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 language | English |
|---|---|
| Pages (from-to) | 201-204 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 386 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - May 20 1996 |
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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 journal › Article
}
TY - JOUR
T1 - Limulus kexin
T2 - A new type of Kex2-like endoprotease specifically expressed in hemocytes of the horseshoe crab
AU - Kawabata, Shun Ichiro
AU - Saeki, Kazuko
AU - Iwanaga, Sadaaki
PY - 1996/5/20
Y1 - 1996/5/20
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=0029929981&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(96)00440-1
DO - 10.1016/0014-5793(96)00440-1
M3 - Article
C2 - 8647282
AN - SCOPUS:0029929981
VL - 386
SP - 201
EP - 204
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2-3
ER -