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P15253

- CALR_RABIT

UniProt

P15253 - CALR_RABIT

Protein

Calreticulin

Gene

CALR

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Apr 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: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein folding Source: InterPro
    2. protein stabilization Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Sarcoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701H → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17172 PublicationsAdd
    BLAST
    Chaini18 – 418401CalreticulinPRO_0000004176Add
    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

    PRIDEiP15253.

    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, PDIA3/ERp57 and TRIM21. Interacts with PPIB By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APPP050673EBI-9005200,EBI-77613From a different organism.
    AppP120232EBI-9005200,EBI-78814From a different organism.

    Protein-protein interaction databases

    BioGridi1172073. 1 interaction.
    IntActiP15253. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP15253.
    SMRiP15253. Positions 206-305.
    ModBaseiSearch...
    MobiDBiSearch...

    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 – 418110C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi415 – 4184Prevents secretion from ER

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi351 – 40858Asp/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.
    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

    HOVERGENiHBG005407.

    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. 1 hit.
    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.

    P15253-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLPVPLLLG LLGLAAAEPV VYFKEQFLDG DGWTERWIES KHKSDFGKFV    50
    LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQP LVVQFTVKHE 100
    QNIDCGGGYV KLFPAGLDQK DMHGDSEYNI MFGPDICGPG TKKVHVIFNY 150
    KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW 200
    DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP 250
    EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
    PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT 350
    KTAEKQMKDK QDEEQRLKEE EEEKKRKEEE EAEEDEEDKD DKEDEDEDEE 400
    DKDEEEEEAA AGQAKDEL 418
    Length:418
    Mass (Da):48,275
    Last modified:April 1, 1990 - v1
    Checksum:iB6082B689DC763A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901P → T AA sequence (PubMed:1911780)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351E → D.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05138 mRNA. Translation: AAA31188.1.
    PIRiA34154.
    C33208.
    D33208.
    S13046.
    RefSeqiNP_001075704.1. NM_001082235.1.
    UniGeneiOcu.1840.

    Genome annotation databases

    GeneIDi100009050.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05138 mRNA. Translation: AAA31188.1 .
    PIRi A34154.
    C33208.
    D33208.
    S13046.
    RefSeqi NP_001075704.1. NM_001082235.1.
    UniGenei Ocu.1840.

    3D structure databases

    ProteinModelPortali P15253.
    SMRi P15253. Positions 206-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1172073. 1 interaction.
    IntActi P15253. 4 interactions.

    Proteomic databases

    PRIDEi P15253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009050.

    Organism-specific databases

    CTDi 811.

    Phylogenomic databases

    HOVERGENi HBG005407.

    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. 1 hit.
    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. "Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum."
      Fliegel L., Burns K., Maclennan D.H., Reithmeier R.A.F., Michalak M.
      J. Biol. Chem. 264:21522-21528(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Slow-twitch skeletal muscle.
    2. "Fast-twitch and slow-twitch skeletal muscles express the same isoform of calreticulin."
      Fliegel L., Michalak M.
      Biochem. Biophys. Res. Commun. 177:979-984(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fast-twitch skeletal muscle.
    3. "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 18-36.
    4. "Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum."
      Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L., Vance J.E., Opas M., Michalak M.
      J. Biol. Chem. 266:7155-7165(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-46.
    5. "Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin."
      Guan S., Falick A.M., Williams D.E., Cashman J.R.
      Biochemistry 30:9892-9900(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Lung.
    6. "Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins."
      Saito Y., Ihara Y., Leach M.R., Cohen-Doyle M.F., Williams D.B.
      EMBO J. 18:6718-6729(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Identification of the Zn2+ binding region in calreticulin."
      Baksh S., Spamer C., Heilmann C., Michalak M.
      FEBS Lett. 376:53-57(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING DOMAIN.
    8. "Identification of an N-domain histidine essential for chaperone function in calreticulin."
      Guo L., Groenendyk J., Papp S., Dabrowska M., Knoblach B., Kay C., Parker J.M., Opas M., Michalak M.
      J. Biol. Chem. 278:50645-50653(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-170.

    Entry informationi

    Entry nameiCALR_RABIT
    AccessioniPrimary (citable) accession number: P15253
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 118 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3