The reference OMIM entry for this protein is 102680

Adducin 1; add1
Adducin, alpha

DESCRIPTION

Adducin is a 200-kD heterodimeric protein associated with the erythrocyte membrane skeleton, which binds to Ca(2+)/calmodulin (see 114180), promotes binding of spectrin to actin, and is a substrate for protein kinases C and A (Gardner and Bennett, 1986; Bennett et al., 1988). The name adducin comes from the Latin 'adducere,' meaning 'to bring together.'

CLONING

Adducin was first purified from human erythrocytes by Gardner and Bennett (1986) and subsequently isolated from bovine brain membranes (Bennett et al., 1988). Joshi and Bennett (1990) investigated the structure and function of the separate domains of alpha adducin. Joshi et al. (1991) isolated reticulocyte cDNAs for alpha- and beta- (ADD2; 102681) adducin. The deduced alpha-adducin protein contains 737 amino acids and shares approximately 49% sequence identity with beta adducin, suggesting evolution by gene duplication. Each adducin subunit has 3 distinct domains: a 39-kD N-terminal globular protease-resistant domain, connected by a 9-kD domain to a 33-kD C-terminal protease-sensitive tail comprised almost entirely by hydrophilic amino acids. The head domains of both alpha- and beta-adducin have limited sequence similarity with the N-terminal actin-binding motif present in members of the spectrin superfamily and actin gelation proteins. The C termini of both proteins contain an identical 22-amino acid sequence showing similarity to the MARCKS protein (177061). Northern blot analysis of rat tissues, K562 erythroleukemia cells, and reticulocytes demonstrated ubiquitous expression of alpha adducin. Goldberg et al. (1992) identified a 4-kb alpha-adducin transcript that was abundantly expressed in the caudate nucleus, the site of major neuronal loss in Huntington disease (HD; 143100). No sequence alterations specific to HD were discovered in sequencing the brain alpha-adducin cDNA from 2 HD patients and an age-matched control. Brain cDNA from both patients and controls showed 2 alternately spliced brain exons not previously described in erythrocyte cDNA. In a comprehensive assay of gene expression, Gilligan et al. (1999) showed the ubiquitous expression of alpha- and gamma-adducin (ADD3; 601568), in contrast to the restricted expression of beta-adducin. Beta-adducin was expressed at high levels in brain and hematopoietic tissues (bone marrow in humans, spleen in mice). See Gilligan and Bennett (1993) for a review of adducin and the other components of the junctional complex of the cell membrane skeleton.

MAPPING

By somatic cell hybrid analysis, Joshi et al. (1991) provisionally assigned the ADD1 gene to chromosome 4 and the ADD2 gene to chromosome 2. Both alpha- and beta-adducin show alternative splicing; thus, there may be several different heterodimeric or homodimeric forms of adducin, each with a different functional specificity. Using the technique of 'exon trapping' devised by Buckler et al. (1991), Taylor et al. (1992) identified exons corresponding to the alpha subunit of adducin within the 4p16.3 region where Huntington disease appeared to be located. They mapped the ADD1 gene immediately telomeric to D4S95. Goldberg et al. (1992) reported the isolation and cloning of cDNA for the brain alpha-adducin gene, which they found to be located within 20 kb of D4S95. Nasir et al. (1994) used an interspecific backcross to map the mouse Add1 gene to chromosome 5, within the region of syntenic homology with the short arm of human chromosome 4. ... More on the omim web site

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Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 102680 was added.