ID   CATL3_PARTE             Reviewed;         308 AA.
AC   Q94715; A0E163;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative cathepsin L 3;
DE            EC=3.4.22.15;
DE   Flags: Precursor;
GN   ORFNames=GSPATT00022199001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-308.
RC   STRAIN=Stock 51;
RX   PubMed=8665938; DOI=10.1111/j.1432-1033.1996.0198q.x;
RA   Voelkel H., Kurz U., Linder J., Klumpp S., Gnau V., Jung G., Schultz J.E.;
RT   "Cathepsin L is an intracellular and extracellular protease in Paramecium
RT   tetraurelia: purification, cloning, sequencing and specific inhibition by
RT   its expressed propeptide.";
RL   Eur. J. Biochem. 238:198-206(1996).
CC   -!- FUNCTION: May be involved in extracellular digestion.
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
CC   -!- CAUTION: This protein may be non-functional as it lacks the cysteine
CC       active site residue which is replaced by Gly-132. {ECO:0000305}.
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DR   EMBL; CT868652; CAK89030.1; -; Genomic_DNA.
DR   EMBL; X91756; CAA62871.1; -; mRNA.
DR   PIR; S68784; S68784.
DR   RefSeq; XP_001456427.1; XM_001456390.1.
DR   AlphaFoldDB; Q94715; -.
DR   SMR; Q94715; -.
DR   STRING; 5888.CAK89030; -.
DR   BindingDB; Q94715; -.
DR   ChEMBL; CHEMBL4097; -.
DR   EnsemblProtists; CAK89030; CAK89030; GSPATT00022199001.
DR   GeneID; 5042212; -.
DR   KEGG; ptm:GSPATT00022199001; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_3_1; -.
DR   InParanoid; Q94715; -.
DR   OMA; IRNQGKC; -.
DR   PRO; PR:Q94715; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..110
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026275"
FT   CHAIN           111..308
FT                   /note="Putative cathepsin L 3"
FT                   /id="PRO_0000026276"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
FT   SITE            132
FT                   /note="Ancestral active site Cys"
FT   DISULFID        129..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        254..298
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  35189 MW;  5615E8B6308FC4A5 CRC64;
     MKQFLTAAIV TLLMTAGYYH LQEDDTNDFE RWALKNNKFY TESEKLYRME IYNSNKRMIE
     EHNQREDVTY QMGENQFMTL SHEEFVDLYL QKSDSSVNIM GASLPEVQLE GLGAVDWRNY
     TTVKEQGQCA SGWAFSVSNS LEAWYAIRGF QKINASTQQI VDCDYNNTGC SGGYNAYAME
     YVLRVGLVSS TNYPYVAKNQ TCKQSRNGTY FINGYSFVGG SQSNLQYYLN NYPISVGVEA
     SNWQFYRSGL FSNCSSNGTN HYALAVGFDS ANNWIVQNSW GTQWGESGNI RLYPQNTCGI
     LNYPYQVY