Lipase/lipooxygenase domain (PLAT/LH2 domain) superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All beta proteins [ 48724] (165)
• Fold: Lipase/lipooxygenase domain (PLAT/LH2 domain) [ 49722]
  • sandwich; 8 strands in 2 sheets; complex topology
    duplication: has weak internal pseudo twofold symmetry
• Superfamily: Lipase/lipooxygenase domain (PLAT/LH2 domain) [ 49723] (3)
• Families:
  • Lipoxigenase N-terminal domain [ 49724] (2)
  • Colipase-binding domain [ 49730]
  • Alpha-toxin, C-terminal domain [ 49738]

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Superfamily statistics

	Genomes (135)	UniProt 15.0	PDB chains (SCOP 1.73)
Domains	2,919	1,406	19
Proteins	1,913	1,173	19

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Functional annotation

• General category: Metabolism
• Detailed category: Lipid metabolism and transport

Function annotation of SCOP domain superfamilies

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InterPro annotation

• Cross references: IPR008976 SSF49723 Protein matches
• Abstract:

  This entry represents a domain found in lipoxygenases and other enzymes. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a beta-sandwich composed of two sheets of four strands each [10469604, 11985859, 11412104]. The most highly conserved regions coincide with the beta-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth beta-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.

InterPro database

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