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P28491

- CALR_PIG

UniProt

P28491 - CALR_PIG

Protein

Calreticulin

Gene

CALR

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 3 (16 May 2012)
      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 By similarity. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis.By similarity1 Publication

    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. carbohydrate binding Source: Ensembl
    3. mRNA binding Source: Ensembl

    GO - Biological processi

    1. cell cycle arrest Source: Ensembl
    2. cellular senescence Source: Ensembl
    3. cortical actin cytoskeleton organization Source: Ensembl
    4. negative regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
    5. negative regulation of neuron differentiation Source: Ensembl
    6. negative regulation of retinoic acid receptor signaling pathway Source: Ensembl
    7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. peptide antigen assembly with MHC class I protein complex Source: Ensembl
    9. positive regulation of cell cycle Source: Ensembl
    10. positive regulation of cell proliferation Source: Ensembl
    11. positive regulation of dendritic cell chemotaxis Source: Ensembl
    12. positive regulation of DNA replication Source: Ensembl
    13. positive regulation of gene expression Source: Ensembl
    14. positive regulation of phagocytosis Source: Ensembl
    15. positive regulation of substrate adhesion-dependent cell spreading Source: Ensembl
    16. protein export from nucleus Source: Ensembl
    17. protein folding Source: InterPro
    18. protein localization to nucleus Source: Ensembl
    19. protein stabilization Source: UniProtKB
    20. regulation of meiosis Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_201997. Scavenging by Class A Receptors.
    REACT_203806. ATF6-alpha activates chaperone genes.
    REACT_206877. Scavenging by Class F Receptors.
    REACT_209237. Calnexin/calreticulin cycle.

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 2

    Subcellular locationi

    Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen. Cytoplasmperinuclear region. Membrane
    Note: During oocyte maturation and after parthenogenetic activation accumulates in the plasma membrane region. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. external side of plasma membrane Source: Ensembl
    3. extracellular space Source: Ensembl
    4. MHC class I peptide loading complex Source: Ensembl
    5. nucleus Source: Ensembl
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. polysome Source: Ensembl
    8. sarcoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 417400CalreticulinPRO_0000004175Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi137 ↔ 163By similarity
    Modified residuei159 – 1591N6-acetyllysineBy similarity
    Modified residuei209 – 2091N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PaxDbiP28491.

    Expressioni

    Tissue specificityi

    In blastocyst expressed in all blastomeres (at protein level). In embryos, expressed in spleen, kidney, liver, fat, muscle, ovary, granulosa cells and cumulus cells.1 Publication

    Developmental stagei

    Expressed in immature GV-stage oocytes, mature MII-stage oocytes, parthenogenetically activated MII-stage oocytes and in pronuclear embryos (at protein level). During in vitro oocyte maturation, expression initially increases after 12 hours of culture, followed by a strong decline at 30 hours (MI stage) and 44 hours (MII stage). Expression remains constant in MII-stage oocytes after parthenogenetic activation, increasing in two- and four-cell parthenotes. Not detected in blastocyst stage embryos.1 Publication

    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

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000014615.

    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 – 417109C-domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi414 – 4174Prevents secretion from ERPROSITE-ProRule annotation

    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

    Sequence similaritiesi

    Belongs to the calreticulin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG305105.
    GeneTreeiENSGT00430000030841.
    HOGENOMiHOG000192435.
    KOiK08057.
    OMAiVKLFPDG.
    OrthoDBiEOG77126Z.
    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. 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.

    P28491-1 [UniParc]FASTAAdd to Basket

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    MLLPVPLLLG LVGLAAAEPT IYFKEQFLDG DGWTDRWIES KHKPDFGRFV    50
    LSSGKFYGDQ EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE 100
    QNIDCGGGYV KLFPDGLDQT DMHGDSEYNI MFGPDICGPG TKKVHVIFNY 150
    KGKNVLINKD IRCKDDEFTH LYTLIVRPDN TYEVKIDNSQ VESGSLEDDW 200
    DFLPPKKIKD PDAVKPEDWD ERAKIDDPTD SKPEDWDKPE HIPDPDAKKP 250
    EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 300
    PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT 350
    KAAEKQMKDK QDEEQRLKEE EEEKKRKEEE EVDKEDEEDK DEDEEEEDEK 400
    EEEEEEDAAA GQAKDEL 417
    Length:417
    Mass (Da):48,288
    Last modified:May 16, 2012 - v3
    Checksum:i31A9E4CC95F2D54F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151A → V in CAA23142. (PubMed:8672129)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GQ984146 mRNA. Translation: ADD52600.1.
    CU463133 Genomic DNA. No translation available.
    F14591 mRNA. Translation: CAA23142.1.
    PIRiB33208.
    RefSeqiNP_001167604.1. NM_001174133.1.
    UniGeneiSsc.48945.

    Genome annotation databases

    EnsembliENSSSCT00000015020; ENSSSCP00000014615; ENSSSCG00000013746.
    GeneIDi100381266.
    KEGGissc:100381266.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GQ984146 mRNA. Translation: ADD52600.1 .
    CU463133 Genomic DNA. No translation available.
    F14591 mRNA. Translation: CAA23142.1 .
    PIRi B33208.
    RefSeqi NP_001167604.1. NM_001174133.1.
    UniGenei Ssc.48945.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000014615.

    Proteomic databases

    PaxDbi P28491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000015020 ; ENSSSCP00000014615 ; ENSSSCG00000013746 .
    GeneIDi 100381266.
    KEGGi ssc:100381266.

    Organism-specific databases

    CTDi 811.

    Phylogenomic databases

    eggNOGi NOG305105.
    GeneTreei ENSGT00430000030841.
    HOGENOMi HOG000192435.
    KOi K08057.
    OMAi VKLFPDG.
    OrthoDBi EOG77126Z.
    TreeFami TF338438.

    Enzyme and pathway databases

    Reactomei REACT_201997. Scavenging by Class A Receptors.
    REACT_203806. ATF6-alpha activates chaperone genes.
    REACT_206877. Scavenging by Class F Receptors.
    REACT_209237. Calnexin/calreticulin cycle.

    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. "Involvement of ER-calreticulin-Ca2+ signaling in the regulation of porcine oocyte meiotic maturation and maternal gene expression."
      Zhang D.X., Li X.P., Sun S.C., Shen X.H., Cui X.S., Kim N.H.
      Mol. Reprod. Dev. 77:462-471(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Oocyte.
    2. Porcine genome sequencing project
      Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
      Winteroe A.K., Fredholm M., Davies W.
      Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-105.
      Tissue: Small intestine.
    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 18-32, SUBCELLULAR LOCATION.
      Tissue: Uterus.

    Entry informationi

    Entry nameiCALR_PIG
    AccessioniPrimary (citable) accession number: P28491
    Secondary accession number(s): D4N5N1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: May 16, 2012
    Last modified: October 1, 2014
    This is version 95 of the entry and version 3 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