P27798 (CALR_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 115.
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 | ||||
| Gene names |
| ||||
| Organism | Caenorhabditis elegans [Reference proteome] | ||||
| Taxonomic identifier | 6239 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis![]() |
Protein attributes
| Sequence length | 395 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | Potential | ||||||||
| Chain | 16 – 395 | 380 | Calreticulin | PRO_0000004180 | |||||||
Regions | |||||||||||
| Repeat | 186 – 197 | 12 | 1-1 | ||||||||
| Repeat | 205 – 216 | 12 | 1-2 | ||||||||
| Repeat | 222 – 233 | 12 | 1-3 | ||||||||
| Repeat | 239 – 250 | 12 | 1-4 | ||||||||
| Repeat | 254 – 264 | 11 | 2-1 | ||||||||
| Repeat | 268 – 278 | 11 | 2-2 | ||||||||
| Repeat | 282 – 292 | 11 | 2-3 | ||||||||
| Region | 186 – 250 | 65 | 4 X approximate repeats | ||||||||
| Region | ? – 192 | N-domain | |||||||||
| Region | 193 – 301 | 109 | P-domain | ||||||||
| Region | 254 – 292 | 39 | 3 X approximate repeats | ||||||||
| Region | 302 – 395 | 94 | C-domain | ||||||||
| Motif | 392 – 395 | 4 | Prevents secretion from ER By similarity | ||||||||
| Compositional bias | 332 – 390 | 59 | Asp/Glu/Lys-rich | ||||||||
Sites | |||||||||||
| Binding site | 105 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 107 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 124 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 131 | 1 | Carbohydrate By similarity | ||||||||
| Binding site | 312 | 1 | Carbohydrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 101 ↔ 133 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "A C. elegans gene encodes a protein homologous to mammalian calreticulin." Smith M.J. DNA Seq. 2:235-240(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Bristol N2. |
| [2] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X59589 Genomic DNA. Translation: CAA42159.1. FO081168 Genomic DNA. Translation: CCD69629.1. |
| PIR | S25851. |
| RefSeq | NP_504575.1. NM_072174.3. |
3D structure databases | |
| ProteinModelPortal | P27798. |
| SMR | P27798. Positions 17-361. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-25701N. |
| IntAct | P27798. 4 interactions. |
| MINT | MINT-226928. |
| STRING | 6239.Y38A10A.5.1. |
2D gel databases | |
| World-2DPAGE | 0020:P27798. |
Proteomic databases | |
| PaxDb | P27798. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | Y38A10A.5.1; Y38A10A.5.1; Y38A10A.5. Y38A10A.5.2; Y38A10A.5.2; Y38A10A.5. |
| GeneID | 178997. |
| KEGG | cel:CELE_Y38A10A.5. |
| UCSC | Y38A10A.5.1. c. elegans. |
Organism-specific databases | |
| CTD | 178997. |
| WormBase | Y38A10A.5; CE21562; WBGene00000802; crt-1. |
Phylogenomic databases | |
| eggNOG | NOG305105. |
| GeneTree | ENSGT00430000030841. |
| HOGENOM | HOG000192435. |
| InParanoid | P27798. |
| KO | K08057. |
| OMA | DGWTDRW. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 2 hits. |
| InterPro | IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. 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 | SSF49899. ConA_like_lec_gl. 1 hit. |
| PROSITE | PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 3 hits. PS00014. ER_TARGET. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 903464. |
Entry information
| Entry name | CALR_CAEEL | ||||||||
| Accession | Primary (citable) accession number: P27798 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
