Q9ZPP1 (CALR_BERST) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 74.
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 | Berberis stolonifera (Barberry) |
| Taxonomic identifier | 33814 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › Ranunculales › Berberidaceae › Berberis![]() |
Protein attributes
| Sequence length | 416 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 | Endoplasmic reticulum lumen By similarity. |
| 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 |
| Gene Ontology (GO) | |
| Biological_process | protein folding Inferred from electronic annotation. Source: InterPro |
| Cellular_component | endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – ? | Potential | |||||||||
| Chain | ? – 416 | Calreticulin | PRO_0000004187 | ||||||||
Regions | |||||||||||
| Repeat | 194 – 205 | 12 | 1-1 | ||||||||
| Repeat | 213 – 224 | 12 | 1-2 | ||||||||
| Repeat | 230 – 241 | 12 | 1-3 | ||||||||
| Repeat | 248 – 259 | 12 | 1-4 | ||||||||
| Repeat | 263 – 273 | 11 | 2-1 | ||||||||
| Repeat | 277 – 287 | 11 | 2-2 | ||||||||
| Repeat | 291 – 301 | 11 | 2-3 | ||||||||
| Region | 194 – 259 | 66 | 4 X approximate repeats | ||||||||
| Region | 263 – 301 | 39 | 3 X approximate repeats | ||||||||
| Motif | 413 – 416 | 4 | Prevents secretion from ER Potential | ||||||||
| Compositional bias | 355 – 411 | 57 | Asp/Glu/Lys-rich | ||||||||
Sites | |||||||||||
| Binding site | 112 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 114 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 131 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 138 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 321 | 1 | Carbohydrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 54 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 108 ↔ 140 | By similarity | |||||||||
Sequences
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References
| [1] | "Calreticulin from Berberis stolonifera." Chou W.-M., Kutchan T.M. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF052040 mRNA. Translation: AAD17490.1. |
3D structure databases | |
| ProteinModelPortal | Q9ZPP1. |
| SMR | Q9ZPP1. Positions 209-282. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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_BERST | ||||||||
| Accession | Primary (citable) accession number: Q9ZPP1 | ||||||||
| 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
