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Q8K3H7 (CALR_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name=ERp60
HACBP
Gene names
Name:CALR
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis By similarity.

Subunit structure

Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21. Interacts with PPIB By similarity.

Subcellular location

Endoplasmic reticulum lumen. Sarcoplasmic 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.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain By similarity.

Sequence similarities

Belongs to the calreticulin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050672EBI-9005068,EBI-3894543From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 417400Calreticulin
PRO_0000004172

Regions

Repeat191 – 202121-1
Repeat210 – 221121-2
Repeat227 – 238121-3
Repeat244 – 255121-4
Repeat259 – 269112-1
Repeat273 – 283112-2
Repeat287 – 297112-3
Region18 – 197180N-domain
Region191 – 255654 X approximate repeats
Region198 – 308111P-domain
Region237 – 27034Interaction with PPIB By similarity
Region259 – 297393 X approximate repeats
Region309 – 417109C-domain
Motif414 – 4174Prevents secretion from ER Potential
Compositional bias351 – 40757Asp/Glu/Lys-rich

Sites

Metal binding261Calcium; via carbonyl oxygen By similarity
Metal binding621Calcium; via carbonyl oxygen By similarity
Metal binding641Calcium; via carbonyl oxygen By similarity
Metal binding3281Calcium By similarity
Binding site1091Carbohydrate By similarity
Binding site1111Carbohydrate By similarity
Binding site1281Carbohydrate By similarity
Binding site1351Carbohydrate By similarity
Binding site3171Carbohydrate By similarity

Amino acid modifications

Modified residue481N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue2091N6-acetyllysine By similarity
Disulfide bond105 ↔ 137 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K3H7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D617DA37D14F2D45

FASTA41748,243
        10         20         30         40         50         60 
MLLSVPLLLG LLGLAAAEPA VYFKEQFLDG DDWTNRWVES KHKSDFGKFV LSSGKFYGDQ 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPGSLDQK 

       130        140        150        160        170        180 
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 

       190        200        210        220        230        240 
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 

       310        320        330        340        350        360 
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KASEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEEDEDE KEEDEEDTTP GQTKDEL 

« Hide

References

[1]Chung J.Y., Lee G.M.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY100688 mRNA. Translation: AAM48568.1.
RefSeqNP_001231051.1. NM_001244122.1.

3D structure databases

ProteinModelPortalQ8K3H7.
SMRQ8K3H7. Positions 206-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8K3H7. 1 interaction.
MINTMINT-4997757.

Proteomic databases

PRIDEQ8K3H7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689096.
KEGGcge:100689096.

Organism-specific databases

CTD811.

Phylogenomic databases

HOVERGENHBG005407.
KOK08057.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR001580. 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]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_CRIGR
AccessionPrimary (citable) accession number: Q8K3H7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families