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Q9ERE7 (MESD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LDLR chaperone MESD
Alternative name(s):
Mesoderm development candidate 2
Mesoderm development protein
Gene names
Name:Mesdc2
Synonyms:Mesd
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.7

Subunit structure

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. Ref.4 Ref.5 Ref.8

Subcellular location

Endoplasmic reticulum Ref.4.

Tissue specificity

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

Domain

The chaperone domain provides a folding template for proper folding of the beta-propeller (BP) domains of LRP5/6. Ref.7

The escort domain ensures LRP5/6 safe-trafficking from the ER to the Golgi by preventing premature ligand-binding. Ref.7

Disruption phenotype

Disruption of embryonic polarity and mesoderm differentiation, likely resulting from a primary defect in Wnt signaling. Ref.4

Sequence similarities

Belongs to the MESD family.

Sequence caution

The sequence AAH14742.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC36476.1 differs from that shown. Reason: Frameshift at position 207.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Lrp4Q8VI562EBI-6662606,EBI-2106160

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 224195LDLR chaperone MESD
PRO_0000096444

Regions

Region1 – 155155Chaperone domain
Region156 – 19540Escort domain
Motif221 – 2244Prevents secretion from ER

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2061P → R in BAC36471. Ref.2

Secondary structure

.................................. 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ERE7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6A94D5B315AE1D66

FASTA22425,207
        10         20         30         40         50         60 
MAASRWLRAV LLFLCASDLL LLPPPNAYAA DTPGEATPPP RKKKDIRDYN DADMARLLEQ 

        70         80         90        100        110        120 
WEKDDDIEEG DLPEHKRPSA PIDFSKLDPG KPESILKMTK KGKTLMMFVT VSGNPTEKET 

       130        140        150        160        170        180 
EEITSLWQGS LFNANYDVQR FIVGSDRAIF MLRDGSYAWE IKDFLVSQDR CAEVTLEGQM 

       190        200        210        220 
YPGKGGGSKE KNKTKPEKAK KKEGDPKPRA SKEDNRAGSR REDL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_075892.3. NM_023403.3.
UniGeneMm.117365.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I9SNMR-A89-184[»]
2KGLNMR-A30-224[»]
2KMINMR-A41-185[»]
2RQKNMR-A45-184[»]
2RQMNMR-A45-184[»]
3OFHX-ray2.01A/B98-183[»]
ProteinModelPortalQ9ERE7.
SMRQ9ERE7. Positions 30-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212555. 1 interaction.
DIPDIP-59114N.
IntActQ9ERE7. 4 interactions.
STRING10090.ENSMUSP00000091768.

PTM databases

PhosphoSiteQ9ERE7.

2D gel databases

REPRODUCTION-2DPAGEIPI00349285.
Q9ERE7.

Proteomic databases

PaxDbQ9ERE7.
PRIDEQ9ERE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000094215; ENSMUSP00000091768; ENSMUSG00000038503.
GeneID67943.
KEGGmmu:67943.
UCSCuc009idx.2. mouse.

Organism-specific databases

CTD23184.
MGIMGI:1891421. Mesdc2.

Phylogenomic databases

eggNOGNOG286690.
GeneTreeENSGT00390000000993.
HOGENOMHOG000230558.
InParanoidQ91WK8.
OMAIVGSNRA.
OrthoDBEOG7XPZ76.
PhylomeDBQ9ERE7.
TreeFamTF315614.

Gene expression databases

ArrayExpressQ9ERE7.
BgeeQ9ERE7.
CleanExMM_MESDC2.
GenevestigatorQ9ERE7.

Family and domain databases

InterProIPR019330. Mesoderm_development_cand-2.
[Graphical view]
PfamPF10185. Mesd. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9ERE7.
NextBio326030.
PROQ9ERE7.
SOURCESearch...

Entry information

Entry nameMESD_MOUSE
AccessionPrimary (citable) accession number: Q9ERE7
Secondary accession number(s): Q8C611 expand/collapse secondary AC list , Q8CCX7, Q91WK8, Q9CVB9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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