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Limulus kexin: a new type of Kex2‐like endoprotease specifically expressed in hemocytes of the horseshoe crab
Author(s) -
Kawabata Shun-ichiro,
Saeki Kazuko,
Iwanaga Sadaaki
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00440-1
Subject(s) - horseshoe crab , limulus , horseshoe (symbol) , biology , evolutionary biology , computer science , ecology , programming language
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.