ENPP2

Also known as ATX, ATX-X, AUTOTAXIN, LysoPLD, NPP2, PD-IALPHA, PDNP2, ectonucleotide pyrophosphatase/phosphodiesterase 2

Autotaxin, also known as ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2), is an enzyme that in humans is encoded by the ENPP2 gene.

Gene data

ENPP2

Name: ectonucleotide pyrophosphatase/phosphodiesterase 2
Type: protein-coding
Aliases: ATX, ATX-X, AUTOTAXIN, LysoPLD, NPP2, PD-IALPHA, PDNP2

The protein encoded by this gene functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids. LPA evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. This gene product stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The gene product is secreted and further processed to make the biologically active form. Several alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Aug 2008].

via MyGene.info

Wikidata facts

Image: 3nkr.png

Sources (6)

Article

7 sections

Contents

Structure
Function
As a drug target
See also
References
Further reading
External links

Autotaxin, also known as ectonucleotide pyrophosphatase/phosphodiesterase family member 2 (E-NPP 2), is an enzyme that in humans is encoded by the ENPP2 gene.

== Structure == Autotaxin is a multi-domain protein with a modular architecture. From the N- to the C-terminus, it comprises two consecutive N-terminal cysteine-rich somatomedin B-like (SMB) domains, followed by a central catalytic phosphodiesterase (PDE) domain and a C-terminal nuclease-like (NUC) domain. The two SMB domains mediate protein–protein interactions, particularly through integrin-dependent binding to cell surfaces. The catalytic PDE domain, which is structurally related to alkaline phosphatases, harbors the enzyme's lysophospholipase D activity responsible for converting lysophosphatidylcholine into lysophosphatidic acid (LPA). The C-terminal NUC domain, although catalytically inactive, is structurally linked to the PDE domain and contributes to substrate binding and overall protein stability. A region at the extreme C-terminus, sometimes referred to as the MORFO domain, overlaps with the NUC region and has been associated with oligodendrocyte remodeling. Thus, the domain organization from N- to C-terminus is: SMB1–SMB2–PDE–NUC, with the MORFO domain often considered part of or overlapping with the NUC domain.