InterPro : IPR000463

Name  Cytosolic fatty-acid binding Short Name  Fatty_acid-bd
Type  Domain Description  The Fatty Acid-Binding Proteins (FABPs) are a family of proteins that areprincipally located in the cytosol and are characterised by the ability tobind to hydrophobic ligands, such as fatty acids, retinol, retinoic acid, bile salts and pigments [, ]. Recently, a number of family members havebeen identified that are secreted, such as gastrotropin and mammary-derivedgrowth inhibitor. The family is implicated in general lipid metabolism,acting as intracellular transporters of hydrophobic metabolic intermediatesand as carriers of lipids between membranes [, , ]. The FABPs exhibit a high degree both of sequence and structural similarity.They are small, 12-18 kDa, soluble proteins composed of 110-160 residues. Their crystal structures show them to be 10-stranded anti-parallel beta-barrels with a +1,+1 topology, which wrap around an internal cavity to form a ligand binding site [, ]. Ligand specificity and affinity is governed by the side chains of amino acids that extend into the cavity, especially the polar residue that interacts through hydrogen bonding and electrostatic interactions with the polar head group of the ligand []. An arginine or a glutamine residue is used for binding fatty acids or retinoids, respectively. The anti-parallel beta-barrel fold is also exploited by the lipocalins, which function similarly by binding smallhydrophobic molecules. Similarity at the sequence level, however, is lessobvious, beingconfined to a single short N-terminal motif.
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

0 Found In

1 Parent Features

Id Name Short Name Type
IPR000566 Lipocalin/cytosolic fatty-acid binding domain Lipocln_cytosolic_FA-bd_dom Domain

4 Publications

First Author Title Year Journal Volume Pages
Bernier I A survey on cytosolic non-enzymic proteins involved in the metabolism of lipophilic compounds: from organic anion binders to new protein families. 1987 Biochimie 69 1127-52
Glatz JF Cellular fatty acid-binding proteins: current concepts and future directions. 1990 Mol Cell Biochem 98 237-51
Ockner RK Historic overview of studies on fatty acid-binding proteins. 1990 Mol Cell Biochem 98 3-9
Jakoby MG Ligand-protein electrostatic interactions govern the specificity of retinol- and fatty acid-binding proteins. 1993 Biochemistry 32 872-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)