MESD_BOVIN
ID MESD_BOVIN Reviewed; 232 AA.
AC Q3T0U1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 {ECO:0000255|PROSITE-
CC ProRule:PRU10138}. Note=Released from apoptotic cells and shed
CC 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; BC102262; AAI02263.1; -; mRNA.
DR RefSeq; NP_001029641.1; NM_001034469.1.
DR AlphaFoldDB; Q3T0U1; -.
DR SMR; Q3T0U1; -.
DR STRING; 9913.ENSBTAP00000002045; -.
DR PaxDb; Q3T0U1; -.
DR PeptideAtlas; Q3T0U1; -.
DR PRIDE; Q3T0U1; -.
DR Ensembl; ENSBTAT00000002045; ENSBTAP00000002045; ENSBTAG00000001565.
DR GeneID; 514610; -.
DR KEGG; bta:514610; -.
DR CTD; 23184; -.
DR VEuPathDB; HostDB:ENSBTAG00000001565; -.
DR VGNC; VGNC:31392; MESD.
DR eggNOG; KOG4357; Eukaryota.
DR GeneTree; ENSGT00390000000993; -.
DR HOGENOM; CLU_111621_0_0_1; -.
DR InParanoid; Q3T0U1; -.
DR OMA; NRATKQR; -.
DR OrthoDB; 1590303at2759; -.
DR TreeFam; TF315614; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000001565; Expressed in uterine horn and 105 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
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 InterPro; IPR019330; MESD.
DR PANTHER; PTHR17600; PTHR17600; 1.
DR Pfam; PF10185; Mesd; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..232
FT /note="LRP chaperone MESD"
FT /id="PRO_0000240318"
FT REGION 1..162
FT /note="Chaperone domain"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT REGION 32..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..202
FT /note="Escort domain"
FT /evidence="ECO:0000250|UniProtKB:Q9ERE7"
FT REGION 185..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 229..232
FT /note="Prevents secretion from ER"
FT COMPBIAS 197..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 232 AA; 25977 MW; C5BE6CC1ADBBE8EB CRC64;
MAASGWARAA VIFLCACDLL LLLLLPPRAF ATEGPAETPG EATPPPRKKK KDIRDYNDAD
MARLLEQWEK DDDIEEGDLP EHKRPSAPID FSQIDPGKPE SILKMTKKGK TLMMFVTVSG
NPTEKETEEI TSLWQGSLFN ANYDVQRFIV GSDRAIFMLR DGGYAWEIKD FLVSQDRCAD
VTLEGQVYPG KGGGSKEKNQ TKQEKGKKKK ERDLKPRASK EDNRAGSKKE EL
