P93508 (CALR_RICCO) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 92.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Calreticulin |
| Organism | Ricinus communis (Castor bean) [Complete proteome] |
| Taxonomic identifier | 3988 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Acalyphoideae › Acalypheae › Ricinus![]() |
Protein attributes
| Sequence length | 415 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| 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. |
| Subcellular location | |
| 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 By similarity. The zinc binding sites are localized to the N-domain By similarity. |
| Sequence similarities | Belongs to the calreticulin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Repeat Signal |
| Ligand | Calcium Lectin Metal-binding Zinc |
| Molecular function | Chaperone |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | protein folding Inferred from electronic annotation. Source: InterPro |
| Cellular_component | endoplasmic reticulum lumen Inferred from direct assay PubMed 11870775. Source: UniProtKB |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Potential | ||||||||
| Chain | 21 – 415 | 395 | Calreticulin | PRO_0000004195 | |||||||
Regions | |||||||||||
| Repeat | 192 – 203 | 12 | 1-1 | ||||||||
| Repeat | 211 – 222 | 12 | 1-2 | ||||||||
| Repeat | 228 – 239 | 12 | 1-3 | ||||||||
| Repeat | 246 – 257 | 12 | 1-4 | ||||||||
| Repeat | 261 – 271 | 11 | 2-1 | ||||||||
| Repeat | 275 – 285 | 11 | 2-2 | ||||||||
| Repeat | 289 – 299 | 11 | 2-3 | ||||||||
| Region | 192 – 257 | 66 | 4 X approximate repeats | ||||||||
| Region | 261 – 299 | 39 | 3 X approximate repeats | ||||||||
| Motif | 412 – 415 | 4 | Prevents secretion from ER Potential | ||||||||
| Compositional bias | 353 – 410 | 58 | Asp/Glu/Lys-rich | ||||||||
Sites | |||||||||||
| Binding site | 110 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 112 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 129 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 136 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 319 | 1 | Carbohydrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 52 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 152 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 106 ↔ 138 | By similarity | |||||||||
Sequences
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References
| [1] | "Cloning and characterization of the calreticulin gene from Ricinus communis L." Coughlan S.J., Hastings C., Winfrey R. Jr. Plant Mol. Biol. 34:897-911(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U74631 Genomic DNA. Translation: AAB71420.1. U74630 mRNA. Translation: AAB71419.1. |
| PIR | T10172. |
| RefSeq | XP_002512501.1. XM_002512455.1. |
3D structure databases | |
| ProteinModelPortal | P93508. |
| SMR | P93508. Positions 207-307. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 8269812. |
| KEGG | rcu:RCOM_1434770. |
Phylogenomic databases | |
| KO | K08057. |
| ProtClustDB | CLSN2719690. |
Family and domain databases | |
| Gene3D | 2.10.250.10. 1 hit. 2.60.120.200. 1 hit. |
| InterPro | IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. IPR009033. Calreticulin/calnexin_P_dom. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. [Graphical view] |
| PANTHER | PTHR11073. PTHR11073. 1 hit. |
| Pfam | PF00262. Calreticulin. 1 hit. [Graphical view] |
| PIRSF | PIRSF002356. Calreticulin. 1 hit. |
| PRINTS | PR00626. CALRETICULIN. |
| SUPFAM | SSF63887. Calret_calnex_P. 1 hit. SSF49899. ConA_like_lec_gl. 1 hit. |
| PROSITE | PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 2 hits. PS00014. ER_TARGET. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CALR_RICCO | ||||||||
| Accession | Primary (citable) accession number: P93508 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
