PMID:3004571

Citation	Fukushima, D, Kitamura, N and Nakanishi, S (1985) Nucleotide sequence of cloned cDNA for human pancreatic kallikrein. Biochemistry 24:8037-43
Abstract	Cloned cDNA sequences for human pancreatic kallikrein have been isolated and determined by molecular cloning and sequence analysis. The identity between human pancreatic and urinary kallikreins is indicated by the complete coincidence between the amino acid sequence deduced from the cloned cDNA sequence and that reported partially for urinary kallikrein. The active enzyme form of the human pancreatic kallikrein consists of 238 amino acids and is preceded by a signal peptide and a profragment of 24 amino acids. A sequence comparison of this with other mammalian kallikreins indicates that key amino acid residues required for both serine protease activity and kallikrein-like cleavage specificity are retained in the human sequence, and residues corresponding to some external loops of the kallikrein diverge from other kallikreins. Analyses by RNA blot hybridization, primer extension, and S1 nuclease mapping indicate that the pancreatic kallikrein mRNA is also expressed in the kidney and sublingual gland, suggesting the active synthesis of urinary kallikrein in these tissues. Furthermore, the tissue-specific regulation of the expression of the members of the human kallikrein gene family has been discussed.
Links	PubMed
Keywords	Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA/isolation & purification; DNA/metabolism; DNA Restriction Enzymes; Humans; Kallikreins/genetics; Pancreas/enzymology
edit table

Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:KLK1		GO:0008233: peptidase activity	ECO:0000314:		F		Figure 5 shows the preteolytic activity in Escherichia Coli after being introduced to the mutated plasmid DNA.	complete CACAO 9924

References

See Help:References for how to manage references in GONUTS.