref. 4; AA sequence | ||||
Sequence: V → L | ||||||
Compositional bias | 207-248 | Basic and acidic residues | ||||
Sequence: KIKDPTATKPEDWDDRATIPDPDDKKPEDWDKPEHIPDPDAT | ||||||
Compositional bias | 348-374 | Basic and acidic residues | ||||
Sequence: NTQAGEKKMKEAQDEVQRKKDEEEAKK | ||||||
Compositional bias | 375-393 | Acidic residues | ||||
Sequence: ASDKDDEDEDDDDEEKDDE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X64461 EMBL· GenBank· DDBJ | CAA45791.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF54416.1 EMBL· GenBank· DDBJ | Genomic DNA |