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.
Department of Experimental Oncology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. bram@stjude.org
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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