ID   MESD_PONAB              Reviewed;         234 AA.
AC   Q5R6F1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   22-FEB-2023, entry version 62.
DE   RecName: Full=LRP chaperone MESD {ECO:0000305};
DE   AltName: Full=LDLR chaperone MESD;
DE   AltName: Full=Mesoderm development candidate 2;
DE   AltName: Full=Mesoderm development protein;
DE   Flags: Precursor;
GN   Name=MESD; Synonyms=MESDC2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone specifically assisting the folding of beta-
CC       propeller/EGF modules within the family of low-density lipoprotein
CC       receptors (LDLRs). Acts as a modulator of the Wnt pathway through
CC       chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and
CC       LRP6, to the plasma membrane. Essential for specification of embryonic
CC       polarity and mesoderm induction. Plays an essential role in
CC       neuromuscular junction (NMJ) formation by promoting cell-surface
CC       expression of LRP4. May regulate phagocytosis of apoptotic retinal
CC       pigment epithelium (RPE) cells. {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- SUBUNIT: Monomer. Interacts with LRP5; the interaction prevents LRP5
CC       from forming aggregates and chaperones LRP6 to the plasma membrane.
CC       Interacts with LRP6; the interaction prevents LRP6 from forming
CC       aggregates and chaperones LRP6 to the plasma membrane. Interacts with
CC       LRP4; the interaction promotes glycosylation of LRP4 and its cell-
CC       surface expression. {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9ERE7}. Note=Released from apoptotic cells and
CC       shed photoreceptor outer segments (By similarity).
CC       {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- DOMAIN: The chaperone domain provides a folding template for proper
CC       folding of the beta-propeller (BP) domains of LRP5/6.
CC       {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- DOMAIN: The escort domain ensures LRP5/6 safe-trafficking from the ER
CC       to the Golgi by preventing premature ligand-binding.
CC       {ECO:0000250|UniProtKB:Q9ERE7}.
CC   -!- SIMILARITY: Belongs to the MESD family. {ECO:0000305}.
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DR   EMBL; CR860539; CAH92665.1; -; mRNA.
DR   RefSeq; NP_001127574.1; NM_001134102.1.
DR   AlphaFoldDB; Q5R6F1; -.
DR   SMR; Q5R6F1; -.
DR   STRING; 9601.ENSPPYP00000007624; -.
DR   GlyCosmos; Q5R6F1; 1 site, No reported glycans.
DR   GeneID; 100174652; -.
DR   KEGG; pon:100174652; -.
DR   CTD; 23184; -.
DR   eggNOG; KOG4357; Eukaryota.
DR   InParanoid; Q5R6F1; -.
DR   OrthoDB; 2880079at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 6.10.250.640; -; 1.
DR   InterPro; IPR019330; MESD.
DR   PANTHER; PTHR17600:SF2; LRP CHAPERONE MESD; 1.
DR   PANTHER; PTHR17600; MESODERM DEVELOPMENT CANDIDATE 2; 1.
DR   Pfam; PF10185; Mesd; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..234
FT                   /note="LRP chaperone MESD"
FT                   /id="PRO_0000240319"
FT   REGION          1..164
FT                   /note="Chaperone domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT   REGION          31..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..204
FT                   /note="Escort domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT   REGION          187..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           231..234
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        71..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   234 AA;  26120 MW;  952FCB4BA2B672DC CRC64;
     MAASSWARKA VVVLCASDLL LLLLLLPPPG SCAAEASPGT PDESTPPPRK KKKDIRDYND
     ADMARLLEQW EKDDDIEEGD LPEHKRPSAP VDFSKIDPSK PESILKMTKK GKTLMMFVTV
     SGSPTEKETE EITSLWQGSL FNANYDVQRF IVGSDRAIFM LRDGNYAWEI KDFLVGQDRC
     ADVTLEGQVY PGKGGGSKEK NKTKQDKGKK KKEGDLKSRS SKEDNRARNK REDL
//