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Protein

Calreticulin

Gene

Calr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi26Calcium; via carbonyl oxygen1 Publication1
Metal bindingi62Calcium; via carbonyl oxygen1 Publication1
Metal bindingi64Calcium; via carbonyl oxygen1 Publication1
Binding sitei109Carbohydrate1
Binding sitei111Carbohydrate1
Binding sitei128Carbohydrate1
Binding sitei135Carbohydrate1
Binding sitei317Carbohydrate1
Metal bindingi328Calcium1 Publication1

GO - Molecular functioni

  • androgen receptor binding Source: MGI
  • calcium ion binding Source: UniProtKB
  • carbohydrate binding Source: UniProtKB
  • glycoprotein binding Source: MGI
  • hormone binding Source: Ensembl
  • integrin binding Source: MGI
  • iron ion binding Source: Ensembl
  • mRNA binding Source: BHF-UCL
  • peptide binding Source: Ensembl
  • poly(A) RNA binding Source: MGI
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1236974. ER-Phagosome pathway.
R-MMU-3000480. Scavenging by Class A Receptors.
R-MMU-3000484. Scavenging by Class F Receptors.
R-MMU-901042. Calnexin/calreticulin cycle.
R-MMU-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name:
ERp60
HACBP
Gene namesi
Name:Calr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88252. Calr.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication
  • Cytoplasmic granule 1 Publication
  • Sarcoplasmic reticulum lumen By similarity

  • Note: Associated with the lytic granules in the cytolytic T-lymphocytes.

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum lumen Source: MGI
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: Ensembl
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • Golgi apparatus Source: Ensembl
  • membrane Source: MGI
  • MHC class I peptide loading complex Source: BHF-UCL
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • phagocytic vesicle Source: Reactome
  • polysome Source: BHF-UCL
  • sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000000417418 – 416CalreticulinAdd BLAST399

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysineBy similarity1
Disulfide bondi105 ↔ 1372 Publications
Modified residuei159N6-acetyllysineBy similarity1
Modified residuei209N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP14211.
MaxQBiP14211.
PaxDbiP14211.
PeptideAtlasiP14211.
PRIDEiP14211.
TopDownProteomicsiP14211.

2D gel databases

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

PTM databases

iPTMnetiP14211.
PhosphoSitePlusiP14211.
SwissPalmiP14211.

Expressioni

Gene expression databases

BgeeiENSMUSG00000003814.
CleanExiMM_CALR.
ExpressionAtlasiP14211. baseline and differential.
GenevisibleiP14211. MM.

Interactioni

Subunit structurei

Monomer. Interacts with GABARAP, NR3C1, PDIA3/ERp57, SPACA9 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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AppP120234EBI-644340,EBI-78814
NcstnP577162EBI-644340,EBI-998934
Psen1P497693EBI-644340,EBI-990067

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198458. 5 interactors.
IntActiP14211. 14 interactors.
MINTiMINT-1679870.
STRINGi10090.ENSMUSP00000003912.

Structurei

Secondary structure

1416
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 25Combined sources5
Helixi30 – 35Combined sources6
Beta strandi37 – 39Combined sources3
Beta strandi42 – 44Combined sources3
Beta strandi49 – 52Combined sources4
Turni60 – 63Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi70 – 84Combined sources15
Beta strandi91 – 98Combined sources8
Beta strandi104 – 107Combined sources4
Beta strandi110 – 113Combined sources4
Helixi119 – 121Combined sources3
Beta strandi129 – 137Combined sources9
Turni138 – 140Combined sources3
Beta strandi141 – 150Combined sources10
Beta strandi153 – 156Combined sources4
Beta strandi166 – 176Combined sources11
Beta strandi180 – 186Combined sources7
Beta strandi189 – 195Combined sources7
Helixi196 – 199Combined sources4
Beta strandi206 – 209Combined sources4
Beta strandi293 – 295Combined sources3
Turni303 – 306Combined sources4
Beta strandi311 – 322Combined sources12
Beta strandi326 – 334Combined sources9
Helixi336 – 345Combined sources10
Helixi347 – 360Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O0VX-ray2.30A18-206[»]
A301-368[»]
3O0WX-ray1.95A18-206[»]
A301-368[»]
3O0XX-ray2.01A/B18-206[»]
A/B301-368[»]
3RG0X-ray2.57A18-238[»]
A273-368[»]
ProteinModelPortaliP14211.
SMRiP14211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati191 – 2021-1Add BLAST12
Repeati210 – 2211-2Add BLAST12
Repeati227 – 2381-3Add BLAST12
Repeati244 – 2551-4Add BLAST12
Repeati259 – 2692-1Add BLAST11
Repeati273 – 2832-2Add BLAST11
Repeati287 – 2972-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 197N-domainAdd BLAST180
Regioni191 – 2554 X approximate repeatsAdd BLAST65
Regioni198 – 308P-domainAdd BLAST111
Regioni237 – 270Interaction with PPIB1 PublicationAdd BLAST34
Regioni259 – 2973 X approximate repeatsAdd BLAST39
Regioni309 – 416C-domainAdd BLAST108

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi413 – 416Prevents secretion from ER4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi351 – 407Asp/Glu/Lys-richAdd BLAST57

Domaini

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).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 similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP14211.
KOiK08057.
OMAiIPNPEYM.
OrthoDBiEOG091G0AP1.
PhylomeDBiP14211.
TreeFamiTF338438.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 2 hits.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14211-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV
60 70 80 90 100
LSSGKFYGDL EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPSGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY
160 170 180 190 200
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW
210 220 230 240 250
DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP
260 270 280 290 300
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
310 320 330 340 350
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT
360 370 380 390 400
KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE
410
KEEDEEESPG QAKDEL
Length:416
Mass (Da):47,995
Last modified:January 1, 1990 - v1
Checksum:i24C03B00913408D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti272K → R in BAE35687 (PubMed:16141072).Curated1
Sequence conflicti407E → Q in BAE35687 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22479.1.
PIRiS06763.
RefSeqiNP_031617.1. NM_007591.3.
UniGeneiMm.1971.
Mm.467043.

Genome annotation databases

EnsembliENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
GeneIDi12317.
KEGGimmu:12317.
UCSCiuc009mnp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22479.1.
PIRiS06763.
RefSeqiNP_031617.1. NM_007591.3.
UniGeneiMm.1971.
Mm.467043.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O0VX-ray2.30A18-206[»]
A301-368[»]
3O0WX-ray1.95A18-206[»]
A301-368[»]
3O0XX-ray2.01A/B18-206[»]
A/B301-368[»]
3RG0X-ray2.57A18-238[»]
A273-368[»]
ProteinModelPortaliP14211.
SMRiP14211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198458. 5 interactors.
IntActiP14211. 14 interactors.
MINTiMINT-1679870.
STRINGi10090.ENSMUSP00000003912.

PTM databases

iPTMnetiP14211.
PhosphoSitePlusiP14211.
SwissPalmiP14211.

2D gel databases

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

Proteomic databases

EPDiP14211.
MaxQBiP14211.
PaxDbiP14211.
PeptideAtlasiP14211.
PRIDEiP14211.
TopDownProteomicsiP14211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
GeneIDi12317.
KEGGimmu:12317.
UCSCiuc009mnp.1. mouse.

Organism-specific databases

CTDi811.
MGIiMGI:88252. Calr.

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP14211.
KOiK08057.
OMAiIPNPEYM.
OrthoDBiEOG091G0AP1.
PhylomeDBiP14211.
TreeFamiTF338438.

Enzyme and pathway databases

ReactomeiR-MMU-1236974. ER-Phagosome pathway.
R-MMU-3000480. Scavenging by Class A Receptors.
R-MMU-3000484. Scavenging by Class F Receptors.
R-MMU-901042. Calnexin/calreticulin cycle.
R-MMU-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

ChiTaRSiCalr. mouse.
PROiP14211.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000003814.
CleanExiMM_CALR.
ExpressionAtlasiP14211. baseline and differential.
GenevisibleiP14211. MM.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 2 hits.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALR_MOUSE
AccessioniPrimary (citable) accession number: P14211
Secondary accession number(s): Q3TVD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.