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Q9SP22

- CALR_MAIZE

UniProt

Q9SP22 - CALR_MAIZE

Protein

Calreticulin

Gene

CRT

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (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 sitei115 – 1151CarbohydrateBy similarity
    Binding sitei117 – 1171CarbohydrateBy similarity
    Binding sitei134 – 1341CarbohydrateBy similarity
    Binding sitei141 – 1411CarbohydrateBy similarity
    Binding sitei324 – 3241CarbohydrateBy 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:CRT
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiQ9SP22.

    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 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 420395CalreticulinPRO_0000004191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9SP22.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SP22.
    SMRiQ9SP22. Positions 212-312.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati197 – 208121-1Add
    BLAST
    Repeati216 – 227121-2Add
    BLAST
    Repeati233 – 244121-3Add
    BLAST
    Repeati251 – 262121-4Add
    BLAST
    Repeati266 – 276112-1Add
    BLAST
    Repeati280 – 290112-2Add
    BLAST
    Repeati294 – 304112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni197 – 262664 X approximate repeatsAdd
    BLAST
    Regioni266 – 304393 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 biasi358 – 41659Asp/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.
    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.

    Q9SP22-1 [UniParc]FASTAAdd to Basket

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    MAIRKGSSYA VAALLALASV AAVAGEVFFQ EKFEDGWESR WVKSEWKKDE    50
    NMAGEWNHTS GKWNGDAEDK GIQTSEDYRF YAISAEYPEF SNKDKTLVLQ 100
    FSVKHEQKLD CGGGYVKLLG GDVDQKTLGG DTSYSIISRP DISRYSTKKV 150
    HTILTKDGKN HLIKKDVPCQ TDQLTHVYTF IIRPDATYSI LIDNEEKHTG 200
    SIYEHWDILP PKKIKDPEAK KPEDWDDKEY IPDPEDKKPE GYDDIPKEIP 250
    DPDAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKQKKIKNP NYQGKWKAPM 300
    IDNPDFKDDP YIYAFDSLKY IGIELWQVKS GTLFDNIIIT DDPALAKTFA 350
    EETWGKHKEA EKAAFDEAEK KKEEEDAAKG GDDEDDDLED EEDDEKADED 400
    KADSDAEDGK DSDDEKHDEL 420
    Length:420
    Mass (Da):47,940
    Last modified:May 1, 2000 - v1
    Checksum:iE73B7F43E7494735
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190454 mRNA. Translation: AAF01470.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190454 mRNA. Translation: AAF01470.1 .

    3D structure databases

    ProteinModelPortali Q9SP22.
    SMRi Q9SP22. Positions 212-312.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9SP22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei Q9SP22.

    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.
    PS00805. CALRETICULIN_REPEAT. 2 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression of the high capacity calcium-binding domain of calreticulin increases bioavailable calcium stores in plants."
      Wyatt S.E., Tsou P.-L., Robertson D.
      Transgenic Res. 11:1-10(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiCALR_MAIZE
    AccessioniPrimary (citable) accession number: Q9SP22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 86 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