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J. Biol. Chem., Vol. 269, Issue 42, 26172-26177, Oct, 1994
A Leinonen, M Mariyama, T Mochizuki, K Tryggvason and ST Reeders
The entire sequence of the human alpha 4(IV) collagen chain was determined
from cDNA clones and polymerase chain reaction-amplified DNAs. The complete
translation product has 1,690 amino acid residues and the processed alpha
4(IV) chain proper 1,652 residues. There is a 38-residue putative signal
peptide, a 1,421-residue collagenous domain starting with a 23-residue
noncollagenous sequence, and a 231-residue NC1 domain. The
Gly-Xaa-Yaa-repeat sequence of the collagenous domain is interrupted at 26
locations by noncollagenous sequences of 1-12 residues in length. The alpha
4(IV) chain contains 31 cysteine residues of which 18 are conserved in the
other type IV collagen alpha chains. The calculated molecular weight of the
mature alpha 4(IV) chain is 164,123. Analysis of the primary structure
showed that the alpha 4(IV) chain belongs to the alpha 2-like type IV
collagen chains together with alpha 2(IV) and alpha 6(IV). Northern
analyses with RNA from several human fetal tissues revealed quite similar
expression patterns for the alpha 4(IV) and alpha 3(IV) chains, but there
were also distinct differences in some tissues. The expression patterns of
alpha 5(IV) and alpha 6(IV) differed extensively between each other and
they also differed from those of alpha 3(IV) and alpha 4(IV).
Complete primary structure of the human type IV collagen alpha 4(IV) chain. Comparison with structure and expression of the other alpha (IV) chains
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06536.
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