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P18418

- CALR_RAT

UniProt

P18418 - CALR_RAT

Protein

Calreticulin

Gene

Calr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    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

    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

    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 cell cycle Source: Ensembl
    15. positive regulation of cell proliferation Source: Ensembl
    16. positive regulation of dendritic cell chemotaxis Source: Ensembl
    17. positive regulation of DNA replication 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

    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 1 PublicationPROSITE-ProRule annotation. Sarcoplasmic reticulum lumen By similarity

    GO - Cellular componenti

    1. acrosomal vesicle Source: RGD
    2. cell surface Source: RGD
    3. cytoplasm Source: RGD
    4. cytosol Source: Ensembl
    5. endoplasmic reticulum Source: MGI
    6. external side of plasma membrane Source: Ensembl
    7. extracellular matrix Source: RGD
    8. extracellular space Source: RGD
    9. Golgi apparatus Source: RGD
    10. intracellular membrane-bounded organelle Source: RGD
    11. MHC class I peptide loading complex Source: Ensembl
    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

    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

    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.By similarity1 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

    1
    416
    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.
    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.
    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

    Experimental Info

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

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 147 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 (PubMed:12782144) 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