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Q9XF98

- CALR_PRUAR

UniProt

Q9XF98 - CALR_PRUAR

Protein

Calreticulin

Gene
N/A
Organism
Prunus armeniaca (Apricot) (Armeniaca vulgaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Nov 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 sitei114 – 1141CarbohydrateBy similarity
    Binding sitei116 – 1161CarbohydrateBy similarity
    Binding sitei133 – 1331CarbohydrateBy similarity
    Binding sitei140 – 1401CarbohydrateBy similarity
    Binding sitei323 – 3231CarbohydrateBy 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
    OrganismiPrunus armeniaca (Apricot) (Armeniaca vulgaris)
    Taxonomic identifieri36596 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

    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
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 421399CalreticulinPRO_0000004194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi110 ↔ 142By similarity
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9XF98.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XF98.
    SMRiQ9XF98. Positions 210-311.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati196 – 207121-1Add
    BLAST
    Repeati215 – 226121-2Add
    BLAST
    Repeati232 – 243121-3Add
    BLAST
    Repeati250 – 261121-4Add
    BLAST
    Repeati265 – 275112-1Add
    BLAST
    Repeati279 – 289112-2Add
    BLAST
    Repeati293 – 303112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni196 – 261664 X approximate repeatsAdd
    BLAST
    Regioni265 – 303393 X approximate repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi418 – 4214Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi357 – 41761Asp/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.

    Q9XF98-1 [UniParc]FASTAAdd to Basket

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    MAFRVPNSSL LSLILLSLLA IASAKVFFEE RFEDGWDKRW VTSEWKKDEN    50
    LAGEWNYTSG KWNGDPNDKG IQTSEDYRFY AISAEFPEFS NKDKTLVFQF 100
    SVKHEQKLDC GGGYIKLLSG DVDQKKFGGD TPYSIMFGPD ICGYSTKKVH 150
    AILNYNNTNN LIKKDVPCET DQLTHVYTFI IRPDATYSIL IDNLEKQTGS 200
    LYSDWDLLPA KKIKDPEAKK PEDWEDQEYI PDPEDKKPEG YDDIPKEITD 250
    PDAKKPEDWD DEEDGEWTAP TIPNPEYKGE WKPKKIKNPN FKGKWKAPLI 300
    DNPEFKDDPE LYVYPNLKYV GIELWQVKSG TLFDNILITD EPEYAKQLAE 350
    ETWGKQKDAE KAAFEELEKK LQEEESKEDP VDSDAEDDDN EAEDGEESDS 400
    ESKPDSTEES AETEAEKHDE L 421
    Length:421
    Mass (Da):48,416
    Last modified:November 1, 1999 - v1
    Checksum:i4F5F94CBAA6C6690
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134733 mRNA. Translation: AAD32207.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134733 mRNA. Translation: AAD32207.1 .

    3D structure databases

    ProteinModelPortali Q9XF98.
    SMRi Q9XF98. Positions 210-311.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9XF98.

    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. "Molecular cloning and nucleotide sequence of a calreticulin from apricot (Prunus armeniaca cv. Bergeron)."
      Mbeguie-A-Mbeguie D., Fils-Lycaon B.R.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Bergeron.
      Tissue: Endocarp and Mesocarp.

    Entry informationi

    Entry nameiCALR_PRUAR
    AccessioniPrimary (citable) accession number: Q9XF98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 84 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