The cDNA encoding porcine RACK1 protein was isolated from porcine spleen cD
NA library. The deduced protein sequence of porcine RACK1 cDNA shows that i
t contains 317 amino acid residues, and shares nearly 100% identity with it
s vertebrate counterparts. Noticeably, the RACK1 protein-was differentially
expressed in various porcine tissues. High expression of RACK1 protein was
observed in the tissues including thymus, pituitary, spleen and liver, whe
reas there was no detectable expression in muscle. The genomic DNA of porci
ne RACK1 with approximate 7.5 kb was constructed by both polymerase chain r
eaction amplification and genomic library screening. It consists of eight e
xons intervened by seven introns, and most of the intron/exon splice sites
conform to the GT/AG rule. The promoter region contains functional serum re
sponse element, YY1-like binding site and AP1 site, which is supported by t
he finding that the expression of RACK1 gene in cultured porcine ST cells h
as a serum response as well as a TPA response. (C) 1999 Elsevier Science B.
V. All rights reserved.