Lipocalin/cytosolic fatty-acid binding domain (IPR000566)

Short name: Lipocln_cytosolic_FA-bd_dom

Overlapping homologous superfamilies

Domain relationships


Proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids share limited regions of sequence homology and a common tertiary structure architecture [PMID: 3622999, PMID: 1608945, PMID: 2217163, PMID: 7684291, PMID: 3238752]. This is an eight stranded antiparallel beta-barrel with a repeated + 1 topology enclosing a internal ligand binding site [PMID: 7684291, PMID: 2217163]. The name 'lipocalin' has been proposed [PMID: 3622999] for this protein family, but cytosolic fatty-acid binding proteins are also included. The sequences of most members of the family, the core or kernal lipocalins, are characterised by three short conserved stretches of residues, while others, the outlier lipocalin group, share only one or two of these [PMID: 1834059, PMID: 7684291]. Proteins known to belong to this family include alpha-1-microglobulin (protein HC); alpha-1-acid glycoprotein (orosomucoid) [PMID: 3064105]; aphrodisin; apolipoprotein D; beta-lactoglobulin; complement component C8 gamma chain [PMID: 1707134]; crustacyanin [PMID: 2026162]; epididymal-retinoic acid binding protein (E-RABP) [PMID: 8069623]; insectacyanin; odorant-binding protein (OBP); human pregnancy-associated endometrial alpha-2 globulin; probasin (PB), a rat prostatic protein; prostaglandin D synthase (EC: [PMID: 1723819]; purpurin; Von Ebner's gland protein (VEGP) [PMID: 7514123]; and lizard epididymal secretory protein IV (LESP IV) [PMID: 8486691].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.