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Protein

LRP chaperone MESD

Gene

Mesd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:12581525). Plays an essential role in neuromuscular junction (NMJ) formation by promoting cell-surface expression of LRP4 (PubMed:24140340). May regulate phagocytosis of apoptotic retinal pigment epithelium (RPE) cells (PubMed:27184668).4 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • low-density lipoprotein particle receptor binding Source: MGI

GO - Biological processi

  • mesoderm development Source: UniProtKB
  • phagocytosis Source: UniProtKB
  • positive regulation of skeletal muscle acetylcholine-gated channel clustering Source: UniProtKB
  • protein folding Source: MGI
  • protein localization to cell surface Source: MGI
  • Wnt signaling pathway Source: UniProtKB-KW

Keywordsi

Molecular functionChaperone
Biological processWnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
LRP chaperone MESDCurated
Alternative name(s):
LDLR chaperone MESD
Mesoderm development candidate 2
Mesoderm development protein
Gene namesi
Name:MesdImported
Synonyms:Mesdc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1891421 Mesd

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000009644430 – 224LRP chaperone MESDAdd BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi192N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9ERE7
MaxQBiQ9ERE7
PaxDbiQ9ERE7
PeptideAtlasiQ9ERE7
PRIDEiQ9ERE7

2D gel databases

REPRODUCTION-2DPAGEiIPI00349285
Q9ERE7

PTM databases

PhosphoSitePlusiQ9ERE7

Expressioni

Tissue specificityi

Expressed in many tissues, but not in skeletal muscles (PubMed:11247670). In the retina expressed in retinal ganglion cells, inner and outer plexiform layers, photoreceptor inner and outer segments and retinal pigment epithelium (at protein level) (PubMed:27184668).2 Publications

Gene expression databases

BgeeiENSMUSG00000038503 Expressed in 290 organ(s), highest expression level in ear vesicle
CleanExiMM_MESDC2
ExpressionAtlasiQ9ERE7 baseline and differential
GenevisibleiQ9ERE7 MM

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. Interacts with LRP4; the interaction promotes glycosylation of LRP4 and its cell-surface expression (PubMed:24140340).4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212555, 2 interactors
DIPiDIP-59114N
IntActiQ9ERE7, 5 interactors
MINTiQ9ERE7
STRINGi10090.ENSMUSP00000091768

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9ERE7
SMRiQ9ERE7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ERE7

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 155Chaperone domain1 PublicationAdd BLAST155
Regioni156 – 195Escort domain1 PublicationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi221 – 224Prevents secretion from ER4

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

eggNOGiKOG4357 Eukaryota
ENOG4111SG4 LUCA
GeneTreeiENSGT00390000000993
HOGENOMiHOG000230558
InParanoidiQ9ERE7
OMAiIVGSNRA
OrthoDBiEOG091G0TTK
PhylomeDBiQ9ERE7
TreeFamiTF315614

Family and domain databases

InterProiView protein in InterPro
IPR019330 MESD
PANTHERiPTHR17600 PTHR17600, 1 hit
PfamiView protein in Pfam
PF10185 Mesd, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q9ERE7-1 [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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YVR4D3YVR4_MOUSE
LRP chaperone MESD
Mesd Mesdc2
154Annotation score:
F6SWV4F6SWV4_MOUSE
LRP chaperone MESD
Mesd Mesdc2
77Annotation score:

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti206P → R in BAC36471 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212555, 2 interactors
DIPiDIP-59114N
IntActiQ9ERE7, 5 interactors
MINTiQ9ERE7
STRINGi10090.ENSMUSP00000091768

PTM databases

PhosphoSitePlusiQ9ERE7

2D gel databases

REPRODUCTION-2DPAGEiIPI00349285
Q9ERE7

Proteomic databases

EPDiQ9ERE7
MaxQBiQ9ERE7
PaxDbiQ9ERE7
PeptideAtlasiQ9ERE7
PRIDEiQ9ERE7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23184
MGIiMGI:1891421 Mesd

Phylogenomic databases

eggNOGiKOG4357 Eukaryota
ENOG4111SG4 LUCA
GeneTreeiENSGT00390000000993
HOGENOMiHOG000230558
InParanoidiQ9ERE7
OMAiIVGSNRA
OrthoDBiEOG091G0TTK
PhylomeDBiQ9ERE7
TreeFamiTF315614

Miscellaneous databases

EvolutionaryTraceiQ9ERE7
PROiPR:Q9ERE7
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038503 Expressed in 290 organ(s), highest expression level in ear vesicle
CleanExiMM_MESDC2
ExpressionAtlasiQ9ERE7 baseline and differential
GenevisibleiQ9ERE7 MM

Family and domain databases

InterProiView protein in InterPro
IPR019330 MESD
PANTHERiPTHR17600 PTHR17600, 1 hit
PfamiView protein in Pfam
PF10185 Mesd, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMESD_MOUSE
AccessioniPrimary (citable) accession number: Q9ERE7
Secondary accession number(s): Q8C611
, Q8CCX7, Q91WK8, Q9CVB9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: March 1, 2001
Last modified: September 12, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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