This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
Facts about Patatin-like phospholipase domain-containing protein 2.
May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes (PubMed:16239926).
Human | |
---|---|
Gene Name: | PNPLA2 |
Uniprot: | Q96AD5 |
Entrez: | 57104 |
Belongs to: |
---|
No superfamily |
Adipose triglyceride lipase; ATGL; ATGL1110001C14Rik; Calcium-independent phospholipase A2; Desnutrin; EC 3.1.1.3; FP17548; IPLA2-zeta; patatin-like phospholipase domain containing 2; patatin-like phospholipase domain-containing protein 2; patatin-like phospholipase domain-containing protein 2-like; PEDF R; PEDFR; PEDF-R; Pigment epithelium-derived factor; PNPLA2; Transport-secretion protein 2; transport-secretion protein 2.2; triglyceride hydrolase; TTS2; TTS2.2; TTS-2.2; TTS2DKFZp667M109
Mass (kDA):
55.316 kDA
Human | |
---|---|
Location: | 11p15.5 |
Sequence: | 11; NC_000011.10 (818890..825573) |
Highest expression in adipose tissue. Also detected in heart, skeletal muscle, and portions of the gastrointestinal tract. Detected in normal retina and retinoblastoma cells. Detected in retinal pigment epithelium and, at lower intensity, in the inner segments of photoreceptors and in the ganglion cell layer of the neural retina (at protein level).
Lipid droplet. Cell membrane; Single-pass type II membrane protein.
PMID: 15550674 by Zimmermann R., et al. Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.
PMID: 15364929 by Jenkins C.M., et al. Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities.