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Protein

Calreticulin

Gene

Calr

Organism
Rattus norvegicus (Rat)
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 similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Calcium; via carbonyl oxygenBy similarity
Metal bindingi62 – 621Calcium; via carbonyl oxygenBy similarity
Metal bindingi64 – 641Calcium; via carbonyl oxygenBy similarity
Binding sitei109 – 1091CarbohydrateBy similarity
Binding sitei111 – 1111CarbohydrateBy similarity
Binding sitei128 – 1281CarbohydrateBy similarity
Binding sitei135 – 1351CarbohydrateBy similarity
Binding sitei317 – 3171CarbohydrateBy similarity
Metal bindingi328 – 3281CalciumBy similarity

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • carbohydrate binding Source: UniProtKB-KW
  • glycoprotein binding Source: RGD
  • hormone binding Source: RGD
  • iron ion binding Source: RGD
  • mRNA binding Source: BHF-UCL
  • peptide binding Source: RGD
  • unfolded protein binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_274632. Calnexin/calreticulin cycle.
REACT_284319. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_302011. Scavenging by Class A Receptors.
REACT_315399. Scavenging by Class F Receptors.
REACT_343414. ER-Phagosome pathway.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Calr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi620288. Calr.

Subcellular locationi

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: Ensembl
  • endoplasmic reticulum Source: RGD
  • external side of plasma membrane Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: RGD
  • extracellular space Source: RGD
  • focal adhesion Source: Ensembl
  • Golgi apparatus Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • MHC class I peptide loading complex Source: Ensembl
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • polysome Source: Ensembl
  • protein complex Source: RGD
  • sarcoplasmic reticulum Source: RGD
  • sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  • smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17173 PublicationsAdd
BLAST
Chaini18 – 416399CalreticulinPRO_0000004177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysineBy similarity
Disulfide bondi105 ↔ 137By similarity
Modified residuei159 – 1591N6-acetyllysineBy similarity
Modified residuei209 – 2091N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP18418.
PRIDEiP18418.

2D gel databases

World-2DPAGE0004:P18418.

Expressioni

Tissue specificityi

Predentin and odontoblast.1 Publication

Gene expression databases

GenevisibleiP18418. RN.

Interactioni

Subunit structurei

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 and C9orf9 homolog (By similarity). Interacts with PDIA3/ERp57.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PDIA3P301012EBI-916742,EBI-979862From a different organism.

Protein-protein interaction databases

BioGridi249008. 3 interactions.
IntActiP18418. 6 interactions.
MINTiMINT-245423.
STRINGi10116.ENSRNOP00000004091.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni220 – 2223Combined sources
Beta strandi223 – 2253Combined sources
Turni234 – 2363Combined sources
Beta strandi240 – 2434Combined sources
Helixi255 – 2584Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi301 – 3033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HHNNMR-A206-305[»]
1K91NMR-A238-273[»]
1K9CNMR-A206-278[»]
ProteinModelPortaliP18418.
SMRiP18418. Positions 206-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati191 – 202121-1Add
BLAST
Repeati210 – 221121-2Add
BLAST
Repeati227 – 238121-3Add
BLAST
Repeati244 – 255121-4Add
BLAST
Repeati259 – 269112-1Add
BLAST
Repeati273 – 283112-2Add
BLAST
Repeati287 – 297112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 197180N-domainAdd
BLAST
Regioni191 – 255654 X approximate repeatsAdd
BLAST
Regioni198 – 308111P-domainAdd
BLAST
Regioni237 – 27034Interaction with PPIBBy similarityAdd
BLAST
Regioni259 – 297393 X approximate repeatsAdd
BLAST
Regioni309 – 416108C-domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi413 – 4164Prevents secretion from ER

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi351 – 40757Asp/Glu/Lys-richAdd
BLAST

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.

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP18418.
KOiK08057.
OMAiDDFSNKG.
OrthoDBiEOG77126Z.
PhylomeDBiP18418.
TreeFamiTF338438.

Family and domain databases

Gene3Di2.60.120.200. 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. 1 hit.
[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.

P18418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV
60 70 80 90 100
LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE
110 120 130 140 150
QNIDCGGGYV KLFPGGLDQK 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 EAEDKEDEDD RDEDEDEEDE
410
KEEDEEDATG QAKDEL
Length:416
Mass (Da):47,995
Last modified:November 1, 1990 - v1
Checksum:i2E6713CED31A2970
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691P → R in CAA31987 (Ref. 9) Curated
Sequence conflicti359 – 3613DKQ → AAG in CAA31987 (Ref. 9) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJH0819.
RefSeqiNP_071794.1. NM_022399.2.
UniGeneiRn.974.

Genome annotation databases

EnsembliENSRNOT00000004091; ENSRNOP00000004091; ENSRNOG00000003029.
GeneIDi64202.
KEGGirno:64202.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJH0819.
RefSeqiNP_071794.1. NM_022399.2.
UniGeneiRn.974.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HHNNMR-A206-305[»]
1K91NMR-A238-273[»]
1K9CNMR-A206-278[»]
ProteinModelPortaliP18418.
SMRiP18418. Positions 206-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249008. 3 interactions.
IntActiP18418. 6 interactions.
MINTiMINT-245423.
STRINGi10116.ENSRNOP00000004091.

2D gel databases

World-2DPAGE0004:P18418.

Proteomic databases

PaxDbiP18418.
PRIDEiP18418.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004091; ENSRNOP00000004091; ENSRNOG00000003029.
GeneIDi64202.
KEGGirno:64202.

Organism-specific databases

CTDi811.
RGDi620288. Calr.

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP18418.
KOiK08057.
OMAiDDFSNKG.
OrthoDBiEOG77126Z.
PhylomeDBiP18418.
TreeFamiTF338438.

Enzyme and pathway databases

ReactomeiREACT_274632. Calnexin/calreticulin cycle.
REACT_284319. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
REACT_302011. Scavenging by Class A Receptors.
REACT_315399. Scavenging by Class F Receptors.
REACT_343414. ER-Phagosome pathway.

Miscellaneous databases

EvolutionaryTraceiP18418.
NextBioi612898.
PROiP18418.

Gene expression databases

GenevisibleiP18418. RN.

Family and domain databases

Gene3Di2.60.120.200. 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. 1 hit.
[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...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCALR_RAT
AccessioniPrimary (citable) accession number: P18418
Secondary accession number(s): P10452
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 24, 2015
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.