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Q9ERE7

- MESD_MOUSE

UniProt

Q9ERE7 - MESD_MOUSE

Protein

LDLR chaperone MESD

Gene

Mesdc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction.2 Publications

    GO - Molecular functioni

    1. low-density lipoprotein particle receptor binding Source: MGI
    2. protein binding Source: IntAct

    GO - Biological processi

    1. mesoderm development Source: UniProtKB
    2. protein folding Source: UniProtKB
    3. protein localization to cell surface Source: MGI
    4. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LDLR chaperone MESD
    Alternative name(s):
    Mesoderm development candidate 2
    Mesoderm development protein
    Gene namesi
    Name:Mesdc2
    Synonyms:Mesd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1891421. Mesdc2.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Disruption of embryonic polarity and mesoderm differentiation, likely resulting from a primary defect in Wnt signaling.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 224195LDLR chaperone MESDPRO_0000096444Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9ERE7.
    PaxDbiQ9ERE7.
    PRIDEiQ9ERE7.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00349285.
    Q9ERE7.

    PTM databases

    PhosphoSiteiQ9ERE7.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, but not in skeletal muscles.1 Publication

    Gene expression databases

    ArrayExpressiQ9ERE7.
    BgeeiQ9ERE7.
    CleanExiMM_MESDC2.
    GenevestigatoriQ9ERE7.

    Interactioni

    Subunit structurei

    Monomer. Interacts with LRP5; the interaction prevents LRP5 from forming aggregates and chaperones LRP6 to the plasma membrane. Interacts with LRP6; the interaction prevents LRP6 from forming aggregates and chaperones LRP6 to the plasma membrane.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Lrp4Q8VI562EBI-6662606,EBI-2106160

    Protein-protein interaction databases

    BioGridi212555. 1 interaction.
    DIPiDIP-59114N.
    IntActiQ9ERE7. 4 interactions.
    STRINGi10090.ENSMUSP00000091768.

    Structurei

    Secondary structure

    1
    224
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni43 – 453
    Helixi47 – 493
    Helixi51 – 6515
    Beta strandi87 – 904
    Helixi93 – 997
    Beta strandi105 – 1139
    Helixi117 – 13317
    Beta strandi138 – 1425
    Beta strandi147 – 1537
    Helixi155 – 1573
    Helixi158 – 1669
    Beta strandi168 – 1703
    Beta strandi171 – 1766
    Beta strandi179 – 1813
    Beta strandi183 – 1864
    Helixi195 – 2039
    Beta strandi208 – 2103
    Helixi211 – 2177

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I9SNMR-A89-184[»]
    2KGLNMR-A30-224[»]
    2KMINMR-A41-185[»]
    2RQKNMR-A45-184[»]
    2RQMNMR-A45-184[»]
    3OFHX-ray2.01A/B98-183[»]
    ProteinModelPortaliQ9ERE7.
    SMRiQ9ERE7. Positions 30-224.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ERE7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 155155Chaperone domainAdd
    BLAST
    Regioni156 – 19540Escort domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi221 – 2244Prevents secretion from ER

    Domaini

    The chaperone domain provides a folding template for proper folding of the beta-propeller (BP) domains of LRP5/6.1 Publication
    The escort domain ensures LRP5/6 safe-trafficking from the ER to the Golgi by preventing premature ligand-binding.1 Publication

    Sequence similaritiesi

    Belongs to the MESD family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG286690.
    GeneTreeiENSGT00390000000993.
    HOGENOMiHOG000230558.
    InParanoidiQ91WK8.
    OMAiNQERCAD.
    OrthoDBiEOG7XPZ76.
    PhylomeDBiQ9ERE7.
    TreeFamiTF315614.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    Q9ERE7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASRWLRAV LLFLCASDLL LLPPPNAYAA DTPGEATPPP RKKKDIRDYN    50
    DADMARLLEQ WEKDDDIEEG DLPEHKRPSA PIDFSKLDPG KPESILKMTK 100
    KGKTLMMFVT VSGNPTEKET EEITSLWQGS LFNANYDVQR FIVGSDRAIF 150
    MLRDGSYAWE IKDFLVSQDR CAEVTLEGQM YPGKGGGSKE KNKTKPEKAK 200
    KKEGDPKPRA SKEDNRAGSR REDL 224
    Length:224
    Mass (Da):25,207
    Last modified:March 1, 2001 - v1
    Checksum:i6A94D5B315AE1D66
    GO

    Sequence cautioni

    The sequence BAC36476.1 differs from that shown. Reason: Frameshift at position 207.
    The sequence AAH14742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061P → R in BAC36471. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF311213 Genomic DNA. Translation: AAG33621.1.
    AK008735 mRNA. Translation: BAB25865.1.
    AK031949 mRNA. Translation: BAC27617.1.
    AK076760 mRNA. Translation: BAC36471.1.
    AK076773 mRNA. Translation: BAC36476.1. Frameshift.
    BC014742 mRNA. Translation: AAH14742.1. Different initiation.
    CCDSiCCDS21415.1.
    RefSeqiNP_075892.3. NM_023403.3.
    UniGeneiMm.117365.

    Genome annotation databases

    EnsembliENSMUST00000094215; ENSMUSP00000091768; ENSMUSG00000038503.
    GeneIDi67943.
    KEGGimmu:67943.
    UCSCiuc009idx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF311213 Genomic DNA. Translation: AAG33621.1 .
    AK008735 mRNA. Translation: BAB25865.1 .
    AK031949 mRNA. Translation: BAC27617.1 .
    AK076760 mRNA. Translation: BAC36471.1 .
    AK076773 mRNA. Translation: BAC36476.1 . Frameshift.
    BC014742 mRNA. Translation: AAH14742.1 . Different initiation.
    CCDSi CCDS21415.1.
    RefSeqi NP_075892.3. NM_023403.3.
    UniGenei Mm.117365.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I9S NMR - A 89-184 [» ]
    2KGL NMR - A 30-224 [» ]
    2KMI NMR - A 41-185 [» ]
    2RQK NMR - A 45-184 [» ]
    2RQM NMR - A 45-184 [» ]
    3OFH X-ray 2.01 A/B 98-183 [» ]
    ProteinModelPortali Q9ERE7.
    SMRi Q9ERE7. Positions 30-224.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212555. 1 interaction.
    DIPi DIP-59114N.
    IntActi Q9ERE7. 4 interactions.
    STRINGi 10090.ENSMUSP00000091768.

    PTM databases

    PhosphoSitei Q9ERE7.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00349285.
    Q9ERE7.

    Proteomic databases

    MaxQBi Q9ERE7.
    PaxDbi Q9ERE7.
    PRIDEi Q9ERE7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000094215 ; ENSMUSP00000091768 ; ENSMUSG00000038503 .
    GeneIDi 67943.
    KEGGi mmu:67943.
    UCSCi uc009idx.2. mouse.

    Organism-specific databases

    CTDi 23184.
    MGIi MGI:1891421. Mesdc2.

    Phylogenomic databases

    eggNOGi NOG286690.
    GeneTreei ENSGT00390000000993.
    HOGENOMi HOG000230558.
    InParanoidi Q91WK8.
    OMAi NQERCAD.
    OrthoDBi EOG7XPZ76.
    PhylomeDBi Q9ERE7.
    TreeFami TF315614.

    Miscellaneous databases

    EvolutionaryTracei Q9ERE7.
    NextBioi 326030.
    PROi Q9ERE7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ERE7.
    Bgeei Q9ERE7.
    CleanExi MM_MESDC2.
    Genevestigatori Q9ERE7.

    Family and domain databases

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

    Publicationsi

    1. "Identification of mesoderm development (mesd) candidate genes by comparative mapping and genome sequence analysis."
      Wines M.E., Lee L., Katari M.S., Zhang L., DeRossi C., Shi Y., Perkins S., Feldman M., McCombie W.R., Holdener B.C.
      Genomics 72:88-98(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129/SvJ.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata, Stomach and Testis.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity."
      Hsieh J.-C., Lee L., Zhang L., Wefer S., Brown K., DeRossi C., Wines M.E., Rosenquist T., Holdener B.C.
      Cell 112:355-367(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRP5 AND LRP6, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    5. "The solution structure of the core of mesoderm development (MESD), a chaperone for members of the LDLR-family."
      Kohler C., Andersen O.M., Diehl A., Krause G., Schmieder P., Oschkinat H.
      J. Struct. Funct. Genomics 7:131-138(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 89-184, SUBUNIT.
    6. "NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6."
      Chen J., Li Q., Liu C.C., Zhou B., Bu G., Wang J.
      J. Biomol. NMR 47:283-288(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 41-185.
    7. "Two structural and functional domains of MESD required for proper folding and trafficking of LRP5/6."
      Chen J., Liu C.C., Li Q., Nowak C., Bu G., Wang J.
      Structure 19:313-323(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 45-184, FUNCTION, DOMAINS CHAPERONE AND ESCORT.
    8. "Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type ? propeller domains."
      Collins M.N., Hendrickson W.A.
      Structure 19:324-336(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 98-183, SUBUNIT.
    9. "The structure of MESD45-184 brings light into the mechanism of LDLR family folding."
      Koehler C., Lighthouse J.K., Werther T., Andersen O.M., Diehl A., Schmieder P., Du J., Holdener B.C., Oschkinat H.
      Structure 19:337-348(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 45-184.

    Entry informationi

    Entry nameiMESD_MOUSE
    AccessioniPrimary (citable) accession number: Q9ERE7
    Secondary accession number(s): Q8C611
    , Q8CCX7, Q91WK8, Q9CVB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    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