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 journalArticle

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

Fingerprint

Furin
Horseshoe Crabs
Hemocytes
Protein Sorting Signals
Gene Library
Yeast
Peptide Hydrolases
Complementary DNA
Amino Acids
Processing
Catalytic Domain
Northern Blotting
Drosophila
Tail
Amino Acid Sequence
Yeasts

All Science Journal Classification (ASJC) codes

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

Cite this

Limulus kexin : A new type of Kex2-like endoprotease specifically expressed in hemocytes of the horseshoe crab. / Kawabata, Shun Ichiro; Saeki, Kazuko; Iwanaga, Sadaaki.

In: FEBS Letters, Vol. 386, No. 2-3, 20.05.1996, p. 201-204.

Research output: Contribution to journalArticle

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