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O04153

- CALR3_ARATH

UniProt

O04153 - CALR3_ARATH

Protein

Calreticulin-3

Gene

CRT3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      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. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei118 – 1181CarbohydrateBy similarity
    Binding sitei120 – 1201CarbohydrateBy similarity
    Binding sitei137 – 1371CarbohydrateBy similarity
    Binding sitei144 – 1441CarbohydrateBy similarity
    Binding sitei327 – 3271CarbohydrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. anthocyanin-containing compound metabolic process Source: TAIR
    2. calcium ion homeostasis Source: TAIR
    3. defense response signaling pathway, resistance gene-independent Source: TAIR
    4. defense response to bacterium Source: TAIR
    5. plant-type hypersensitive response Source: TAIR
    6. protein folding Source: TAIR

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin-3
    Alternative name(s):
    Protein PRIORITY IN SWEET LIFE 1
    Gene namesi
    Name:CRT3
    Ordered Locus Names:At1g08450
    ORF Names:T27G7.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G08450.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: TAIR
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. endoplasmic reticulum membrane Source: TAIR

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Loss of seedling growth inhibition in response to the pathogen-associated molecular pattern (PAMP) elf18 and increased susceptibility to phytopathogenic bacteria.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671P → L in psl1-1; no effect on EFR accumulation, but decreased response to the PAMP elf18. 1 Publication
    Mutagenesisi115 – 1151G → D in crt3-3; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi142 – 1421G → E in crt3-4; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi147 – 1471G → E in crt3-5; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi179 – 1791H → Y in crt3-6; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi203 – 2031G → D in crt3-7; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi244 – 2441G → S in psl1-3; no effect on EFR accumulation, but decreased response to the PAMP elf18. 1 Publication
    Mutagenesisi293 – 2931P → S in crt3-10; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. 1 Publication
    Mutagenesisi335 – 3351S → L in psl1-4; loss of EFR accumulation and loss of response to the PAMP elf18. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 424396Calreticulin-3PRO_0000004186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi114 ↔ 146By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO04153.
    PRIDEiO04153.

    Expressioni

    Gene expression databases

    ArrayExpressiO04153.
    GenevestigatoriO04153.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48930N.

    Structurei

    3D structure databases

    ProteinModelPortaliO04153.
    SMRiO04153. Positions 30-385.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati200 – 211121-1Add
    BLAST
    Repeati219 – 230121-2Add
    BLAST
    Repeati236 – 247121-3Add
    BLAST
    Repeati254 – 265121-4Add
    BLAST
    Repeati269 – 279112-1Add
    BLAST
    Repeati283 – 293112-2Add
    BLAST
    Repeati297 – 307112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 265664 X approximate repeatsAdd
    BLAST
    Regioni269 – 307393 X approximate repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi421 – 4244Prevents secretion from ERPROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi361 – 41454Arg/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

    eggNOGiNOG295283.
    HOGENOMiHOG000192435.
    InParanoidiO04153.
    KOiK08057.
    OMAiFGSMYTD.
    PhylomeDBiO04153.

    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.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: O04153-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGLPQNKLSF FCFFFLVSVL TLAPLAFSEI FLEEHFEGGW KSRWVLSDWK    50
    RNEGKAGTFK HTAGKWPGDP DNKGIQTYND AKHYAISAKI PEFSNKNRTL 100
    VVQYSVKIEQ DIECGGAYIK LLSGYVNQKQ FGGDTPYSLM FGPDICGTQT 150
    KKLHVIVSYQ GQNYPIKKDL QCETDKLNHF YTFILRPDAS YSVLVDNKER 200
    EFGSMYTDWD ILPPRKIKVK NAKKPEDWDD REYIDDPNDV KPEGFDSIPR 250
    EIPDRKAKEP EDWDEEENGL WEPPKIPNSA YKGPWKAKRI KNPNYKGKWK 300
    NPWIDNPEFE DDPDLYVLKS IKYAGIEVWQ VKAGSIFDNI LICDDPAYAR 350
    SIVDDYFAQH RESEKELFAE AEKERKARED EEARIAREEG ERRRKERDHR 400
    YGDRRRRYKR PNPRDYMDDY HDEL 424
    Length:424
    Mass (Da):49,844
    Last modified:February 5, 2008 - v2
    Checksum:i64445A06359F0B8C
    GO

    Sequence cautioni

    The sequence AAF22902.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791S → F in AAC49697. (PubMed:9159940)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66345 mRNA. Translation: AAC49697.1.
    AC006932 Genomic DNA. Translation: AAF22902.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE28291.1.
    AY056320 mRNA. Translation: AAL07169.1.
    RefSeqiNP_563816.1. NM_100718.4. [O04153-1]
    UniGeneiAt.24804.

    Genome annotation databases

    EnsemblPlantsiAT1G08450.1; AT1G08450.1; AT1G08450. [O04153-1]
    GeneIDi837365.
    KEGGiath:AT1G08450.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66345 mRNA. Translation: AAC49697.1 .
    AC006932 Genomic DNA. Translation: AAF22902.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE28291.1 .
    AY056320 mRNA. Translation: AAL07169.1 .
    RefSeqi NP_563816.1. NM_100718.4. [O04153-1 ]
    UniGenei At.24804.

    3D structure databases

    ProteinModelPortali O04153.
    SMRi O04153. Positions 30-385.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48930N.

    Proteomic databases

    PaxDbi O04153.
    PRIDEi O04153.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G08450.1 ; AT1G08450.1 ; AT1G08450 . [O04153-1 ]
    GeneIDi 837365.
    KEGGi ath:AT1G08450.

    Organism-specific databases

    TAIRi AT1G08450.

    Phylogenomic databases

    eggNOGi NOG295283.
    HOGENOMi HOG000192435.
    InParanoidi O04153.
    KOi K08057.
    OMAi FGSMYTD.
    PhylomeDBi O04153.

    Gene expression databases

    ArrayExpressi O04153.
    Genevestigatori O04153.

    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. "Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana."
      Nelson D.E., Glaunsinger B., Bohnert H.J.
      Plant Physiol. 114:29-37(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Receptor quality control in the endoplasmic reticulum for plant innate immunity."
      Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H., Dong X., Robatzek S., Schulze-Lefert P.
      EMBO J. 28:3439-3449(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PRO-67; GLY-244 AND SER-335.
    6. "Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR."
      Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D., Zipfel C., Jones J.D.
      Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-115; GLY-142; GLY-147; HIS-179; GLY-203 AND PRO-293, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCALR3_ARATH
    AccessioniPrimary (citable) accession number: O04153
    Secondary accession number(s): Q93ZR4, Q9SJE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3