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P18418

- CALR_RAT

UniProt

P18418 - CALR_RAT

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Protein
Calreticulin
Gene
Calr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

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

GO - Molecular functioni

  1. calcium ion binding Source: RGD
  2. carbohydrate binding Source: Ensembl
  3. glycoprotein binding Source: RGD
  4. hormone binding Source: RGD
  5. iron ion binding Source: RGD
  6. mRNA binding Source: BHF-UCL
  7. peptide binding Source: RGD
  8. protein binding Source: IntAct
  9. unfolded protein binding Source: RGD
Complete GO annotation...

GO - Biological processi

  1. cardiac muscle cell differentiation Source: RGD
  2. cell cycle arrest Source: Ensembl
  3. cellular response to lithium ion Source: RGD
  4. cellular response to organic substance Source: RGD
  5. cellular senescence Source: Ensembl
  6. chaperone-mediated protein folding Source: RGD
  7. cortical actin cytoskeleton organization Source: Ensembl
  8. negative regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
  9. negative regulation of neuron differentiation Source: Ensembl
  10. negative regulation of retinoic acid receptor signaling pathway Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  12. negative regulation of translation Source: BHF-UCL
  13. peptide antigen assembly with MHC class I protein complex Source: Ensembl
  14. positive regulation of DNA replication Source: Ensembl
  15. positive regulation of cell cycle Source: Ensembl
  16. positive regulation of cell proliferation Source: Ensembl
  17. positive regulation of dendritic cell chemotaxis Source: Ensembl
  18. positive regulation of gene expression Source: Ensembl
  19. positive regulation of phagocytosis Source: Ensembl
  20. positive regulation of substrate adhesion-dependent cell spreading Source: Ensembl
  21. protein export from nucleus Source: Ensembl
  22. protein folding Source: RGD
  23. protein localization to nucleus Source: Ensembl
  24. protein stabilization Source: UniProtKB
  25. regulation of meiosis Source: Ensembl
  26. response to drug Source: RGD
  27. response to estradiol Source: RGD
  28. response to organic substance Source: RGD
  29. response to testosterone Source: RGD
  30. spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_100458. ATF6-alpha activates chaperone genes.
REACT_196415. Calnexin/calreticulin cycle.
REACT_198733. Scavenging by Class A Receptors.
REACT_198755. Scavenging by Class F Receptors.

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: Chromosome 19

Organism-specific databases

RGDi620288. Calr.

Subcellular locationi

Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen By similarity 1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: RGD
  2. MHC class I peptide loading complex Source: Ensembl
  3. acrosomal vesicle Source: RGD
  4. cell surface Source: RGD
  5. cytoplasm Source: RGD
  6. cytosol Source: Ensembl
  7. endoplasmic reticulum Source: MGI
  8. external side of plasma membrane Source: Ensembl
  9. extracellular matrix Source: RGD
  10. extracellular space Source: RGD
  11. intracellular membrane-bounded organelle Source: RGD
  12. nucleus Source: RGD
  13. perinuclear region of cytoplasm Source: RGD
  14. polysome Source: Ensembl
  15. protein complex Source: RGD
  16. sarcoplasmic reticulum Source: RGD
  17. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell
  18. 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 Publications
Add
BLAST
Chaini18 – 416399Calreticulin
PRO_0000004177Add
BLAST

Amino acid modifications

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

GenevestigatoriP18418.

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 By similarity. Interacts with PDIA3/ERp57.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi249008. 3 interactions.
IntActiP18418. 5 interactions.
MINTiMINT-245423.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HHNNMR-A206-305[»]
1K91NMR-A238-273[»]
1K9CNMR-A206-278[»]
ProteinModelPortaliP18418.
SMRiP18418. Positions 206-305.

Miscellaneous databases

EvolutionaryTraceiP18418.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 197180N-domain
Add
BLAST
Regioni191 – 255654 X approximate repeats
Add
BLAST
Regioni198 – 308111P-domain
Add
BLAST
Regioni237 – 27034Interaction with PPIB By similarity
Add
BLAST
Regioni259 – 297393 X approximate repeats
Add
BLAST
Regioni309 – 416108C-domain
Add
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-rich
Add
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.
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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
HOVERGENiHBG005407.
InParanoidiP18418.
KOiK08057.
OMAiVKLFPDG.
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.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[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

MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV    50
LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE 100
QNIDCGGGYV KLFPGGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY 150
KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW 200
DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP 250
EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT 350
KAAEKQMKDK QDEEQRLKEE EEDKKRKEEE EAEDKEDEDD RDEDEDEEDE 400
KEEDEEDATG QAKDEL 416
Length:416
Mass (Da):47,995
Last modified:November 1, 1990 - v1
Checksum:i2E6713CED31A2970
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691P → R in CAA31987. 1 Publication
Sequence conflicti359 – 3613DKQ → AAG in CAA31987. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JH0819.
RefSeqi NP_071794.1. NM_022399.2.
UniGenei Rn.974.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HHN NMR - A 206-305 [» ]
1K91 NMR - A 238-273 [» ]
1K9C NMR - A 206-278 [» ]
ProteinModelPortali P18418.
SMRi P18418. Positions 206-305.
ModBasei Search...

Protein-protein interaction databases

BioGridi 249008. 3 interactions.
IntActi P18418. 5 interactions.
MINTi MINT-245423.

2D gel databases

World-2DPAGE 0004:P18418.

Proteomic databases

PaxDbi P18418.
PRIDEi P18418.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004091 ; ENSRNOP00000004091 ; ENSRNOG00000003029 .
GeneIDi 64202.
KEGGi rno:64202.

Organism-specific databases

CTDi 811.
RGDi 620288. Calr.

Phylogenomic databases

eggNOGi NOG305105.
GeneTreei ENSGT00430000030841.
HOGENOMi HOG000192435.
HOVERGENi HBG005407.
InParanoidi P18418.
KOi K08057.
OMAi VKLFPDG.
OrthoDBi EOG77126Z.
PhylomeDBi P18418.
TreeFami TF338438.

Enzyme and pathway databases

Reactomei REACT_100458. ATF6-alpha activates chaperone genes.
REACT_196415. Calnexin/calreticulin cycle.
REACT_198733. Scavenging by Class A Receptors.
REACT_198755. Scavenging by Class F Receptors.

Miscellaneous databases

EvolutionaryTracei P18418.
NextBioi 612898.
PROi P18418.

Gene expression databases

Genevestigatori P18418.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR001580. 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 ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 146 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 (1 Publication) thought to be D-beta-hydroxybutyrate dehydrogenase.

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

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