Isolation of a cDNA encoding the chicken homologue of the human calcium-modulating cyclophilin ligand.
In order to identify important regions of the human CAML (calcium-modulating cyclophilin ligand) protein, a cDNA encoding the chicken homologue was isolated using low-stringency hybridization screening of a T-lymphocyte cDNA library. The deduced amino acid sequences of chicken and human CAML show areas of extensive conservation, suggesting an evolutionarily important role in signaling.
Bram
R J
RJ
Department of Experimental Oncology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. bram@stjude.org
D000591:Amino Acid Isomerases / Q000235:genetics*; D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D002352:Carrier Proteins / Q000235:genetics*; D002645:Chickens; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D015723:Gene Library; D006801:Humans; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D019696:Peptidylprolyl Isomerase; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction / Q000235:genetics; D013601:T-Lymphocytes / Q000737:chemistry
D002352:Carrier Proteins; D018076:DNA, Complementary; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase