Structure and chromosome assignment of the murine p36 calpactin I heavy chain gene

Abstract

p36 is a major substrate of both viral and growth factor receptor associated protein kinases. This protein has recently been named calpactin I heavy chain since it is the large subunit of a Ca2(+)-dependent phospholipid and actin binding heterotetramer. The primary structure of p36 has been determined from analysis of cloned cDNA. The protein contains 338 amino acids, has an approximate molecular weight of 39,000, and is comprised of several distinct domains, including four 75 amino acid repeats. From two overlapping cosmid clones isolated from different mouse genomic liver libraries, the complete intron/exon structure of the p36 gene was determined and the 5' and 3' noncoding regions of the gene were analyzed. The coding and 3' untranslated region of the p36 gene contains 12 exons which range in size from 48 to 322 base pairs (bp) with an average size of 107 bp. The repeat structures found at the protein level are not delineated by single exons, but the N-terminal p11-binding domain is encoded by a single exon. Structural mapping of the gene demonstrated that the lengths of the first two introns in the coding region are together approximately 6 kilobases (kb), while the other introns range in size from 600 to 3600 bp with an average size of 1650 bp. The p36 gene is at least 22 kb in length and has a coding sequence of approximately 1 kb, representing only 4.5% of the gene.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino acid sequence analysis of the annexin super‐gene family of proteins

“…Amiguet et al [28] have described the 22-exon structure for the AIIM gene. They observed that the intron locations do not correspond with the boundaries between the annexin repeats, although the 4/5 (position 19/20 AIIM2) and 10/11 (AIIM4) exon boundaries occur at equivalent positions within repeats 2 and 4 respectively.…”

Structure of the human annexin VI gene.

“…2 of which 10 out of 26 have split codons. The frequency of split codons in other annexin genes is similar, typically 4 of 12 (15)(16)(17)(18)(19)(20). The first coding exon is 43 bp long, smaller than the corresponding exons of the annexin I and I genes, and consistent with the fact that the N-terminal sequence prior to the first protein repeat is smaller in annexin VI than in either annexins I or II.…”

“…The first coding exon is 43 bp long, smaller than the corresponding exons of the annexin I and I genes, and consistent with the fact that the N-terminal sequence prior to the first protein repeat is smaller in annexin VI than in either annexins I or II. The sizes of the remaining coding exons are identical to those of the corresponding exons of the annexin I and II genes (15)(16)(17)(18)(19)(20). The exceptions to this are exon 21 that is only 18 nt and is alternatively spliced (2) and exon 26 that is 406 bp and includes the translation stop codon and 3' untranslated sequence.…”

“…The boundaries of exons 4,5,7,8,9,11,13,15,20,23, and 24 were sequenced using complementary pairs of exonspecific oligonucleotides designed to lie in the middle of exons whose positions were predicted from the intron-exon organization of those annexin genes so far characterized (15)(16)(17)(18)(19)(20). Sequencing reactions were performed in the presence of Mn2+ so that sequence close to the primer could be determined, as recommended in the United States Biochemical Sequenase handbook.…”

“…Several groups have recently started to investigate the annexin I and II genes to gain insight into the determinants of specific and common patterns of gene regulation. The organization of the annexin I gene is completely conserved among humans, rats, mice, and pigeons (15)(16)(17) (although there are differences in intron sizes); likewise the human and murine annexin II genes are conserved (18,19). Most striking is the observation that the positions of the intron-exon boundaries within the core domains of the annexin I and II genes are almost exactly conserved (20).…”