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Protein

LDLR chaperone MESD

Gene

Mesdc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • low-density lipoprotein particle receptor binding Source: MGI

GO - Biological processi

  • mesoderm development Source: UniProtKB
  • protein folding Source: UniProtKB
  • protein localization to cell surface Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1891421. Mesdc2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB-SubCell
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000009644430 – 224LDLR chaperone MESDAdd BLAST195

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9ERE7.
MaxQBiQ9ERE7.
PaxDbiQ9ERE7.
PeptideAtlasiQ9ERE7.
PRIDEiQ9ERE7.

2D gel databases

REPRODUCTION-2DPAGEIPI00349285.
Q9ERE7.

PTM databases

PhosphoSitePlusiQ9ERE7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSMUSG00000038503.
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.3 Publications

Binary interactionsi

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

GO - Molecular functioni

  • low-density lipoprotein particle receptor binding Source: MGI

Protein-protein interaction databases

BioGridi212555. 1 interactor.
DIPiDIP-59114N.
IntActiQ9ERE7. 4 interactors.
STRINGi10090.ENSMUSP00000091768.

Structurei

Secondary structure

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni43 – 45Combined sources3
Helixi47 – 49Combined sources3
Helixi51 – 65Combined sources15
Beta strandi87 – 90Combined sources4
Helixi93 – 99Combined sources7
Beta strandi105 – 113Combined sources9
Helixi117 – 133Combined sources17
Beta strandi138 – 142Combined sources5
Beta strandi147 – 153Combined sources7
Helixi155 – 157Combined sources3
Helixi158 – 166Combined sources9
Beta strandi168 – 170Combined sources3
Beta strandi171 – 176Combined sources6
Beta strandi179 – 181Combined sources3
Beta strandi183 – 186Combined sources4
Helixi195 – 203Combined sources9
Beta strandi208 – 210Combined sources3
Helixi211 – 217Combined sources7

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...

Miscellaneous databases

EvolutionaryTraceiQ9ERE7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 155Chaperone domainAdd BLAST155
Regioni156 – 195Escort domainAdd 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.
OMAiMAASGWA.
OrthoDBiEOG091G0TTK.
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

        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 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.

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. 1 interactor.
DIPiDIP-59114N.
IntActiQ9ERE7. 4 interactors.
STRINGi10090.ENSMUSP00000091768.

PTM databases

PhosphoSitePlusiQ9ERE7.

2D gel databases

REPRODUCTION-2DPAGEIPI00349285.
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. Mesdc2.

Phylogenomic databases

eggNOGiKOG4357. Eukaryota.
ENOG4111SG4. LUCA.
GeneTreeiENSGT00390000000993.
HOGENOMiHOG000230558.
InParanoidiQ9ERE7.
OMAiMAASGWA.
OrthoDBiEOG091G0TTK.
PhylomeDBiQ9ERE7.
TreeFamiTF315614.

Miscellaneous databases

EvolutionaryTraceiQ9ERE7.
PROiQ9ERE7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038503.
CleanExiMM_MESDC2.
ExpressionAtlasiQ9ERE7. baseline and differential.
GenevisibleiQ9ERE7. MM.

Family and domain databases

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

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: November 2, 2016
This is version 110 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.