Disease relevance of SLC10A3

• P1 and P3 proteins of influenza virus are required for complementary RNA synthesis [1].
• A synthetic peptide modeled after the sequence displayed by one of these phage, designated P3, was found to strongly inhibit the binding of laminin-1 to alpha 6 beta 1 [2].
• The P3 protein expressed from the recombinant vaccinia virus VV-P3 exhibited in vivo proteolytic activity as evident by processing of the polyprotein to generate the 3CD protein, consisting of a fusion between the 3Cpro and 3Dpol proteins [3].

High impact information on SLC10A3

• MRK preferentially phosphorylates R-P-X-S/T-P sites, with the preference for arginine at position -3 (P-3) being more stringent than for prolines at P-2 and P+1 [4].
• Thus, there is an essential interaction(s) between 3CD and other viral P2 or P3 protein products required for efficient RNA replication which is not fully achieved between proteins from the two different members of the same virus genus [5].
• In addition, it contains clusters of basic amino acids which may provide sites for the interaction of P3 protein with the capped primer, template, and/or other polymerase proteins during the transcriptive and replicative processes of influenza viral RNA [6].
• Based on knowledge obtained by mapping the WSN virus genome, it then was possible to determine that biologically functional P3 protein (coded for by RNA 1) and P1 protein (RNA 2) are required for complementary RNA synthesis of influenza virus [1].
• Analysis of 56 CVYV Spanish field isolates collected from 2001 to 2005 showed low genetic diversity (0.0026, 0.0013, and 0.0012 for the P1-Pro, P3, and CP regions, respectively) [7].

Biological context of SLC10A3

• A synthetic peptide with a scrambled P3 amino acid sequence barely inhibited the binding of laminin-1 to alpha 6 beta 1 [2].
• The population structure and genetic diversity of Cucumber vein yellowing virus (CVYV) from Spain were estimated by analyses of partial nucleotide sequences of the P1-proteinase (P1-Pro), P3 protein (P3), and the coat protein (CP) coding regions [7].
• A 435-bp minimal promoter was defined by transfection of HepG2 with luciferase expression constructs containing genomic fragments from the P3 start region [8].
• These findings imply a fundamental role for P3 in NAT1 regulation and define additional regions for genetic polymorphisms associated with enhanced cancer risk [8].

Anatomical context of SLC10A3

• The hepatoma-derived HepG2 cell line expressed a high level of P3 mRNA with the same spliced structure and start site pattern as found in normal tissues [8].
• In the present study, analysis of human RNAs representing 27 tissue types by reverse transcriptase-polymerase chain reaction (RT-PCR) and quantitative RT-PCR showed the upstream 51.5 kb promoter, designated P3, to be most active in specific tissues, including kidney, liver, lung, and trachea [8].

Analytical, diagnostic and therapeutic context of SLC10A3

• Like other vertebrate and invertebrate trypsin-like molecules, isoelectric-focusing studies with the natural Der p 3 protein have indicated that several isoforms exist [9].

References