Recombinant Human Beta-adducin (ADD2)

Uniprot Id

P35612

Target Species

Human

Target Name

ADD2

Target Full Name

Beta-adducin

Target Function

Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to the erythrocyte membrane receptor SLC2A1/GLUT1 and may therefore provide a link between the spectrin cytoskeleton to the plasma membrane. Binds to calmodulin. Calmodulin binds preferentially to the beta subunit.

Target Subcellular Location

Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side.

Target Protein Families

Aldolase class II family, Adducin subfamily

Target Tissue Specificity

Expressed mainly in brain, spleen, kidney cortex and medulla, and heart. Also expressed in human umbilical vein endothelial cells, human vascular smooth muscle cells, kidney tubular cells and K-562 cell line.

Target Synonyms

ADD 2; ADD2; ADDB; ADDB_HUMAN; Adducin 2 (beta); Adducin2; Beta adducin; Beta-adducin; Erythrocyte adducin subunit beta; OTTHUMP00000203378; OTTHUMP00000203908

Target Background

Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Alternatively spliced transcript variants have been described.