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Literature summary extracted from

  • Pradere, J.P.; Tarnus, E.; Gres, S.; Valet, P.; Saulnier-Blache, J.S.
    Secretion and lysophospholipase D activity of autotaxin by adipocytes are controlled by N-glycosylation and signal peptidase (2007), Biochim. Biophys. Acta, 1771, 93-102.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.4.39 expressed in COS-7 cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.4.39 DELTAA30-G41 deletion mutants are generated from plasmid pcDNA-mATX, encompasses furin site Mus musculus
3.1.4.39 DELTAA30-I33 deletion mutants are generated from plasmid pcDNA-mATX, between signal peptidase and furin site Mus musculus
3.1.4.39 DELTAA36-E40 deletion mutants are generated from plasmid pcDNA-mATX Mus musculus
3.1.4.39 DELTAC25 deletion mutants are generated from plasmid pcDNA-mATX, amino acid -3 referring to the potential signal peptidase cleavage site Mus musculus
3.1.4.39 DELTAE40-P43 deletion mutants are generated from plasmid pcDNA-mATX Mus musculus
3.1.4.39 DELTAG27 deletion mutants are generated from plasmid pcDNA-mATX, amino acid -1 referring to the potential signal peptidase cleavage site Mus musculus
3.1.4.39 DELTAG27-A30 deletion mutants are generated from plasmid pcDNA-mATX, contain potential signal peptidase clevage site Mus musculus
3.1.4.39 DELTAG27-R35 deletion mutants are generated from plasmid pcDNA-mATX, encompasses both furin and signal peptidase cleavage sites Mus musculus
3.1.4.39 DELTAL46-S49 deletion mutants are generated from plasmid pcDNA-mATX Mus musculus
3.1.4.39 DELTAN23 deletion mutants are generated from plasmid pcDNA-mATX, amino acid -5 referring to the potential signal peptidase cleavage site Mus musculus
3.1.4.39 DELTAN23-G27 deletion mutants are generated from plasmid pcDNA-mATX, encompasses -1 and -3 amino acids referring to the potential signal peptidase clevage site Mus musculus
3.1.4.39 DELTAN410 deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, point deletion of the amino-acid N410 inhibits lysophospholipase D activity of ATX, does not modify the ATX secretion and strongly inhibits ATX activity Mus musculus
3.1.4.39 DELTAN53 deletion mutants are generated from plasmid pcDNA-mATX, contains a N-glycosylation site, does not modify the ATX secretion and slightly reduces (25%) ATX activity Mus musculus
3.1.4.39 DELTAN53/DELTAN410 deletion mutants are generated from plasmid pcDNA-mATX, two N-glycosylation sites, double point deletion of the amino-acids N53 and N410 inhibits secretion of ATX, without altering the ATX amount in cell homogenate Mus musculus
3.1.4.39 DELTAP43-L46 deletion mutants are generated from plasmid pcDNA-mATX Mus musculus
3.1.4.39 DELTAR32-R35 deletion mutants are generated from plasmid pcDNA-mATX, furine site Mus musculus
3.1.4.39 DELTAS49-N53 deletion mutants are generated from plasmid pcDNA-mATX, contains N-glycosylation site Mus musculus
3.1.4.39 DELTAV12-G27 deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide and signal peptide cleavage site, ATX secretion is suppressed Mus musculus
3.1.4.39 DELTAV12-V22 deletion mutants are generated from plasmid pcDNA-mATX, hydrophobic domain of signal peptide, ATX secretion is suppressed Mus musculus
3.1.4.39 additional information deletions of the amino acids N53 and N410 lead to a reduction of the molecular weight of ATX Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.4.39 brefeldin-A inhibitor of trans-Golgi transport, inhibits secretion of ATX Mus musculus
3.1.4.39 Globomycin Treatment with the signal peptidase inhibitor inhibits ATX secretion by adipocytes treated for 6 h Mus musculus
3.1.4.39 lactacystin proteasome inhibitor, restores the detection of ATX in cell homogenate of the mutants DELTAV12-V22 and DELTAV12-G27, Synthesis and secretion of ATX are highly dependent on the hydrophobic core of the signal peptide, but not on the amino acid composition the putative signal peptidase cleavage site Mus musculus
3.1.4.39 additional information possible involement of furin in secretion of ATX by adipocytes tested, furin inhibitor decanoyl-Arg–Val–Lys–Arg–chloromethylketone does not modify secretion or lysophospholipase D activity of ATX Mus musculus
3.1.4.39 N-glycosidase treatment with N-glycosidase inhibits lysophospholipase D activity of ATX. N-glycosylation of ATX strongly influences its secretion and its lysoPLD activity Mus musculus
3.1.4.39 tunicamycin inhibits secretion of ATX Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.4.39 extracellular results suggest that cell ATX behaves mainly as a soluble protein Mus musculus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.4.39 120000
-
 analyzed by Western blot, ATX is undetectable in conditioned media from undifferentiated 3T3F442A preadipocytes. Conditioned media treated with N-glycosidase and O-glycosidase, N-glycosidase leads to a reduction of 9.6 kDa apparent molecular weight of ATX, O-glycosidase is without influence Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.4.39 lysophosphatidylcholine + H2O Mus musculus
-
 lysophosphatidic acid + choline
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.39 Mus musculus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.4.39 glycoprotein
-
 Mus musculus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.4.39 Western blot in cell homogenates requires a pre-purification with concanavalin A-sepharose Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.4.39 adipocyte Immunocyto-fluorescence microscopy reveals that ATX is detected in 3T3F442A adipocytes and is almost undetectable in 3T3F442A preadipocytes. 3T3F442A mouse preadipose cell line Mus musculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.4.39 additional information
-
 lysophospholipase D activity is measured by conversion of radiolabeled lysophosphatidylcholine into radiolabeled lysophosphatidic acid Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.39 lysophosphatidylcholine + H2O
-
 Mus musculus lysophosphatidic acid + choline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.39 ATX
-
 Mus musculus
3.1.4.39 autotaxin
-
 Mus musculus
3.1.4.39 ectonucleotide pyrophosphatase phosphodiesterase-2
-
 Mus musculus
3.1.4.39 ENPP2
-
 Mus musculus
3.1.4.39 lysophospholipase D
-
 Mus musculus