Gs. Marchetto et Hl. Henry, CLONING AND SEQUENCING OF THE CDNA-ENCODING THE AVIAN KIDNEY CAMP-DEPENDENT PROTEIN-KINASE INHIBITOR PROTEIN, Gene, 158(2), 1995, pp. 303-304
The endogenous inhibitor of cAMP-dependent protein kinase (PKA) is dow
n-regulated in the kidneys from vitamin-D-replete chicks as compared t
o vitamin-D-deficient chicks. Screening of a vitamin-D-deficient chick
kidney library resulted in the isolation of a 450-bp cDNA clone encod
ing the 76-amino acid (aa) protein kinase inhibitor (PKI). The deduced
aa sequence of avian PKI shares 80 and 41% identity with the mammalia
n PKI alpha and PKI beta 1 isoforms, respectively. The chick and mamma
lian PKI contain conserved N-terminal sequences, including the pseudo-
substrate site ((18)GRRNA(22)), which are required for potent inhibiti
on of the catalytic subunit of PKA. Chick kidney PKI contains ten uniq
ue aa in the C-terminal portion of the protein that are not shared wit
h the mammalian PKI alpha or beta isoforms.