AF189: Hemopexin family
The hemopexin family is named after hemopexin, a serum glycoprotein that binds heme and transports it to the liver for breakdown and iron recovery. Structurally, hemopexin consists of two similar halves of approximately 200 amino acid residues connected by a histidine-rich hinge region. Each half is itself formed by the repetition of a basic unit of 35 to 45 residues. Hemopexin-like domains have been found also in other types of proteins :
- Vitronectin is a cell adhesion and spreading factor found in plasma and tissues.
- Matrixins are members of the matrix metalloproteinase family that cleave extracellular matrix constituents.
- Seed albumins are legume seed proteins with lectin and heme-binding activities. They are possibly involved in regulating polyamine metabolism during seed development .
Allergens from this family
Vig r 4, a seed albumin from mung bean was characterized as pepsin-resistant, IgE-binding protein .
Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins.
J Leukoc Biol 2007, 81, 870-92. [PubMed] [Full Text]
Biochemical and functional characterization of an albumin protein belonging to the hemopexin superfamily from Lens culinaris seeds.
J Agric Food Chem 2011, 59, 9637-44. [PubMed] [Full Text]
Potential allergens of green gram (Vigna radiata L. Millsp) identified as members of cupin superfamily and seed albumin.
Clin Exp Allergy 2011, 41, 1157-68. [PubMed] [Full Text]
Links to Pfam
Family-defining Pfam domains (at least one of these domains is present in each family member):
Links to Wikipedia
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