Evolutionary and structural relationships among the group-specific component, albumin and α-fetoprotein

Funmei Yang, Victor J. Luna, Robert D. Mcanelly, Kathleen H. Naberhaus, Rod L. Cupples, Barbara H. Bowman

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

The group-specific component (Gc) is a plasma protein that binds vitamin D. Recent characterization of human Gc cDNA demonstrated homology with serum albumin and α-fetoprotein. This study compares the sequences of the three proteins and demonstrates a strong evolutionary relationship. Albumin, α-fetoprotein and Gc evolved from an ancestral gene containing an intragenic triplication. Comparison of the amino acid sequences and patterns of double disulfide bonds suggests that the Gc gene may have diverged from an ancestral gene earlier in evolution than the genes encoding albumin and α-fetoprotein. Analysis of the amino acid and nucleotide sequences of the three internal domains of Gc revealed 19-23% amino acid sequence identity and the localization of three homology blocks with 40-44% nucleotide sequence identity. The deduced amino sequence of Gc furnished data for comparing its molecular configuration based on the predicted secondary structure with those predicted form human albumin and α-fetoprotein. Utilization of Gc cDNA has also led to the identification of its genomic DNA and detectioin of a human DNA polymorphism.

Original languageEnglish (US)
Pages (from-to)8007-8017
Number of pages11
JournalNucleic acids research
Volume13
Issue number22
DOIs
StatePublished - Nov 25 1985

ASJC Scopus subject areas

  • Genetics

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