Isolation of cDNA encoding a novel serpin of crayfish hemocytes.
We have cloned a serpin-type proteinase inhibitor from a crayfish hemocyte cDNA library. The deduced amino acid sequence consists of 429 amino acids with a putative signal peptide of 21 amino acids. The mature protein has a calculated molecular mass of 45,029 daltons. Identities ranging up to 38% were observed between the crayfish serpin and other members of the serpin family. Phylogenetic analysis shows that the crayfish serpin has a closer relationship to insect serpins than to other animal serpins. Phe369-Ser370 were proposed to be the P1-P1' residues of the inhibitor reactive site. This protein was found to be expressed in hemocytes but not in the hepatopancreas of the crayfish Pacifastacus leniusculus.
Liang
Z
Z
Department of Physiological Botany, University of Uppsala, Sweden.
Söderhäll
K
K
D000595:Amino Acid Sequence; D000818:Animals; D003400:Astacoidea / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D006434:Hemocytes / Q000201:enzymology*; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D015843:Serpins / Q000235:genetics*
D018076:DNA, Complementary; D015843:Serpins