STRUCTURAL AND FUNCTIONAL-ANALYSIS OF THE PORCINE SECRETORY CARRIER MEMBRANE-PROTEIN-1 GENE (SCAMP1)

The secretory carrier membrane proteins (SCAMPs) are highly conserved integral vesicle membrane components of the post-Golgi secretory and e ndocytic pathways. We have isolated and characterized the porcine SCAM PI cDNA and gene coding for a variant of the SCAMP family. The SCAMPI cDNA has a length of 3827 bp including a 133-bp 5' and 2701-bp 3' untr anslated region. The mRNA has an open reading frame of 1014 nt coding for a protein of 338 amino acids with a calculated molecular mass of 3 7.9 kDa and a pI of 7.9. The porcine SCAMPI is 97.04% identical with t he human and rat paralogs, respectively. The SCAMPI gene consists of n ine exons with sizes ranging from 78 to 2842 bp and spans at least 70 kb of genomic DNA on porcine Chromosome (Chr) 2q21-q22. The promoter o f the SCAMPI gene is TATA-box-less, and transcription starts at a G-nu cleotide 133 nt upstream the start codon.