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P29413

- CALR_DROME

UniProt

P29413 - CALR_DROME

Protein

Calreticulin

Gene

Crc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      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 sitei109 – 1091CarbohydrateBy similarity
    Binding sitei111 – 1111CarbohydrateBy similarity
    Binding sitei128 – 1281CarbohydrateBy similarity
    Binding sitei135 – 1351CarbohydrateBy similarity
    Binding sitei317 – 3171CarbohydrateBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. brain morphogenesis Source: FlyBase
    2. central nervous system development Source: FlyBase
    3. imaginal disc-derived wing morphogenesis Source: FlyBase
    4. locomotion involved in locomotory behavior Source: FlyBase
    5. neurogenesis Source: FlyBase
    6. olfactory behavior Source: FlyBase
    7. peripheral nervous system development Source: FlyBase
    8. protein folding Source: InterPro
    9. sleep Source: FlyBase
    10. startle response Source: FlyBase

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    Calcium, Lectin, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_180278. Calnexin/calreticulin cycle.
    REACT_93794. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calreticulin
    Gene namesi
    Name:Crc
    ORF Names:CG9429
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0005585. Crc.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. extracellular space Source: FlyBase
    3. fusome Source: FlyBase
    4. lipid particle Source: FlyBase

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 406389CalreticulinPRO_0000004182Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi105 ↔ 137By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP29413.
    PRIDEiP29413.

    Expressioni

    Gene expression databases

    BgeeiP29413.

    Interactioni

    Protein-protein interaction databases

    BioGridi66325. 89 interactions.
    DIPiDIP-19046N.
    IntActiP29413. 3 interactions.
    MINTiMINT-755481.

    Structurei

    3D structure databases

    ProteinModelPortaliP29413.
    SMRiP29413. Positions 21-365.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati191 – 202121-1Add
    BLAST
    Repeati210 – 221121-2Add
    BLAST
    Repeati227 – 238121-3Add
    BLAST
    Repeati244 – 255121-4Add
    BLAST
    Repeati259 – 269112-1Add
    BLAST
    Repeati273 – 283112-2Add
    BLAST
    Repeati287 – 297112-3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni191 – 255654 X approximate repeatsAdd
    BLAST
    Regioni259 – 297393 X approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi353 – 40250Asp/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.
    GeneTreeiENSGT00430000030841.
    InParanoidiP29413.
    KOiK08057.
    OMAiKNWVYSE.
    OrthoDBiEOG77126Z.
    PhylomeDBiP29413.

    Family and domain databases

    Gene3Di2.60.120.200. 2 hits.
    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. 3 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P29413-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMWCKTVIVL LATVGFISAE VYLKENFDNE NWEDTWIYSK HPGKEFGKFV    50
    LTPGTFYNDA EADKGIQTSQ DARFYAASRK FDGFSNEDKP LVVQFSVKHE 100
    QNIDCGGGYV KLFDCSLDQT DMHGESPYEI MFGPDICGPG TKKVHVIFSY 150
    KGKNHLISKD IRCKDDVYTH FYTLIVRPDN TYEVLIDNEK VESGNLEDDW 200
    DFLAPKKIKD PTATKPEDWD DRATIPDPDD KKPEDWDKPE HIPDPDATKP 250
    EDWDDEMDGE WEPPMIDNPE FKGEWQPKQL DNPNYKGAWE HPEIANPEYV 300
    PDDKLYLRKE ICTLGFDLWQ VKSGTIFDNV LITDDVELAA KAAAEVKNTQ 350
    AGEKKMKEAQ DEVQRKKDEE EAKKASDKDD EDEDDDDEEK DDESKQDKDQ 400
    SEHDEL 406
    Length:406
    Mass (Da):46,808
    Last modified:October 1, 1993 - v2
    Checksum:i65D72C69D0BEC427
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071G → A AA sequence (PubMed:2365822)Curated
    Sequence conflicti184 – 1841V → L AA sequence (PubMed:2365822)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64461 Genomic DNA. Translation: CAA45791.1.
    AE014297 Genomic DNA. Translation: AAF54416.1.
    PIRiA56637.
    RefSeqiNP_001262430.1. NM_001275501.1.
    NP_524293.2. NM_079569.5.
    UniGeneiDm.2457.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082103; FBpp0081581; FBgn0005585.
    GeneIDi41166.
    KEGGidme:Dmel_CG9429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64461 Genomic DNA. Translation: CAA45791.1 .
    AE014297 Genomic DNA. Translation: AAF54416.1 .
    PIRi A56637.
    RefSeqi NP_001262430.1. NM_001275501.1.
    NP_524293.2. NM_079569.5.
    UniGenei Dm.2457.

    3D structure databases

    ProteinModelPortali P29413.
    SMRi P29413. Positions 21-365.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66325. 89 interactions.
    DIPi DIP-19046N.
    IntActi P29413. 3 interactions.
    MINTi MINT-755481.

    Proteomic databases

    PaxDbi P29413.
    PRIDEi P29413.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082103 ; FBpp0081581 ; FBgn0005585 .
    GeneIDi 41166.
    KEGGi dme:Dmel_CG9429.

    Organism-specific databases

    CTDi 41166.
    FlyBasei FBgn0005585. Crc.

    Phylogenomic databases

    eggNOGi NOG305105.
    GeneTreei ENSGT00430000030841.
    InParanoidi P29413.
    KOi K08057.
    OMAi KNWVYSE.
    OrthoDBi EOG77126Z.
    PhylomeDBi P29413.

    Enzyme and pathway databases

    Reactomei REACT_180278. Calnexin/calreticulin cycle.
    REACT_93794. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi Crc. drosophila.
    GenomeRNAii 41166.
    NextBioi 822514.
    PROi P29413.

    Gene expression databases

    Bgeei P29413.

    Family and domain databases

    Gene3Di 2.60.120.200. 2 hits.
    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. 3 hits.
    PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a Drosophila melanogaster gene encoding a calreticulin homologue."
      Smith M.J.
      DNA Seq. 3:247-250(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia 'memory molecule'."
      McCauliffe D.P., Zappi E., Lieu T.S., Michalak M., Sontheimer R.D., Capra J.D.
      J. Clin. Invest. 86:332-335(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 91-124 AND 182-220.

    Entry informationi

    Entry nameiCALR_DROME
    AccessioniPrimary (citable) accession number: P29413
    Secondary accession number(s): Q9VHA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3