JMJD6 Protein Overview: Sequence, Structure, Function and Protein Interaction

JMJD6 Protein Overview

The culmination of apoptosis in vivo is phagocytosis of cellular corpses. During apoptosis, the asymmetry of plasma membrane phospholipids is lost, which exposes phosphatidylserine externally. The phagocytosis of apoptotic cells can be inhibited stereospecifically by phosphatidylserine and its structural analogs, but not by other anionic phospholipids, suggesting that phosphatidylserine is specifically recognized. Fadok et al. (2000) used phage display to clone a gene that appeared to recognize phosphatidylserine on apoptotic cells. Fadok et al. (2000) showed that this gene, phosphatidylserine receptor or PSR, when transfected into B and T lymphocytes, enabled them to recognize and engulf apoptotic cells in a phosphatidylserine-specific manner. Flow cytometric analysis using a monoclonal antibody suggested that the protein is expressed on the surface of macrophages, fibroblasts, and epithelial cells; this antibody, like phosphatidylserine liposomes, inhibited the phagocytosis of apoptotic cells and, in macrophages, induced an antiinflammatory state. This candidate phosphatidylserine receptor is highly homologous to genes in Caenorhabditis elegans and Drosophila, suggesting that phosphatidylserine recognition on apoptotic cells during their removal by phagocytes is highly conserved throughout phylogeny. Nagase et al. (1998) cloned the phosphatidylserine receptor from a human brain cDNA library and designated it KIAA0585. They demonstrated that KIAA0585 was highly homologous to an uncharacterized open reading frame in C. elegans. Using RT-PCR, Nagase et al. (1998) found that expression was high in heart, skeletal muscle, and kidney, and moderate or low in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis, and ovary. A number of homologous sequences were present in human, mouse, Drosophila, and C. elegans EST databases. The predicted 427-amino acid protein has 1 predicted transmembrane domain and an area in the C terminus that contains a series of serines that represent potential O-glycosylation sites. The predicted molecular weight for this protein based on sequence analysis was 47 to 48 kD for human, mouse, and Drosophila gene products and 40 kD for that of the nematode. Western blot analysis suggested an apparent molecular weight of 70 kD; deglycosylation reduces the apparent size to approximately 50 kD, which is compatible with the predicted molecular weight of 47 kD.

JMJD6 protein family

Belongs to the JMJD6 family.

JMJD6 protein name

Recommended name
Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
Short name
Protein PTDSR
Aliases
KIAA0585, PTDSR1
Alternative name
Histone arginine demethylase JMJD6 JmjC domain-containing protein 6 Jumonji domain-containing protein 6 Lysyl-hydroxylase JMJD6 Peptide-lysine 5-dioxygenase JMJD6 Phosphatidylserine receptor

JMJD6 Protein Sequence

Species Human JMJD6 protein
Length 403
Mass (Da) 46462
Sequence Human JMJD6 protein sequence
Species Mouse JMJD6 protein
Length 403
Mass (Da) 46567
Sequence Mouse JMJD6 protein sequence
Species Rat JMJD6 protein
Length 403
Mass (Da) 46540
Sequence Rat JMJD6 protein sequence

JMJD6 Protein Molecular Weight & PI

Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 1-403 Bifunctional arginine demethylase and

Molecular weight (Da)

46462.01

Theoretical pI

8.84

JMJD6 Protein Structure

Crystal structure of Fe(II)- and 2OG-dependent oxygenase JMJD6 (aa 1-403) in complex with Mn(II) and NOG
Deposited
2018-02-13   Released:  2018-05-09
Deposition Author(s)
Islam, M.S., Schofield, C.J., McDonough, M.A.
Organism(s)
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
1.6680 Å
R-Value Free
0.193
R-Value Work
0.165
6FQC From PDB

Human JMJD6 protein Secondary structure

JMJD6 Protein Interaction

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