ID   CATL1_PARTE             Reviewed;         314 AA.
AC   Q94714; A0DWD1;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cathepsin L 1;
DE            EC=3.4.22.15;
DE   Flags: Precursor;
GN   ORFNames=GSPATT00020990001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 110-129 AND 181-204.
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).
RN   [2]
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).
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:0000255|PROSITE-
CC       ProRule:PRU10088}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK87348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X91754; CAA62869.1; -; mRNA.
DR   EMBL; CT868618; CAK87348.1; ALT_INIT; Genomic_DNA.
DR   PIR; S68783; S68783.
DR   AlphaFoldDB; Q94714; -.
DR   SMR; Q94714; -.
DR   STRING; 5888.CAK87348; -.
DR   MEROPS; C01.A54; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; Q94714; -.
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; IPR000169; Pept_cys_AS.
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   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..109
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8665938"
FT                   /id="PRO_0000026273"
FT   CHAIN           110..314
FT                   /note="Cathepsin L 1"
FT                   /id="PRO_0000026274"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   DISULFID        132..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..302
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  35159 MW;  56B4489D118FF097 CRC64;
     MMLLGASLYL NNTQEVSDEI DTANLYANWK MKYNRRYTNQ RDEMYRYKVF TDNLNYIRAF
     YESPEEATFT LELNQFADMS QQEFAQTYLS LKVPRTAKLN AANSNFQYKG AEVDWTDNKK
     VKYPAVKNQG SCGSCWAFSA VGALEINTDI ELNRKYELSE QDLVDCSGPY DNDGCNGGWM
     DSAFEYVADN GLAEAKDYPY TAKDGTCKTS VKRPYTHVQG FKDIDSCDEL AQTIQERTVA
     VAVDANPWQF YRSGVLSKCT KNLNHGVVLV GVQADGAWKI RNSWGSSWGE AGHIRLAGGD
     TCGICAAPSF PILG