PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7503422-3	1995	The results obtained with cathepsin A purified from human placenta demonstrate that the enzyme has the highest affinity for substrates with large hydrophobic (Phe, Leu) or positively charged (Arg) amino acid residues in P1" position.	Leucine	164-167	cathepsin A	Homo sapiens	26-37	
9553770-8	1998	Whereas deamidase cleaves a variety of peptides with C-terminal or penultimate hydrophobic residues (e.g. substance P, angiotensin I, bradykinin, endothelin, fMet-Leu-Phe).	Leucine	163-166	cathepsin A	Homo sapiens	8-17	
34946974-5	2021	The polymorphism (85_87CTG>-) in exon 2 was a mutation causing a deletion of leucine, resulting in the change of the leucine 9-repeat (Leu9) to 8-repeat (Leu8) in the signal peptide region of CatA protein.	Leucine	77-84	cathepsin A	Homo sapiens	192-196	
34946974-5	2021	The polymorphism (85_87CTG>-) in exon 2 was a mutation causing a deletion of leucine, resulting in the change of the leucine 9-repeat (Leu9) to 8-repeat (Leu8) in the signal peptide region of CatA protein.	Leucine	117-124	cathepsin A	Homo sapiens	192-196