4.6 Article

Genomic organization, expression profile, and characterization of the new protein PRA1 domain family, member 2 (PRAF2)

Journal

GENE
Volume 371, Issue 1, Pages 154-165

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.gene.2005.12.009

Keywords

chemokine receptor CCR5; comparative genormcs; immunohistochemistry; JM4; PRAF protein family; tumor tissue

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PRA1 domain family, member 2 (PRAF2) is a new 19 kDa protein with four putative transmembrane (TM) domains. PRAF2 (formerly designated JM4) belongs to a new protein family, which plays a role in the regulation of intracellular protein transport. Recently, PRAF2 was found to interact with the chemokine receptor CCR5 [Schweneker, M., Bachmann, A.S., Moelling, K., 2005. JM4 is a four-transmembrane protein binding to the CCR5 receptor. FEBS Lett. 579, 1751-1758]. In order to further study the function and regulation of PRAF2, we determined its genomic structure and its protein expression pattern in normal and cancerous human tissues. PRAF2 encodes a 178-residue protein, whose sequence is related to PRAF1 (PRA1/prenylin) and PRAF3 (JWA/GTRAP3-18). The human PRAF2 gene contains three exons separated by two introns and is located on human chromosome Xp11.23. The recombinant PRAF2 protein was readily expressed in Schneider 2 (S2) insect cells, and the native protein was detected in human tissues with strong expression in the brain, small intestine, lung, spleen, and pancreas. The protein was undetectable in tissue of the testes. Strong PRAF2 protein expression was also found in human tumor tissues of the breast, colon, lung, and ovary, with a weaker staining pattern in normal tissues of the same patient. Our studies show for the first time that the CCR5-interacting PRAT2 protein is expressed in several human tissues with a possible function in ER/Golgi transport and vesicular traffic. (c) 2006 Elsevier B.V. All rights reserved.

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