Title : Cloning and deduced amino acid
sequence of a novel cartilage
protein (
CILP ) identifies a proform including a nucleotide
pyrophosphohydrolase
Abstract :
- The cDNA cloning and expression in vitro and in eukaryotic cells of a novel protein isolated from human articular cartilage, cartilage intermediate layer protein ( CILP ) is described
- A single 4
- 2-kilobase mRNA detected in human articular cartilage encodes a polypeptide of 1184 amino acids with a calculated molecular mass of 132.5 kDa
- The protein has a putative signal peptide of 21 amino acids, and is a proform of two polypeptides
- The amino-terminal half corresponds to CILP (molecular mass of 78.5 kDa, not including post-translational modifications) and the carboxyl-terminal half corresponds to a protein homologous to a porcine nucleotide pyrophosphohydrolase , NTPPHase (molecular mass of 51.8 kDa, not including post-translational modifications)
- CILP has 30 cysteines and six putative N-glycosylation sites
- The human homolog of porcine NTPPHase described here contains 10 cysteine residues and two putative N-glycosylation sites
- In the precursor protein the NTPPHase region is immediately preceded by a tetrapeptide conforming to a furin proteinase cleavage consensus sequence
- Expression of the full-length cDNA in a cell-free translation system and in COS-7 or EBNA cells indicates that the precursor protein is synthesized as a single polypeptide chain that is processed, possibly by a furin-like protease , into two polypeptides upon or preceding secretion
Output (sent_index, trigger,
protein,
sugar,
site):
- 6. N-glycosylation, , -, -, sites
- 7. N-glycosylation, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
- 0. protein, sequence
- 4. protein, peptide
- 6. CILP, cysteines
- 6. CILP, sites
- 8. NTPPHase, region
- 8. furin proteinase, sequence
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):