Coding sequence and alternative splicing of the mouse alpha 1(XI) collagen gene (Col11a1).
Several overlapping cDNA clones corresponding to the entire coding sequence of the mouse alpha 1(XI) collagen gene (Col11 a1) were isolated. The conceptual amino acid translation indicated a high degree of sequence identity (93%) with the human alpha 1(XI) chain. The cloning experiments also revealed alternative splicing of the sequence coding for 85 residues located within the acidic region of the amino-globular domain of alpha 1(XI). Analysis of RNA samples from different embryonic tissues suggested that alternative splicing might be confined to tissue destined to become bone.
Department of Molecular Biology and Biochemistry, Okayama University Medical School, Japan.
H
H
Yoshioka
K
K
Inoguchi
M
M
Khaleduzzaman
Y
Y
Ninomiya
K
K
Andrikopoulos
F
F
Ramirez
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D003094:Collagen / Q000235:genetics*; D018076:DNA, Complementary / Q000235:genetics; D005260:Female; D005796:Genes; D006801:Humans; D008297:Male; D051379:Mice / Q000235:genetics*; D008969:Molecular Sequence Data; D009115:Muridae / Q000235:genetics; D012326:RNA Splicing; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013329:Structure-Activity Relationship
D018076:DNA, Complementary; D003094:Collagen