Primary structure of human transferrin receptor deduced from the mRNA sequence

Nature. 1984 Oct 18-24;311(5987):675-8. doi: 10.1038/311675b0.

Abstract

In vertebrates all iron is taken up via the carrier protein transferrin. The carrier first binds its receptor and the receptor-ligand complex is then internalized via coated pits. The transferrin receptor is a transmembrane glycoprotein (apparent molecular weight (MW) 180,000) composed of two disulphide-bonded sub-units (each of apparent MW 90,000) It contains three N-linked glycan units and is post-translationally modified with both phosphate and fatty acyl groups. Here we have determined the nucleotide sequence of the coding region of the human transferrin receptor mRNA and from this deduced the amino acid sequence of the protein. The receptor does not contain an N-terminal signal peptide but there is a membrane-spanning segment 62 amino acids from the N-terminus. It therefore has a somewhat unusual configuration with a small N-terminal cytoplasmic domain and a C-terminal extracellular domain of 672 amino acids.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cell Membrane / ultrastructure
  • Cloning, Molecular
  • DNA / metabolism
  • DNA Restriction Enzymes
  • Genes*
  • Humans
  • RNA, Messenger / genetics*
  • Receptors, Cell Surface / analysis
  • Receptors, Cell Surface / genetics*
  • Receptors, Transferrin
  • Transferrin / metabolism

Substances

  • RNA, Messenger
  • Receptors, Cell Surface
  • Receptors, Transferrin
  • Transferrin
  • DNA
  • DNA Restriction Enzymes

Associated data

  • GENBANK/X01060