ID CATL2_FASHE Reviewed; 14 AA. AC P80342; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 02-SEP-2026, entry version 69. DE RecName: Full=Cathepsin L2; DE EC=3.4.22.15; DE Flags: Fragment; OS Fasciola hepatica (Liver fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; OC Rhabditophora; Neodermata; Trematoda; Digenea; Plagiorchiida; OC Echinostomata; Echinostomatoidea; Fasciolidae; Fasciola. OX NCBI_TaxID=6192; RN [1] RP PROTEIN SEQUENCE. RX PubMed=8033913; DOI=10.1111/j.1432-1033.1994.tb18969.x; RA Dowd A.J., Smith A.M., McGonicle S., Dalton J.P.; RT "Purification and characterisation of a second cathepsin L proteinase RT secreted by the parasitic trematode Fasciola hepatica."; RL Eur. J. Biochem. 223:91-98(1994). CC -!- FUNCTION: Thiol protease that assists the parasite in burrowing through CC the gut wall and liver of its mammalian host. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specificity close to that of papain. As compared to cathepsin CC B, cathepsin L exhibits higher activity toward protein substrates, CC but has little activity on Z-Arg-Arg-NHMec, and no peptidyl- CC dipeptidase activity.; EC=3.4.22.15; CC -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds. CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE- CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089, CC ECO:0000255|PROSITE-ProRule:PRU10090}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; S45655; S45655. DR DrugBank; DB12245; Triclabendazole. DR MEROPS; C01.093; -. DR BRENDA; 3.4.22.B60; 2230. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Hydrolase; Lysosome; Protease; KW Thiol protease. FT CHAIN 1..>14 FT /note="Cathepsin L2" FT /id="PRO_0000050539" FT NON_TER 14 SQ SEQUENCE 14 AA; 1605 MW; 9CAEAB74E9DA110A CRC64; AVPDKIDRRE SGYV //