Description
Product Characteristics:
FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.
Synonyms: CAAX farnesyltransferase alpha subunit, Farnesyl protein transferase alpha subunit, Farnesyltransferase CAAX box alpha, Farnesyltransferase, CAAX box, alpha, FPTA, FTase alpha, GGTase I alpha, PGGT1A, Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit, Protein prenyltransferase alpha subunit repeat containing 2, PTAR2, Ras proteins prenyltransferase alpha, Ras proteins prenyltransferase subunit alpha, Type I protein geranyl geranyltransferase alpha subunit, FNTA_HUMAN.
Target Information: Prenyltransferases can attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of proteins with a C-terminal CAAX box. CAAX geranylgeranyltransferase and CAAX farnesyltransferase are heterodimers that share the same alpha subunit but have different beta subunits. This gene encodes the alpha subunit of these transferases. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 11 and 13. [provided by RefSeq, May 2010]