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perilipin 1

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ProteinQ415624· pop 8· linked from 15 articles

perilipin 1

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Also known as PLIN1, lipid droplet-associated protein, perilipin-1

Perilipin, also known as lipid droplet-associated protein, perilipin 1, or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.

Protein · UniProt

Perilipin-1

Gene
PLIN1
Organism
Homo sapiens (Human)
Length
522 aa
Molecular mass
55,990 Da
Evidence
1: Evidence at protein level

Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels

Endoplasmic reticulumLipid dropletLipid metabolismPhosphoproteinProteomics identificationReference proteome
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Encyclopedic overview

12 sections
Contents
  • Perilipin family of proteins
  • Evolution
  • Composition and structure
  • Human perilipin
  • Murine perilipin
  • Function
  • Modulator of adipocyte lipid metabolism
  • Clinical significance
  • Overexpression
  • Deficiency
  • References
  • Further reading

Perilipin, also known as lipid droplet-associated protein, perilipin 1, or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.

== Perilipin family of proteins == Perilipin is part of a gene family with six currently-known members. In vertebrates, closely related genes include adipophilin (also known as adipose differentiation-related protein or Perilipin 2), TIP47 (Perilipin 3), Perilipin 4 and Perilipin 5 (also called MLDP, LSDP5, or OXPAT). Insects express related proteins, LSD1 and LSD2, in fat bodies. The yeast Saccharomyces cerevisiae expresses PLN1 (formerly PET10), that stabilizes lipid droplets and aids in their assembly.

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