Q40401 · CALR_NICPL
- ProteinCalreticulin
- GeneCAL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids416 (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 | 117 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 119 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 136 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 143 | an alpha-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 326 | 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 | |
Cellular Component | endoplasmic reticulum membrane | |
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
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Solanales > Solanaceae > Nicotianoideae > Nicotianeae > Nicotiana
Accessions
- Primary accessionQ40401
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MATQRRANPSSLHLITVFSLLVAVVSA | ||||||
Chain | PRO_0000004192 | 28-416 | Calreticulin | |||
Sequence: EVFFEESFNDGWESRWVKSEWKKDENMAGEWNHTSGKWNGDANDKGIQTSEDYRFYAISAEFPEFSNKGKNLVFQFSVKHEQKLDCGGGYMKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILTYNDTNHLIKKEVPCETDQLTHVYTFILRPDATYSILIDNVEKQSGSLYSDWDLLPPKTIKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKPKKIKNPNYKGKWKAPLIDNPDFKDDPDLYVFPKLKYVGVELWQVKSGTLFDNIVICDDPEYAKAIAEETWGKQKDAEKAAFEEAEKKREEEESKAAPADSDAEEDDDADDDSDDADDKSESKDDEAHDEL | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 113↔145 | |||||
Sequence: CGGGYMKLLSGDVDQKKFGGDTPYSIMFGPDIC | ||||||
Glycosylation | 159 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 199-210 | 1-1 | ||||
Sequence: KQSGSLYSDWDL | ||||||
Region | 199-264 | 4 X approximate repeats | ||||
Sequence: KQSGSLYSDWDLLPPKTIKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKKPEDWDD | ||||||
Region | 215-286 | Disordered | ||||
Sequence: TIKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKKPEDWDDEEDGEWTAPTIPNPEYKGPWKP | ||||||
Compositional bias | 216-258 | Basic and acidic residues | ||||
Sequence: IKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKK | ||||||
Repeat | 218-229 | 1-2 | ||||
Sequence: DPSAKKPEDWDE | ||||||
Repeat | 235-246 | 1-3 | ||||
Sequence: DPEDKKPEGYDD | ||||||
Repeat | 253-264 | 1-4 | ||||
Sequence: DPDAKKPEDWDD | ||||||
Repeat | 268-278 | 2-1 | ||||
Sequence: GEWTAPTIPNP | ||||||
Region | 268-306 | 3 X approximate repeats | ||||
Sequence: GEWTAPTIPNPEYKGPWKPKKIKNPNYKGKWKAPLIDNP | ||||||
Repeat | 282-292 | 2-2 | ||||
Sequence: GPWKPKKIKNP | ||||||
Repeat | 296-306 | 2-3 | ||||
Sequence: GKWKAPLIDNP | ||||||
Compositional bias | 355-381 | Basic and acidic residues | ||||
Sequence: TWGKQKDAEKAAFEEAEKKREEEESKA | ||||||
Region | 355-416 | Disordered | ||||
Sequence: TWGKQKDAEKAAFEEAEKKREEEESKAAPADSDAEEDDDADDDSDDADDKSESKDDEAHDEL | ||||||
Compositional bias | 382-405 | Acidic residues | ||||
Sequence: APADSDAEEDDDADDDSDDADDKS | ||||||
Motif | 413-416 | 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.
- Length416
- Mass (Da)47,481
- Last updated1996-11-01 v1
- Checksum5026F3152B8828C0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 216-258 | Basic and acidic residues | ||||
Sequence: IKDPSAKKPEDWDEKEFIDDPEDKKPEGYDDIPEEITDPDAKK | ||||||
Compositional bias | 355-381 | Basic and acidic residues | ||||
Sequence: TWGKQKDAEKAAFEEAEKKREEEESKA | ||||||
Compositional bias | 382-405 | Acidic residues | ||||
Sequence: APADSDAEEDDDADDDSDDADDKS |