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Literature DB >> 7513365

Evolution of prothrombin: isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin.

D K Banfield¹, D M Irwin, D A Walz, R T MacGillivray.

Abstract

The cDNA sequences of chicken and hagfish prothrombin have been determined. The sequences predict that prothrombin from both species is synthesized as a prepro-protein consisting of a putative Gla domain, two kringle domains, and a two-chain protease domain. Chicken and hagfish prothrombin share 51.6% amino acid sequence identity (313/627 residues). Both chicken and hagfish prothrombin are structurally very similar to human, bovine, rat, and mouse prothrombin and all six species share 41% amino acid sequence identity. Amino acid sequence alignments of human, bovine, rat, mouse, chicken, and hagfish prothrombin suggest that the thrombin B-chain and the propeptide-Gla domain are the regions most constrained for the common function(s) of vertebrate prothrombins.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 1994 PMID： 7513365 DOI： 10.1007/bf00166164

Source DB: PubMed Journal: J Mol Evol ISSN： 0022-2844 Impact factor: 2.395

63 in total

1. Structure of Ca2+ prothrombin fragment 1 including the conformation of the Gla domain.

Authors: M Soriano-Garcia; C H Park; A Tulinsky; K G Ravichandran; E Skrzypczak-Jankun
Journal: Biochemistry Date: 1989-08-22 Impact factor: 3.162

Review 2. Surface-dependent reactions of the vitamin K-dependent enzyme complexes.

Authors: K G Mann; M E Nesheim; W R Church; P Haley; S Krishnaswamy
Journal: Blood Date: 1990-07-01 Impact factor: 22.113

3. Simultaneous editing of multiple nucleic acid and protein sequences with ESEE.

Authors: E L Cabot; A T Beckenbach
Journal: Comput Appl Biosci Date: 1989-07

4. Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1.

Authors: C H Park; A Tulinsky
Journal: Biochemistry Date: 1986-07-15 Impact factor: 3.162

Review 5. The molecular basis of blood coagulation.

Authors: B Furie; B C Furie
Journal: Cell Date: 1988-05-20 Impact factor: 41.582

Review 6. Fibrinogen and fibrin.

Authors: R F Doolittle
Journal: Annu Rev Biochem Date: 1984 Impact factor: 23.643

7. Partial characterization of vertebrate prothrombin cDNAs: amplification and sequence analysis of the B chain of thrombin from nine different species.

Authors: D K Banfield; R T MacGillivray
Journal: Proc Natl Acad Sci U S A Date: 1992-04-01 Impact factor: 11.205

8. Vitamin K-dependent carboxylation. A synthetic peptide based upon the gamma-carboxylation recognition site sequence of the prothrombin propeptide is an active substrate for the carboxylase in vitro.

Authors: M M Ulrich; B Furie; M R Jacobs; C Vermeer; B C Furie
Journal: J Biol Chem Date: 1988-07-15 Impact factor: 5.157

Evolution of prothrombin: isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin.

1. Structure of Ca2+ prothrombin fragment 1 including the conformation of the Gla domain.

Review 2. Surface-dependent reactions of the vitamin K-dependent enzyme complexes.

3. Simultaneous editing of multiple nucleic acid and protein sequences with ESEE.

4. Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1.

Review 5. The molecular basis of blood coagulation.

Review 6. Fibrinogen and fibrin.

7. Partial characterization of vertebrate prothrombin cDNAs: amplification and sequence analysis of the B chain of thrombin from nine different species.

8. Vitamin K-dependent carboxylation. A synthetic peptide based upon the gamma-carboxylation recognition site sequence of the prothrombin propeptide is an active substrate for the carboxylase in vitro.

9. Recognition site directing vitamin K-dependent gamma-carboxylation resides on the propeptide of factor IX.

10. An Arg-Gly-Asp sequence within thrombin promotes endothelial cell adhesion.

1. Demonstration of the extrinsic coagulation pathway in teleostei: identification of zebrafish coagulation factor VII.

2. Thrombin a-chain: activation remnant or allosteric effector?

3. Correlated motions and residual frustration in thrombin.