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Protein

LDLR chaperone MESD

Gene

MESDC2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Biological processi

  1. protein folding Source: UniProtKB
  2. 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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 234201LDLR chaperone MESDPRO_0000240319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer (By similarity). 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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5R6F1.
SMRiQ5R6F1. Positions 98-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 164164Chaperone domainBy similarityAdd
BLAST
Regioni165 – 20440Escort domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi231 – 2344Prevents secretion from ER

Domaini

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

Sequence similaritiesi

Belongs to the MESD family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ5R6F1.

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.

Q5R6F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASSWARKA VVVLCASDLL LLLLLLPPPG SCAAEASPGT PDESTPPPRK
60 70 80 90 100
KKKDIRDYND ADMARLLEQW EKDDDIEEGD LPEHKRPSAP VDFSKIDPSK
110 120 130 140 150
PESILKMTKK GKTLMMFVTV SGSPTEKETE EITSLWQGSL FNANYDVQRF
160 170 180 190 200
IVGSDRAIFM LRDGNYAWEI KDFLVGQDRC ADVTLEGQVY PGKGGGSKEK
210 220 230
NKTKQDKGKK KKEGDLKSRS SKEDNRARNK REDL
Length:234
Mass (Da):26,120
Last modified:December 21, 2004 - v1
Checksum:i952FCB4BA2B672DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860539 mRNA. Translation: CAH92665.1.
RefSeqiNP_001127574.1. NM_001134102.1.
UniGeneiPab.1436.

Genome annotation databases

GeneIDi100174652.
KEGGipon:100174652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860539 mRNA. Translation: CAH92665.1.
RefSeqiNP_001127574.1. NM_001134102.1.
UniGeneiPab.1436.

3D structure databases

ProteinModelPortaliQ5R6F1.
SMRiQ5R6F1. Positions 98-193.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174652.
KEGGipon:100174652.

Organism-specific databases

CTDi23184.

Phylogenomic databases

InParanoidiQ5R6F1.

Family and domain databases

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

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiMESD_PONAB
AccessioniPrimary (citable) accession number: Q5R6F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: December 21, 2004
Last modified: January 7, 2015
This is version 42 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.