Search by BoMiProt ID - Bomi6949

Primary Information

BoMiProt ID Bomi6949
Protein Name Mammalian ependymin-related protein 1/MERP-1
Organism Bos taurus
Uniprot IDA6QLI0
Milk FractionWhey
Ref Sequence ID NP_001095758.1
Aminoacid Length 236
Molecular Weight 26485
FASTA Sequence Download
Gene Name EPDR1/MERP1
Gene ID 615376
Protein Existence Status reviewed

Secondary Information

Protein Function lysosomal activator protein or a lipid transporter.transmembrane glycoproteins .role in cell proliferation.role in intercellular contacts between neural cells.extracellular domain may display antiadhesive properties and it shows a calcium-dependent ability to interact with collagen fibrils
Biochemical Properties  At acidic pH, EPDR1 can bind to liposomes that contain the anionic lipid bis-monoacylglycero-phosphate (BMP) or the ganglioside GM1, consistent with a role in the degradation or transport of lipids and/or lipoproteins within the lysosome.The structure revealed an extended and twisted 11 stranded antiparallel β sheet made up of two smaller sub-sheets consisting of strands 1–6 and strands 7–11 refer to as shelf-I and shelf-II, respectively .The two shelves are linked by antiparallel H-bonding between β1 and β11, placing strands β6 and β7 at opposite ends of the sheet.EPDR1 contains several highly conserved cysteine residues.
PTMs glycosylation and disulfide bond formation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions 1-6, 50-57, 140-154, 222-236
DisProt Annotation
TM Helix Prediction 1TMH; (20-42)
Significance of PTMs The N- and C-termini in EPDR1 are connected to the core fold by three conserved disulfide bonds.adopt the LolA/B-type β-clam fold 9 Cys residues that precede strand β1 are connected to shelf-II by one disulfide bond, while the 33 amino acids that follow strand β11 are connected to shelf-I by two disulfide bonds.contains a single glycosylation site at residue Asn130 of loop L7 on the back-side of the glove.
Bibliography Wei Y, Xiong ZJ, Li J, Zou C, Cairo CW, Klassen JS, Privé GG. Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters. Commun Biol. 2019 Feb 5;2:52. doi: 10.1038/s42003-018-0262-9. PMID: 30729188; PMCID: PMC6363788.