CATL2_FASHE
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 03-AUG-2022, entry version 68.
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; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC 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}.
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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.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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