High impact information on Gzmf

• There are three potential asparagine-linked glycosylation sites in MCSP-1 and MCSP-3, and four in MCSP-2-deduced amino acid sequences [1].
• Genomic organization and subchromosomal in situ localization of the murine granzyme F, a serine protease expressed in CD8+ T cells [2].
• Granzyme F belongs to a closely related family of seven murine serine proteases stored in cytoplasmic granules of lymphoid cell populations [2].
• To characterize the genomic sequences responsible for its highly restricted expression, we isolated a cosmid clone and sequenced a 7.5-kb genomic fragment that contains the promoter region and all five exons of the murine granzyme F gene [2].
• By the use of two fluorochromes for simultaneous high resolution in situ hybridization, the granzyme F gene was localized in close proximity distally from the TCR alpha-chain locus on mouse chromosome 14 [2].

Anatomical context of Gzmf

• In contrast to the murine granzymes A to E and G, granzyme F is exclusively expressed in the CD4-CD8+ subset of peripheral T cells [2].

Associations of Gzmf with chemical compounds

• NH2-terminal amino acids of MCSP-2- and MCSP-3-predicted proteins were identical to those reported for granzyme E and F, respectively [1].

Other interactions of Gzmf

• The putative mature proteins of MCSP-2 and MCSP-3 are each composed of 228 amino acids with molecular weights of 25,477 and 25,360, respectively [1].
• Structure and evolution of the cytotoxic cell proteinase genes CCP3, CCP4 and CCP5 [3].
• Three proteins with inhibitory activity were thus purified, the serine esterase MCSP-3/granzyme F and the histones H2B and H3 [4].

References