ID   MESD_RAT                Reviewed;         224 AA.
AC   Q5U2R7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 102.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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. {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; BC085892; AAH85892.1; -; mRNA.
DR   RefSeq; NP_001008346.1; NM_001008345.1.
DR   AlphaFoldDB; Q5U2R7; -.
DR   BMRB; Q5U2R7; -.
DR   SMR; Q5U2R7; -.
DR   STRING; 10116.ENSRNOP00000052447; -.
DR   GlyCosmos; Q5U2R7; 1 site, No reported glycans.
DR   GlyGen; Q5U2R7; 1 site.
DR   PhosphoSitePlus; Q5U2R7; -.
DR   jPOST; Q5U2R7; -.
DR   PaxDb; 10116-ENSRNOP00000052447; -.
DR   ABCD; Q5U2R7; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000105170.1; ENSRNOP00000092593.1; ENSRNOG00000012366.7.
DR   GeneID; 308796; -.
DR   KEGG; rno:308796; -.
DR   AGR; RGD:1310344; -.
DR   CTD; 23184; -.
DR   RGD; 1310344; Mesd.
DR   eggNOG; KOG4357; Eukaryota.
DR   GeneTree; ENSGT00390000000993; -.
DR   HOGENOM; CLU_111621_0_0_1; -.
DR   InParanoid; Q5U2R7; -.
DR   OMA; QQRCADV; -.
DR   OrthoDB; 2880079at2759; -.
DR   PhylomeDB; Q5U2R7; -.
DR   TreeFam; TF315614; -.
DR   PRO; PR:Q5U2R7; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000012366; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR   GO; GO:0001503; P:ossification; ISO:RGD.
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.
DR   Genevisible; Q5U2R7; RN.
PE   2: Evidence at transcript level;
KW   Chaperone; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..224
FT                   /note="LRP chaperone MESD"
FT                   /id="PRO_0000240320"
FT   REGION          1..155
FT                   /note="Chaperone domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT   REGION          156..195
FT                   /note="Escort domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT   REGION          178..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           221..224
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        188..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   224 AA;  25216 MW;  88B146EBB72B4EB8 CRC64;
     MAASSWLRAV LLFLCASDLL LLSPPEAYAT DTPGEAITPP RKKKDIRDYN DADMARLLEQ
     WEKDDDIEEG DLPEHKRPSA PIDFSKLDPG KPESILKMTK KGKTLMMFVT ISGNPTEKET
     EEITSLWQGS LFNANYDVQR FIVGSDRAIF MLRDGSYAWE IKDFLVNQDR CAEVTLEGQM
     YPGKGGGSKE KNKTKPEKGK KKEGDPKPRA SKEDNRAGSR REDL
//