Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen

FEBS Lett. 1987 Dec 10;225(1-2):188-94. doi: 10.1016/0014-5793(87)81155-9.


We have determined the primary structure of the alpha 1(IV)-chain of human type IV collagen by nucleotide sequencing of overlapping cDNA clones that were isolated from a human placental cDNA library. The present data provide the sequence of 295 amino acids not previously determined. Altogether, the alpha 1(IV)-chain contains 1642 amino acids and has a molecular mass of 157625 Da. There are 1413 residues in the collagenous domain and 229 amino acids in the carboxy-terminal globular domain. The human alpha 1(IV)-chain contains a total of 21 interruptions in the collagenous Gly-X-Y repeat sequence. These interruptions vary in length between two and eleven residues. The alpha 1(IV)-chain contains four cysteine residues in the triple-helical domain, four cysteines in the 15-residue long noncollagenous sequence at the amino-terminus and 12 cysteines in the carboxy-terminal NC-domain.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Basement Membrane / analysis
  • Collagen* / genetics
  • DNA / genetics
  • DNA / isolation & purification
  • DNA, Recombinant / isolation & purification
  • Disulfides
  • Female
  • Humans
  • Molecular Sequence Data
  • Placenta / analysis
  • Pregnancy
  • Repetitive Sequences, Nucleic Acid


  • DNA, Recombinant
  • Disulfides
  • Collagen
  • DNA

Associated data

  • GENBANK/Y00706