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Q9ERE7

- MESD_MOUSE

UniProt

Q9ERE7 - MESD_MOUSE

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Protein

LDLR chaperone MESD

Gene

Mesdc2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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-KW
  2. plasma membrane Source: MGI
Complete GO annotation...

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

BgeeiQ9ERE7.
CleanExiMM_MESDC2.
ExpressionAtlasiQ9ERE7. baseline and differential.
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.
InParanoidiQ9ERE7.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASRWLRAV LLFLCASDLL LLPPPNAYAA DTPGEATPPP RKKKDIRDYN
60 70 80 90 100
DADMARLLEQ WEKDDDIEEG DLPEHKRPSA PIDFSKLDPG KPESILKMTK
110 120 130 140 150
KGKTLMMFVT VSGNPTEKET EEITSLWQGS LFNANYDVQR FIVGSDRAIF
160 170 180 190 200
MLRDGSYAWE IKDFLVSQDR CAEVTLEGQM YPGKGGGSKE KNKTKPEKAK
210 220
KKEGDPKPRA SKEDNRAGSR REDL
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 Q9ERE7.
OMAi NQERCAD.
OrthoDBi EOG7XPZ76.
PhylomeDBi Q9ERE7.
TreeFami TF315614.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9ERE7.
CleanExi MM_MESDC2.
ExpressionAtlasi Q9ERE7. baseline and differential.
Genevestigatori Q9ERE7.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 96 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