ID   CATL2_PARTE             Reviewed;         314 AA.
AC   A0E358;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Cathepsin L 2;
DE            EC=3.4.22.15;
DE   Flags: Precursor;
GN   ORFNames=GSPATT00022898001;
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).
CC   -!- FUNCTION: May be involved in extracellular digestion. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK89725.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CT868656; CAK89725.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A0E358; -.
DR   SMR; A0E358; -.
DR   STRING; 5888.A0E358; -.
DR   MEROPS; C01.A54; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; A0E358; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; 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   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF953; CYSTEINE PROTEINASES SUPERFAMILY PROTEIN; 1.
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; Cysteine proteinases; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Secreted; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..109
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000307837"
FT   CHAIN           110..314
FT                   /note="Cathepsin L 2"
FT                   /id="PRO_0000307838"
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;  34935 MW;  2D580F2BB700AFD0 CRC64;
     MMLLGASLYL NNTQEVSDEI DTANLYANWK MKYNRRYTSQ RDEMYRFKVF SDNLNYIRAF
     QDSTESATYT LELNQFADMS QQEFASTYLS LRVPKTAKLN ASNANFQYKG AEVDWTDNKK
     VKYPAVKNQG SCGSCWAFSA VGALEINTDI ELNKKYELSE QDLVDCSGPY DNEGCNGGWM
     DSAFEYVADN GLAEAKDYPY TAKDGTCKTS VKRPYTHVQG FTDIDSCDEL AQAIQERTVS
     VAVDANPWQF YRSGVLSKCT KNLNHGVVLV GVQADGAWKI RNSWGSSWGE AGHIRLAGGD
     TCGICAAPSF PILG
//