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P14211 (CALR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.11 Ref.12

Subunit structure

Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21 By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PPIB. Ref.8 Ref.9

Subcellular location

Endoplasmic reticulum lumen. Cytoplasmic granule. Sarcoplasmic reticulum lumen By similarity. Note: Associated with the lytic granules in the cytolytic T-lymphocytes. Ref.7

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.

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 electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to organic substance

Inferred from electronic annotation. Source: Ensembl

cellular senescence

Inferred from mutant phenotype PubMed 14726956. Source: BHF-UCL

chaperone-mediated protein folding

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton organization

Inferred from direct assay PubMed 15136153. Source: MGI

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 electronic annotation. Source: Ensembl

peptide antigen assembly with MHC class I protein complex

Inferred from mutant phenotype PubMed 11825569. Source: BHF-UCL

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from mutant phenotype PubMed 14726956. Source: BHF-UCL

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 mutant phenotype PubMed 15998798. Source: UniProtKB

positive regulation of phagocytosis

Inferred from mutant phenotype PubMed 17187072. Source: BHF-UCL

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 localization to nucleus

Inferred from mutant phenotype PubMed 15998798. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of meiosis

Inferred from direct assay PubMed 15136153. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

MHC class I peptide loading complex

Inferred from mutant phenotype PubMed 11825569. Source: BHF-UCL

acrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay PubMed 14517290PubMed 15131110PubMed 15977177PubMed 21532570PubMed 21892174. Source: MGI

endoplasmic reticulum lumen

Inferred from direct assay PubMed 21187406. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 15136153. Source: MGI

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 15136153. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Traceable author statement. Source: Reactome

polysome

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

sarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.12. Source: UniProtKB

carbohydrate binding

Inferred from direct assay Ref.11. Source: UniProtKB

hormone binding

Inferred from electronic annotation. Source: Ensembl

iron ion binding

Inferred from electronic annotation. Source: Ensembl

mRNA binding

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

peptide binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.1 Ref.5
Chain18 – 416399Calreticulin
PRO_0000004174

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

Amino acid modifications

Modified residue481N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue2091N6-acetyllysine Ref.10
Disulfide bond105 ↔ 137 Ref.11 Ref.12

Experimental info

Sequence conflict2721K → R in BAE35687. Ref.3
Sequence conflict4071E → Q in BAE35687. Ref.3

Secondary structure

.................................................... 416
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14211 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 24C03B00913408D8

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

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPSGLDQK 

       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 EAEDKEDDDD RDEDEDEEDE KEEDEEESPG QAKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein."
Smith M.J., Koch G.L.E.
EMBO J. 8:3581-3586(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-48 AND 129-161.
Strain: BALB/c.
Tissue: Liver.
[2]"Determination of the sequence of an expressible cDNA clone encoding ERp60/calregulin by the use of a novel nested set method."
Mazzarella R.A., Gold P., Cunningham M., Green M.
Gene 120:217-225(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain and 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].
Strain: FVB/N-3.
Tissue: Mammary gland.
[5]"Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-38.
Tissue: Fibroblast.
[6]Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-36; 56-64; 74-151; 154-159; 163-222; 225-272; 323-351; 341-357 AND 392-413, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[7]"The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes."
Dupuis M., Schaerer E., Krause K.-H., Tschopp J.
J. Exp. Med. 177:1-7(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3; HSPA5 AND HSP90B1.
[9]"Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain."
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.
J. Biol. Chem. 285:35551-35557(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIB.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[11]"Structural basis of carbohydrate recognition by calreticulin."
Kozlov G., Pocanschi C.L., Rosenauer A., Bastos-Aristizabal S., Gorelik A., Williams D.B., Gehring K.
J. Biol. Chem. 285:38612-38620(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM AND TETRASACCHARIDE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BOND.
[12]"Structural and functional relationships between the lectin and arm domains of calreticulin."
Pocanschi C.L., Kozlov G., Brockmeier U., Brockmeier A., Williams D.B., Gehring K.
J. Biol. Chem. 286:27266-27277(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 18-368 IN COMPLEX WITH CALCIUM IONS, FUNCTION, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14926 mRNA. Translation: CAA33053.1.
M92988 mRNA. Translation: AAA37569.1.
AK075605 mRNA. Translation: BAC35852.1.
AK160197 mRNA. Translation: BAE35687.1.
BC003453 mRNA. Translation: AAH03453.1.
PIRS06763.
RefSeqNP_031617.1. NM_007591.3.
UniGeneMm.1971.
Mm.467043.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O0VX-ray2.30A18-368[»]
3O0WX-ray1.95A18-368[»]
3O0XX-ray2.01A/B18-368[»]
3RG0X-ray2.57A18-368[»]
ProteinModelPortalP14211.
SMRP14211. Positions 18-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198458. 5 interactions.
IntActP14211. 14 interactions.
MINTMINT-1679870.

PTM databases

PhosphoSiteP14211.

2D gel databases

COMPLUYEAST-2DPAGEP14211.
REPRODUCTION-2DPAGEIPI00123639.
P14211.
SWISS-2DPAGEP14211.

Proteomic databases

PaxDbP14211.
PRIDEP14211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
GeneID12317.
KEGGmmu:12317.
UCSCuc009mnp.1. mouse.

Organism-specific databases

CTD811.
MGIMGI:88252. Calr.

Phylogenomic databases

eggNOGNOG305105.
GeneTreeENSGT00430000030841.
HOGENOMHOG000192435.
HOVERGENHBG005407.
InParanoidP14211.
KOK08057.
OMAKSECENI.
OrthoDBEOG77126Z.
PhylomeDBP14211.
TreeFamTF338438.

Enzyme and pathway databases

ReactomeREACT_102124. Immune System.
REACT_196573. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP14211.
BgeeP14211.
CleanExMM_CALR.
GenevestigatorP14211.

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

ChiTaRSCALR. mouse.
EvolutionaryTraceQ3TVD2.
NextBio280884.
PROP14211.
SOURCESearch...

Entry information

Entry nameCALR_MOUSE
AccessionPrimary (citable) accession number: P14211
Secondary accession number(s): Q3TVD2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 155 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot