The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning

Cell. 1984 Nov;39(1):49-59. doi: 10.1016/0092-8674(84)90190-9.


Synthetic oligonucleotide probes have been used to identify two overlapping cDNA clones that represent the entire coding region of the mRNA for the major intrinsic protein (MIP) of bovine lens cell membrane. Hybridization studies indicate that bovine MIP is encoded by a single-copy gene. The cDNA hybridizes to the rat genome, but MIP mRNA is not detected in rat liver. Analysis of the deduced amino acid sequence provides support for the potential role of MIP as a junctional protein. The structure predicted for MIP suggests that it traverses the lipid bilayer six times with both carboxy and amino termini on the cytoplasmic side, and that it has at least one amphiphilic transmembrane segment, as expected if the protein were to participate in the formation of an aqueous channel.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aquaporins
  • Base Sequence
  • Cattle
  • Cell Membrane / metabolism
  • Cloning, Molecular*
  • DNA / metabolism*
  • DNA Restriction Enzymes
  • Eye Proteins / genetics*
  • Genes*
  • Lens, Crystalline / cytology
  • Lens, Crystalline / metabolism*
  • Membrane Glycoproteins*
  • Nucleic Acid Conformation
  • Poly A / genetics
  • RNA / genetics
  • RNA, Messenger / genetics


  • Aquaporins
  • Eye Proteins
  • Membrane Glycoproteins
  • RNA, Messenger
  • aquaporin 0
  • Poly A
  • RNA
  • DNA
  • DNA Restriction Enzymes

Associated data

  • GENBANK/K02818