Figure 2.

Arrestin protein family: multiple sequence alignment of phylogenetically diverse members. The alpha and beta classes of arrestins are distinct. Positions that may be widely conserved by common descent are yellow, beta/visual-specific are red and alpha-specific are blue (ambiguous in gray). Black positions in the Tail are the PPXY (or (P/L)PXY or "PY") motifs. PPXY motifs can have alternative residues in the first position. Notably, the sea urchin alpha arrestin has two PPXY and seven QPXY motifs. The sea urchin and nematode alphas also share the PY-like sequence (Y/F)APXYP(Y/F)Y. The arrestin domains are given below the alignment, n for N domain, c for C and t for Tail; italics show sequence not considered as part of the N and C domains according to Pfam. Shading on that line maps secondary structure elements on cone arrestin (symbol ARR3, HUGO nomenclature; aka arrestin 4, X-arrestin) – beta strands in gray and the one alpha helix in black [78]. Underlining highlights regions involved in receptor specificity, as described in Ref. [78] and references within. Two sets of intra-molecular interactions are important for keeping visual/beta arrestins in their basal conformation (see text): number symbols (#) mark residues that make up the "polar core"; asterisks (*) show residues involved in the "three-element interaction". Identifiers follow: fly a, D. melanogaster alpha arrestin CG18745-PA; nem worm a, nematode C. elegans alpha T12D8.4; nem worm b, beta F53H8.2; sea urchin, Strongylocentrotus purpuratus alpha XP_001175756; others are listed by gene name [see Additional file 2].

Alvarez BMC Evolutionary Biology 2008 8:222   doi:10.1186/1471-2148-8-222
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