Primary Information |
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| BoMiProt ID | Bomi6949 |
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| Protein Name | Mammalian ependymin-related protein 1/MERP-1 |
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| Organism | Bos taurus |
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| Uniprot ID | A6QLI0 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001095758.1 |
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| Aminoacid Length | 236 |
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| Molecular Weight | 26485 |
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| FASTA Sequence |
Download |
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| Gene Name | EPDR1/MERP1 |
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| Gene ID | 615376 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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 |
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| 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. |
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| PTMs | glycosylation and disulfide bond formation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|A6QLI0|EPDR1_BOVIN Mammalian ependymin-related protein 1 OS=Bos taurus OX=9913 GN=EPDR1 PE=2 SV=1
MPRRAPLRVARGSLDAWLLGGLWVCALGCLCGVGMAAPGAGAGAGGSLGAQRPCQAPQQW
EGRQVLYRQSTGRYSRALLSYDGLNQRVRVLDERKALIPCKRLFEYILLYKDGVMFQIEQ
ATKQCSKITLTEPWDPLDIPQN*142STFEDQYSIGGPQEQITVQEWSDRKSARSYETWIGIYT
VKDCYPVQETVTKN*194YSVILSTRFFDIQLGIKDPSVFIPPSTCQTAQPERMSEECSW
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| Predicted Disorder Regions | 1-6, 50-57, 140-154, 222-236 |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (20-42) |
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| 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. |
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| 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. |
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