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Q9STD3

- CALR_CHLRE

UniProt

Q9STD3 - CALR_CHLRE

Protein

Calreticulin

Gene
N/A
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 sitei110 – 1101CarbohydrateBy similarity
    Binding sitei112 – 1121CarbohydrateBy similarity
    Binding sitei131 – 1311CarbohydrateBy similarity
    Binding sitei138 – 1381CarbohydrateBy similarity
    Binding sitei321 – 3211CarbohydrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. anthocyanin-containing compound metabolic process Source: EnsemblPlants/Gramene
    2. calcium ion homeostasis Source: EnsemblPlants/Gramene
    3. defense response signaling pathway, resistance gene-independent Source: EnsemblPlants/Gramene
    4. defense response to bacterium Source: EnsemblPlants/Gramene
    5. plant-type hypersensitive response Source: EnsemblPlants/Gramene
    6. protein folding Source: InterPro
    7. response to cadmium ion Source: EnsemblPlants/Gramene
    8. response to oxidative stress Source: EnsemblPlants/Gramene
    9. response to salt stress Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
    Taxonomic identifieri3055 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. apoplast Source: EnsemblPlants/Gramene
    2. chloroplast Source: EnsemblPlants/Gramene
    3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    4. endoplasmic reticulum membrane Source: EnsemblPlants/Gramene
    5. mitochondrion Source: EnsemblPlants/Gramene
    6. plasmodesma Source: EnsemblPlants/Gramene
    7. vacuolar membrane Source: EnsemblPlants/Gramene

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 420402CalreticulinPRO_0000004189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi106 ↔ 140By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ9STD3.
    ProMEXiQ9STD3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9STD3.
    SMRiQ9STD3. Positions 209-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati194 – 205121-1Add
    BLAST
    Repeati213 – 224121-2Add
    BLAST
    Repeati230 – 241121-3Add
    BLAST
    Repeati248 – 259121-4Add
    BLAST
    Repeati263 – 273112-1Add
    BLAST
    Repeati277 – 287112-2Add
    BLAST
    Repeati291 – 301112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni194 – 259664 X approximate repeatsAdd
    BLAST
    Regioni263 – 301393 X approximate repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi417 – 4204Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi355 – 41460Asp/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.
    KOiK08057.
    OMAiRWVNSKH.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    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. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9STD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKWGVVAVLA TLVVAASAKD YFKETFDGSW ADRWTKSSWK VSDGSAGEFK    50
    LTAGKWYGDA EADKGIQTGP DSKFFAISAP LATVFDNTGK DTVVQFSVKH 100
    EQDLDCGGGY IKVVPATSEK QMGEFGGDTP YSIMFGPDIC GYSTRKVHVI 150
    LTYKGKNYLI KKDIKAETDQ LTHVYTLVIK PDNTYQVLID LKEVASGSLY 200
    EDWDMLPPKT IKDPKASKPE DWDEREEIAD PEDKKPEGWD DIPATIADKD 250
    AKKPEDWDDE EDGTWEPPMI PNPEYKGEWK AKMIKNPAYK GIWVAPDIDN 300
    PDYVHDDKLY NFKDLKFVGF ELWQVKSGSI FDNILVTDDL EAAKKFAEDT 350
    WGKHKDEEKA MFDKVKKEED EKKAKDAPPP PVDAEAAEEE DDEYEDKEEP 400
    SGMGSIKIPK EEEESGHDEL 420
    Length:420
    Mass (Da):47,328
    Last modified:May 1, 2000 - v1
    Checksum:iDD3BA3AFFBF61C9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000765 mRNA. Translation: CAB54526.1.
    RefSeqiXP_001689661.1. XM_001689609.1.
    UniGeneiCre.14231.

    Genome annotation databases

    GeneIDi5715514.
    KEGGicre:CHLREDRAFT_78954.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ000765 mRNA. Translation: CAB54526.1 .
    RefSeqi XP_001689661.1. XM_001689609.1.
    UniGenei Cre.14231.

    3D structure databases

    ProteinModelPortali Q9STD3.
    SMRi Q9STD3. Positions 209-306.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9STD3.
    ProMEXi Q9STD3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5715514.
    KEGGi cre:CHLREDRAFT_78954.

    Phylogenomic databases

    eggNOGi NOG305105.
    KOi K08057.
    OMAi RWVNSKH.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    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. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a cDNA encoding Chlamydomonas reinhardtii calreticulin."
      Zuppini A., Kaydamov C.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 137c / CC-125.

    Entry informationi

    Entry nameiCALR_CHLRE
    AccessioniPrimary (citable) accession number: Q9STD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3