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  • Title: Limulus kexin: a new type of Kex2-like endoprotease specifically expressed in hemocytes of the horseshoe crab.
    Author: Kawabata S, Saeki K, Iwanaga S.
    Journal: FEBS Lett; 1996 May 20; 386(2-3):201-4. PubMed ID: 8647282.
    Abstract:
    A Kex2-like protease was identified in hemocytes of the horseshoe crab (Tachypleus tridentatus), named limulus kexin, and a full-length cDNA was obtained from a hemocyte cDNA library. The deduced amino acid sequence contains 752 residues, composed of five domains with a signal sequence, a propeptide, a catalytic domain, a Ser/Thr-rich domain, and a transmembrane domain. The domain organization is very similar to that of the yeast Kex2 except that limulus kexin does not have a cytoplasmic tail. The catalytic domain exhibits striking sequence identities with those of furins, especially Drosophila furin1 (79%). Northern blotting showed specific expression of limulus kexin in hemocytes, suggesting the involvement in proteolytic processing of the granule components of hemocytes.
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