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P18418 (CALR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
CALBP
CRP55
Calcium-binding protein 3
Short name=CABP3
Calregulin
Endoplasmic reticulum resident protein 60
Short name=ERp60
HACBP
Gene names
Name:Calr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length416 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 and TRIM21. Interacts with PPIB By similarity. Interacts with PDIA3/ERp57. Ref.11

Subcellular location

Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen By similarity Ref.10.

Tissue specificity

Predentin and odontoblast. Ref.10

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.

Sequence similarities

Belongs to the calreticulin family.

Caution

Was originally (Ref.9) thought to be D-beta-hydroxybutyrate dehydrogenase.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Sarcoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell differentiation

Inferred from expression pattern PubMed 9011638. Source: RGD

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from expression pattern PubMed 16236328. Source: RGD

cellular response to organic substance

Inferred from expression pattern PubMed 10833321. Source: RGD

cellular senescence

Inferred from electronic annotation. Source: Ensembl

chaperone-mediated protein folding

Inferred from mutant phenotype PubMed 12401114. Source: RGD

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of retinoic acid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of translation

Inferred from direct assay PubMed 14726956. Source: BHF-UCL

peptide antigen assembly with MHC class I protein complex

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendritic cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

protein folding

Traceable author statement Ref.13. Source: RGD

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 11032977. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 16339744. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 11452518. Source: RGD

response to testosterone

Inferred from expression pattern PubMed 9751517. Source: RGD

spermatogenesis

Inferred from expression pattern Ref.2. Source: RGD

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: RGD

MHC class I peptide loading complex

Inferred from electronic annotation. Source: Ensembl

acrosomal vesicle

Inferred from direct assay Ref.2. Source: RGD

cell surface

Inferred from direct assay PubMed 11891802. Source: RGD

cytoplasm

Inferred from direct assay PubMed 11891802. Source: RGD

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay PubMed 18385140. Source: MGI

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular matrix

Inferred from direct assay Ref.10. Source: RGD

extracellular space

Inferred from direct assay Ref.10. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 11452518. Source: RGD

nucleus

Inferred from direct assay PubMed 12603316. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 8600158. Source: RGD

polysome

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 12401114. Source: RGD

sarcoplasmic reticulum

Inferred from direct assay PubMed 8600158. Source: RGD

sarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

smooth endoplasmic reticulum

Inferred from direct assay PubMed 22665516. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 8500729. Source: RGD

carbohydrate binding

Inferred from electronic annotation. Source: Ensembl

glycoprotein binding

Inferred from physical interaction PubMed 12401114. Source: RGD

hormone binding

Inferred from physical interaction PubMed 12603316. Source: RGD

iron ion binding

Inferred from direct assay PubMed 8500729. Source: RGD

mRNA binding

Inferred from direct assay PubMed 14726956. Source: BHF-UCL

peptide binding

Inferred from direct assay PubMed 10833321. Source: RGD

protein binding

Inferred from physical interaction PubMed 22665516. Source: IntAct

unfolded protein binding

Inferred from mutant phenotype PubMed 12401114. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDIA3P301012EBI-916742,EBI-979862From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.5 Ref.6 Ref.7
Chain18 – 416399Calreticulin
PRO_0000004177

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 – 416108C-domain
Motif413 – 4164Prevents secretion from ER
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

Experimental info

Sequence conflict2691P → R in CAA31987. Ref.9
Sequence conflict359 – 3613DKQ → AAG in CAA31987. Ref.9

Secondary structure

.............. 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18418 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 2E6713CED31A2970

FASTA41647,995
        10         20         30         40         50         60 
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDQ 

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

       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 KAAEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEDEEDE KEEDEEDATG QAKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Structural homology between the rat calreticulin gene product and the Onchocerca volvulus antigen Ral-1."
Murthy K.K., Banville D., Srikant C.B., Carrier F., Bell A., Holmes C., Patel Y.C.
Nucleic Acids Res. 18:4933-4933(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain cortex.
[2]"An endoplasmic reticulum protein, calreticulin, is transported into the acrosome of rat sperm."
Nakamura M., Moriya M., Baba T., Michikawa Y., Yamanobe T., Arai K., Okinaga S., Kobayashi T.
Exp. Cell Res. 205:101-110(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[3]"Retention and retrieval: both mechanisms cooperate to maintain calreticulin in the endoplasmic reticulum."
Soennichsen B., Fuellekrug J., van Nguyen P., Diekmann W., Robinson D.G., Mieskes G.
J. Cell Sci. 107:2705-2717(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[5]"Calreticulin is present in the acrosome of spermatids of rat testis."
Nakamura M., Michikawa Y., Baba T., Okinaga S., Arai K.
Biochem. Biophys. Res. Commun. 186:668-673(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-32.
Strain: Sprague-Dawley.
Tissue: Testis.
[6]"Identification of protein disulfide isomerase and calreticulin as autoimmune antigens in LEC strain of rats."
Yokoi T., Nagayama S., Kajiwara R., Kawaguchi Y., Horiuchi R., Kamataki T.
Biochim. Biophys. Acta 1158:339-344(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-32.
Strain: LEC.
Tissue: Liver.
[7]"Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain."
Treves S., de Mattei M., Lanfredi M., Villa A., Green N.M., Maclennan D.H., Meldolesi J., Pozzan T.
Biochem. J. 271:473-480(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-29.
[8]Lubec G., Afjehi-Sadat L., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-36; 88-98 AND 163-185, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[9]Lone Y.-C., Bailly A., Latruffe N.
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-361.
Strain: Sprague-Dawley.
[10]"Calreticulin -- an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix."
Somogyi E., Petersson U., Hultenby K., Wendel M.
Matrix Biol. 22:179-191(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[11]"TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain."
Frickel E.M., Riek R., Jelesarov I., Helenius A., Wuethrich K., Ellgaard L.
Proc. Natl. Acad. Sci. U.S.A. 99:1954-1959(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDIA3.
[12]"NMR structure of the calreticulin P-domain."
Ellgaard L., Riek R., Herrmann T., Guntert P., Braun D., Helenius A., Wuthrich K.
Proc. Natl. Acad. Sci. U.S.A. 98:3133-3138(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 206-305.
[13]"NMR structures of 36 and 73-residue fragments of the calreticulin P-domain."
Ellgaard L., Bettendorff P., Braun D., Herrmann T., Fiorito F., Jelesarov I., Guntert P., Helenius A., Wuthrich K.
J. Mol. Biol. 322:773-784(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 206-278.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53363 mRNA. Translation: CAA37446.1.
D78308 mRNA. Translation: BAA11345.1.
X79327 mRNA. Translation: CAA55890.1.
BC062395 mRNA. Translation: AAH62395.1.
X13702 mRNA. Translation: CAA31987.1.
PIRJH0819.
RefSeqNP_071794.1. NM_022399.2.
UniGeneRn.974.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HHNNMR-A206-305[»]
1K91NMR-A238-273[»]
1K9CNMR-A206-278[»]
ProteinModelPortalP18418.
SMRP18418. Positions 206-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249008. 3 interactions.
IntActP18418. 5 interactions.
MINTMINT-245423.

2D gel databases

World-2DPAGE0004:P18418.

Proteomic databases

PaxDbP18418.
PRIDEP18418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004091; ENSRNOP00000004091; ENSRNOG00000003029.
GeneID64202.
KEGGrno:64202.

Organism-specific databases

CTD811.
RGD620288. Calr.

Phylogenomic databases

eggNOGNOG305105.
GeneTreeENSGT00430000030841.
HOGENOMHOG000192435.
HOVERGENHBG005407.
InParanoidP18418.
KOK08057.
OMAVKLFPDG.
OrthoDBEOG77126Z.
PhylomeDBP18418.
TreeFamTF338438.

Gene expression databases

GenevestigatorP18418.

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. 2 hits.
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...

Other

EvolutionaryTraceP18418.
NextBio612898.
PROP18418.

Entry information

Entry nameCALR_RAT
AccessionPrimary (citable) accession number: P18418
Secondary accession number(s): P10452
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 145 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references