Limulus kexin: A new type of Kex2-like endoprotease specifically expressed in hemocytes of the horseshoe crab

Shun Ichiro Kawabata, Kazuko Saeki, Sadaaki Iwanaga

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)201-204
Number of pages4
JournalFEBS Letters
Volume386
Issue number2-3
DOIs
Publication statusPublished - May 20 1996

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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