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Nucleotide sequence coding for the human type IV collagen α 2 chain cDNA reveals extensive homology with the NC‐1 domain of α 1 (IV) but not with the collagenous domain or 3 untranslated region
Author(s) -
Hostikka Sirkka Liisa,
Kurkinen Markku,
Tryggvason Karl
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80706-8
Subject(s) - complementary dna , coding region , nucleic acid sequence , untranslated region , homology (biology) , sequence (biology) , microbiology and biotechnology , biology , nucleotide , genetics , chemistry , dna , gene , messenger rna
We have isolated two overlapping cDNA clones that provide the complete nucleotide sequence coding for the NC‐1 domain and 3′‐untranslated region of the α 2 chain of human type IV collagen as well as a sequence encoding 232 residues of the collagenous domain. An extensive homology was observed between the sequences of the NC‐1 domain of the α 1 (IV) and α 2 (IV) chains, but considerably less between the sequences encoding collagenous and 3′‐untranslated regions. There were four interruptions in the collagenous sequence studied whereas the comparable region of the α 1 (IV) chain had only two. A potential oligosaccharide attachment site was found in a 6‐residue long interruption of the collagenous domain but none in the NC‐1 domain.