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Carp cDNA sequence encoding a putative diazepam-binding inhibitor/endozepine/acyl-CoA-binding protein

J L Chang¹, H J Tsai

¹Institute of Fisheries Science, National Taiwan University, Taipei, Taiwan.

Biochimica Et Biophysica Acta

|November 14, 1996

Summary

Researchers isolated and sequenced the common carp

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Area of Science:

Molecular Biology
Biochemistry
Comparative Genomics

Background:

Diazepam-binding inhibitor (DBI), also known as endozepine (EP) or acyl-CoA-binding protein (ACBP), is a conserved protein involved in various cellular processes.
Understanding the molecular characteristics of DBI/EP/ACBP in different species aids in comparative studies of protein function and evolution.

Purpose of the Study:

To isolate and sequence the full-length cDNA encoding common carp DBI/EP/ACBP.
To analyze the deduced amino acid sequence and compare it with homologous proteins from other species.

Main Methods:

Isolation and sequencing of full-length cDNA from common carp.
Bioinformatic analysis of the deduced amino acid sequence.
Sequence alignment and identity comparison with mammalian, amphibian, avian, and yeast DBI/EP/ACBP.

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Main Results:

A full-length cDNA sequence for common carp DBI/EP/ACBP was successfully obtained.
The deduced protein consists of 87 amino acids, lacking a signal peptide.
High sequence identity was observed between common carp and human (77%) and bovine (78%) DBI/EP/ACBP, with lower identity to rat, frog, duck, and yeast orthologs.

Conclusions:

The common carp DBI/EP/ACBP sequence has been characterized.
The findings provide insights into the evolutionary conservation of DBI/EP/ACBP across vertebrates and yeast.
This study contributes to the understanding of DBI/EP/ACBP function in fish models.