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Q9ZPP1

- CALR_BERST

UniProt

Q9ZPP1 - CALR_BERST

Protein

Calreticulin

Gene
N/A
Organism
Berberis stolonifera (Barberry)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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 sitei112 – 1121CarbohydrateBy similarity
    Binding sitei114 – 1141CarbohydrateBy 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. protein folding Source: InterPro

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    OrganismiBerberis stolonifera (Barberry)
    Taxonomic identifieri33814 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesBerberidaceaeBerberidoideaeBerberis

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    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
    Chaini? – 416CalreticulinPRO_0000004187
    Signal peptidei1 – ?Sequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi108 ↔ 140By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZPP1.
    SMRiQ9ZPP1. Positions 209-282.
    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
    Motifi413 – 4164Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi355 – 41157Asp/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

    Family and domain databases

    Gene3Di2.10.250.10. 1 hit.
    2.60.120.200. 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. 2 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9ZPP1-1 [UniParc]FASTAAdd to Basket

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    MAIAERRSRS HLALRVRDRV SAEVFFEERF EDGWESKWVK SDWKRDENMA    50
    GEWNFTSGKW NGDANDKGIQ TSEDYRFYAI SAAFPEFSNK GKTLVFQFSV 100
    KHEQKLDCGG GYMKLLSGDV DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI 150
    LTKGETNHLI KKDVPCETDQ LTHVYTFILR PDASYSILID NVEKQSGSVY 200
    TDWDILPPKQ IKDPEAKKPE DWEDKEYIPD PEDKKPEGYD DIPKEITDPE 250
    AKKPEDWDDE EDGEWTAPTI PNPDYKGEWK PKKIKNPNFK GKWKAPMIDN 300
    PDFKDDPDIY VFPKLKYVGI ELWQVKSGTM FDNVLICDDP DYAKKLAEET 350
    WGKNKDAEKA AFDEAEKKKE EEEAKDDPTE SDDEKPDEEG ESDGEGDDES 400
    KDIDNEEDDE DVHDEL 416
    Length:416
    Mass (Da):47,927
    Last modified:May 1, 1999 - v1
    Checksum:i08AC46885BF69114
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052040 mRNA. Translation: AAD17490.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052040 mRNA. Translation: AAD17490.1 .

    3D structure databases

    ProteinModelPortali Q9ZPP1.
    SMRi Q9ZPP1. Positions 209-282.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.10.250.10. 1 hit.
    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. 2 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Calreticulin from Berberis stolonifera."
      Chou W.-M., Kutchan T.M.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiCALR_BERST
    AccessioniPrimary (citable) accession number: Q9ZPP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 77 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