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Q7Z1E6

- CALR_BOMMO

UniProt

Q7Z1E6 - CALR_BOMMO

Protein

Calreticulin

Gene

crt

Organism
Bombyx mori (Silk moth)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091CarbohydrateBy similarity
    Binding sitei111 – 1111CarbohydrateBy similarity
    Binding sitei128 – 1281CarbohydrateBy similarity
    Binding sitei135 – 1351CarbohydrateBy similarity
    Binding sitei317 – 3171CarbohydrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    Gene namesi
    Name:crtImported
    OrganismiBombyx mori (Silk moth)
    Taxonomic identifieri7091 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
    ProteomesiUP000005204: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 398379CalreticulinSequence AnalysisPRO_0000279696Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi105 ↔ 137By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed in fat bodies. Not expressed in midgut, silk gland, ovary or testis.2 Publications

    Inductioni

    Induced by disturbances in intracellular calcium levels caused by the chelators BAPTA-AM and EDTA, the endoplasmic reticulum calcium-ATPase inhibitor thapsigargin and by calcium. Not induced by the endoplasmic reticulum stress-inducing drugs brefeldin A, DTT and tunicamycin, or by heat stress and hydrogen peroxide.1 Publication

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ7Z1E6.
    SMRiQ7Z1E6. Positions 205-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 197178N-domainSequence AnalysisAdd
    BLAST
    Regioni191 – 255654 X approximate repeatsSequence AnalysisAdd
    BLAST
    Regioni198 – 308111P-domainSequence AnalysisAdd
    BLAST
    Regioni259 – 297393 X approximate repeatsSequence AnalysisAdd
    BLAST
    Regioni309 – 39890C-domainSequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi395 – 3984Prevents secretion from ERSequence Analysis

    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.Sequence Analysis

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    KOiK08057.

    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.

    Q7Z1E6-1 [UniParc]FASTAAdd to Basket

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    MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK    50
    LTAGKFFSDP EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE 100
    QDIDCGGGYL KVFDCKLEQK DMHGETPYEI MFGPDICGPG TKKVHVIFSY 150
    KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN TYEVLIDNEK VESGDLEADW 200
    DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE HIPDPDATKP 250
    EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT 300
    PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ 350
    EGEKKMKSEQ DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL 398
    Length:398
    Mass (Da):45,802
    Last modified:October 1, 2003 - v1
    Checksum:i0BC049839F5950EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361W → K AA sequence (PubMed:11280994)Curated
    Sequence conflicti41 – 411H → A AA sequence (PubMed:11280994)Curated
    Sequence conflicti45 – 451E → D AA sequence (PubMed:11280994)Curated
    Sequence conflicti47 – 471G → E AA sequence (PubMed:11280994)Curated
    Sequence conflicti49 – 491F → K AA sequence (PubMed:11280994)Curated
    Sequence conflicti205 – 2051N → P in BAC57964. 1 PublicationCurated
    Sequence conflicti285 – 2851Y → F in BAC57964. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY297158 mRNA. Translation: AAP50845.1.
    AB090887 mRNA. Translation: BAC57964.1.
    RefSeqiNP_001037075.1. NM_001043610.1.
    UniGeneiBmo.1394.

    Genome annotation databases

    GeneIDi692629.
    KEGGibmor:692629.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY297158 mRNA. Translation: AAP50845.1 .
    AB090887 mRNA. Translation: BAC57964.1 .
    RefSeqi NP_001037075.1. NM_001043610.1.
    UniGenei Bmo.1394.

    3D structure databases

    ProteinModelPortali Q7Z1E6.
    SMRi Q7Z1E6. Positions 205-305.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 692629.
    KEGGi bmor:692629.

    Organism-specific databases

    CTDi 45841.

    Phylogenomic databases

    KOi K08057.

    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 a cDNA encoding putative calreticulin from the silkworm, Bombyx mori."
      Kim S.R., Lee K.S., Kim I., Kang S.W., Nho S.K., Sohn H.D., Jin B.R.
      Int. J. Ind. Entomol. 6:93-97(2003)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Endoplasmic reticulum stress response of Bombyx mori calreticulin."
      Goo T.W., Park S., Jin B.R., Yun E.Y., Kim I., Nho S.-K., Kang S.-W., Kwon O.-Y.
      Mol. Biol. Rep. 32:133-139(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    3. Takahashi T., Yamashita T.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: p50T.
      Tissue: Fat bodyImported.
    4. "Protein database for several tissues derived from five instar of silkworm."
      Zhong B.-X.
      Yi Chuan Xue Bao 28:217-224(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-49.
      Strain: Xinhang X Keming1 Publication.
      Tissue: Body wall1 Publication and Fat body1 Publication.

    Entry informationi

    Entry nameiCALR_BOMMO
    AccessioniPrimary (citable) accession number: Q7Z1E6
    Secondary accession number(s): P82199, Q869E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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