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Q8T9B6

- MESD_DROME

UniProt

Q8T9B6 - MESD_DROME

Protein

LDLR chaperone boca

Gene

boca

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 70 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wg pathway, since some LDLRs are coreceptors for the canonical Wnt pathway.1 Publication

    GO - Biological processi

    1. ER to Golgi vesicle-mediated transport Source: FlyBase
    2. low-density lipoprotein receptor particle metabolic process Source: FlyBase
    3. oogenesis Source: FlyBase
    4. proboscis development Source: FlyBase
    5. protein targeting to membrane Source: FlyBase
    6. Wnt signaling pathway Source: FlyBase

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LDLR chaperone boca
    Gene namesi
    Name:boca
    ORF Names:CG30498
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0004132. boca.

    Subcellular locationi

    Endoplasmic reticulum 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. apical part of cell Source: FlyBase
    2. cytoplasm Source: FlyBase
    3. endoplasmic reticulum lumen Source: FlyBase

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi49 – 491W → R in boca1; induces lethality. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 180162LDLR chaperone bocaPRO_0000385021Add
    BLAST

    Proteomic databases

    PaxDbiQ8T9B6.
    PRIDEiQ8T9B6.

    Expressioni

    Gene expression databases

    BgeeiQ8T9B6.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with Arrow and Yolkless.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi71878. 74 interactions.
    DIPiDIP-59112N.
    STRINGi7227.FBpp0088027.

    Structurei

    Secondary structure

    1
    180
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi94 – 10310
    Helixi106 – 12217
    Beta strandi127 – 1337
    Beta strandi136 – 1438
    Helixi144 – 1463
    Helixi147 – 1548
    Beta strandi160 – 1656
    Beta strandi168 – 1714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OFEX-ray2.29A/B88-172[»]
    3OFFX-ray2.00A89-172[»]
    ProteinModelPortaliQ8T9B6.
    SMRiQ8T9B6. Positions 31-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8T9B6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni93 – 16674Structured coreBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 1804Prevents secretion from ER

    Domaini

    The LDLR maturation activity resides in the N- and C-terminal unstructured regions.By similarity

    Sequence similaritiesi

    Belongs to the MESD family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG286690.
    GeneTreeiENSGT00390000000993.
    InParanoidiQ8T9B6.
    OMAiAIFLFKD.
    OrthoDBiEOG7XPZ76.
    PhylomeDBiQ8T9B6.

    Family and domain databases

    InterProiIPR019330. Mesoderm_development_cand-2.
    [Graphical view]
    PfamiPF10185. Mesd. 1 hit.
    [Graphical view]
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8T9B6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTRLVLLLL ALTPLVLAKK FKEEEKPAWA KKDIRDYSEA DLERLLDQWE    50
    EDEEPLEDDE LPEHLRPQPK LDLSNLDSKS PEDLLKVSKK GRTLMTFVSV 100
    TGNPTREESD TITKLWQTSL WNNHIQAERY MVDDNRAIFL FKDGTQAWDA 150
    KDFLIEQERC KGVTIENKEY PGVNAKKDEL 180
    Length:180
    Mass (Da):21,002
    Last modified:September 22, 2009 - v2
    Checksum:iB51E057C901A6546
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151L → V in AAL39985. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF59229.2.
    AY069840 mRNA. Translation: AAL39985.1.
    BT044294 mRNA. Translation: ACH92359.1.
    RefSeqiNP_724578.1. NM_165541.2.
    UniGeneiDm.14878.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088953; FBpp0088027; FBgn0004132.
    GeneIDi48986.
    KEGGidme:Dmel_CG30498.
    UCSCiCG30498-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF59229.2 .
    AY069840 mRNA. Translation: AAL39985.1 .
    BT044294 mRNA. Translation: ACH92359.1 .
    RefSeqi NP_724578.1. NM_165541.2.
    UniGenei Dm.14878.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OFE X-ray 2.29 A/B 88-172 [» ]
    3OFF X-ray 2.00 A 89-172 [» ]
    ProteinModelPortali Q8T9B6.
    SMRi Q8T9B6. Positions 31-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 71878. 74 interactions.
    DIPi DIP-59112N.
    STRINGi 7227.FBpp0088027.

    Proteomic databases

    PaxDbi Q8T9B6.
    PRIDEi Q8T9B6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088953 ; FBpp0088027 ; FBgn0004132 .
    GeneIDi 48986.
    KEGGi dme:Dmel_CG30498.
    UCSCi CG30498-RA. d. melanogaster.

    Organism-specific databases

    CTDi 48986.
    FlyBasei FBgn0004132. boca.

    Phylogenomic databases

    eggNOGi NOG286690.
    GeneTreei ENSGT00390000000993.
    InParanoidi Q8T9B6.
    OMAi AIFLFKD.
    OrthoDBi EOG7XPZ76.
    PhylomeDBi Q8T9B6.

    Miscellaneous databases

    EvolutionaryTracei Q8T9B6.
    GenomeRNAii 48986.
    NextBioi 839609.
    PROi Q8T9B6.

    Gene expression databases

    Bgeei Q8T9B6.

    Family and domain databases

    InterProi IPR019330. Mesoderm_development_cand-2.
    [Graphical view ]
    Pfami PF10185. Mesd. 1 hit.
    [Graphical view ]
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    4. "Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila."
      Culi J., Mann R.S.
      Cell 112:343-354(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ARROW AND YOLKLESS, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-49.

    Entry informationi

    Entry nameiMESD_DROME
    AccessioniPrimary (citable) accession number: Q8T9B6
    Secondary accession number(s): A1Z712
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3