High impact information on Acp26Aa

• Moreover, CG11864 itself is processed inside males while en route to the female and before its action in processing ovulin and Acp36DE [1].
• The egg-laying hormone ovulin (Acp26Aa) is among the most rapidly evolving proteins in the Drosophila genome [2].
• One seminal-fluid protein, ovulin (Acp26Aa), stimulates an early step in the egg-laying process, the release of oocytes by the ovary [3].
• By using this assay to assess the functionality of ovulin's cleavage products, we find that two of the four cleavage products of ovulin can stimulate ovulation independently [3].
• Three seminal fluid peptides elicit postmating responses: ovulin, sex-peptide (SP), and DUP99B [4].

Biological context of Acp26Aa

• Rates of indel substitution within Acp26Aa in the D. pseudoobscura subgroup were up to several times those in noncoding regions of the Drosophila genome [5].
• An early function is necessary to promote cell proliferation, whereas a late function, which regulates the expression of accessory gland products such as the sex peptide and Acp26Aa protein, is essential for maturation and differentiation of accessory glands [6].
• Positive selection and the molecular evolution of a gene of male reproduction, Acp26Aa of Drosophila [7].
• To know if selection has been operating in the recent past and to understand the details of its dynamics, we obtained DNA sequences of Acp26Aa and the nearby Acp26Ab gene from 39 D. melanogaster chromosomes [8].
• Acp26Aa acts specifically on the process of ovulation (the release of mature eggs from the ovaries), which is initiated 1.5 h after mating [9].

Anatomical context of Acp26Aa

• To address where and how seminal fluid proteins enter the hemolymph of the mated female, we compared the kinetics of transfer and localization in mated females of two seminal fluid proteins that enter the hemolymph (Acp26Aa and Acp62F) and one that does not (Acp36DE) [10].

Associations of Acp26Aa with chemical compounds

• We also generated transgenic flies that produce Acp26Aa tagged with Aequorea victoria green fluorescent protein (GFP) to monitor its transfer in vivo [10].

Other interactions of Acp26Aa

• Different forces drive the evolution of the Acp26Aa and Acp26Ab accessory gland genes in the Drosophila melanogaster species complex [11].
• We also found several indel substitutions and polymorphisms in Acp26Aa and Acp32CD [5].
• Four loci [Acp26Aa, Fbp2, Vha68-1, and Su(H)] were previously found to deviate from a neutral mutation-drift equilibrium as a consequence of one or several selective sweeps [12].

References