cDNA Cloning and Deduced Amino Acid Sequence of Prothrombin Activator (Ecarin) from Kenyan Echis carinatus Venom

Shinji Nishida, Taizo Fujita, Noriatsu Kohno, Hideko Atoda, Takashi Morita, Hiroyuki Takeya, Isao Kido, Mark J.I. Paine, Shun-Ichiro Kawabata, Sadaaki Iwanaga

研究成果: ジャーナルへの寄稿記事

79 引用 (Scopus)

抄録

The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis carinatus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus gramineus venom (61% identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jararaca venom (62% identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a “cysteine switch” motif (-Pro-Lys- Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191-616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64% identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His- Xaa-Xaa-Gly-Xaa-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg- Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30β (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.

元の言語英語
ページ(範囲)1771-1778
ページ数8
ジャーナルBiochemistry
34
発行部数5
DOI
出版物ステータス出版済み - 1 1 1995

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Cloning
Venoms
Prothrombin
Organism Cloning
Amino Acid Sequence
Disintegrins
Complementary DNA
Amino Acids
Protein Precursors
Metalloproteases
Cysteine
Bothrops
Astacoidea
Enzyme Precursors
Proteins
Sequence Homology
Chelation
Matrix Metalloproteinases
Gene Library
Base Pairing

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Nishida, S., Fujita, T., Kohno, N., Atoda, H., Morita, T., Takeya, H., ... Iwanaga, S. (1995). cDNA Cloning and Deduced Amino Acid Sequence of Prothrombin Activator (Ecarin) from Kenyan Echis carinatus Venom. Biochemistry, 34(5), 1771-1778. https://doi.org/10.1021/bi00005a034

cDNA Cloning and Deduced Amino Acid Sequence of Prothrombin Activator (Ecarin) from Kenyan Echis carinatus Venom. / Nishida, Shinji; Fujita, Taizo; Kohno, Noriatsu; Atoda, Hideko; Morita, Takashi; Takeya, Hiroyuki; Kido, Isao; Paine, Mark J.I.; Kawabata, Shun-Ichiro; Iwanaga, Sadaaki.

:: Biochemistry, 巻 34, 番号 5, 01.01.1995, p. 1771-1778.

研究成果: ジャーナルへの寄稿記事

Nishida, S, Fujita, T, Kohno, N, Atoda, H, Morita, T, Takeya, H, Kido, I, Paine, MJI, Kawabata, S-I & Iwanaga, S 1995, 'cDNA Cloning and Deduced Amino Acid Sequence of Prothrombin Activator (Ecarin) from Kenyan Echis carinatus Venom', Biochemistry, 巻. 34, 番号 5, pp. 1771-1778. https://doi.org/10.1021/bi00005a034
Nishida, Shinji ; Fujita, Taizo ; Kohno, Noriatsu ; Atoda, Hideko ; Morita, Takashi ; Takeya, Hiroyuki ; Kido, Isao ; Paine, Mark J.I. ; Kawabata, Shun-Ichiro ; Iwanaga, Sadaaki. / cDNA Cloning and Deduced Amino Acid Sequence of Prothrombin Activator (Ecarin) from Kenyan Echis carinatus Venom. :: Biochemistry. 1995 ; 巻 34, 番号 5. pp. 1771-1778.
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abstract = "The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a venomous gland cDNA library of Kenyan Echis carinatus. The cDNA sequence with 2379 base pairs encodes an open reading frame of 616 amino acids with a remarkable sequence homology to the putative precursor protein of trigramin from Trimeresurus gramineus venom (61{\%} identity) and a large hemorrhagin, jararhagin, from the pit viper Bothrops jararaca venom (62{\%} identity). Thus, ecarin, as well as jararhagin and trigramin, is translated as a precursor protein, which may be processed posttranslationally. The ecarin proprotein has a “cysteine switch” motif (-Pro-Lys- Met-Cys-Gly-Val-) similar to that involved in the activation of matrix metalloproteinase zymogens. The processed mature protein consists of 426 amino acid residues (residues 191-616), showing the strongest sequence similarity with that of Russell's viper venom factor X activator (RVV-X) heavy chain (64{\%} identity). Like RVV-X heavy chain, ecarin contains metalloproteinase, disintegrin, and cysteine-rich domains. The metalloproteinase domain has a typical zinc-chelating sequence (-His-Glu-Xaa-Xaa-His- Xaa-Xaa-Gly-Xaa-Xaa-His-), as found in crayfish astacin. In the disintegrin domain of ecarin, the Arg- Gly-Asp sequence is replaced by Arg-Asp-Asp, as found in the disintegrin domains of RVV-X heavy chain (Arg-Asp-Glu) and a guinea pig sperm fusion protein, PH-30β (Thr-Asp-Glu). These findings show that while there are structural and evolutionary relationships among these proteins, each has a unique functional activity.",
author = "Shinji Nishida and Taizo Fujita and Noriatsu Kohno and Hideko Atoda and Takashi Morita and Hiroyuki Takeya and Isao Kido and Paine, {Mark J.I.} and Shun-Ichiro Kawabata and Sadaaki Iwanaga",
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AU - Atoda, Hideko

AU - Morita, Takashi

AU - Takeya, Hiroyuki

AU - Kido, Isao

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