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

FEBS Letters

Saeki, Kazuko¹  Kawabata, Shun-ichiro¹  Iwanaga, Sadaaki¹ 

[1] Department of Biology, Faculty of Science, Kyushu University 33, Fukuoka 812-81, Japan

关键词: Kex2-like protease;    Subtilisin-like proprotein convertase;    Kexin;    Furin;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/0014-5793(96)00440-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown