ID   CATL_SCHMA              Reviewed;         319 AA.
AC   Q26534;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Cathepsin L;
DE            EC=3.4.22.15;
DE   AltName: Full=SMCL1;
DE   Flags: Precursor;
GN   Name=CL1;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=7838171; DOI=10.1016/0166-6851(94)90091-4;
RA   Smith A.M., Dalton J.P., Clough K.A., Kilbane C.L., Harrop S.A., Hole N.,
RA   Brindley P.J.;
RT   "Adult Schistosoma mansoni express cathepsin L proteinase activity.";
RL   Mol. Biochem. Parasitol. 67:11-19(1994).
CC   -!- FUNCTION: May be crucial for metabolism of host hemoglobin.
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: 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   EMBL; U07345; AAC46485.1; -; mRNA.
DR   AlphaFoldDB; Q26534; -.
DR   SMR; Q26534; -.
DR   STRING; 6183.Smp_034410.1; -.
DR   MEROPS; C01.166; -.
DR   eggNOG; KOG1542; Eukaryota.
DR   BRENDA; 3.4.22.B49; 5608.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
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.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_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; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..104
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026279"
FT   CHAIN           105..319
FT                   /note="Cathepsin L"
FT                   /id="PRO_0000026280"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..167
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..200
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..307
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  36136 MW;  9CFE68A3F1193479 CRC64;
     MPVNLEYLGF KLPGNVDEKY VQFKLKYRKQ YHETEDEIRF NIFKSNILKA QLYQVFVRGS
     AIYGVTPYSD LTTDEFARTH LTASWVVPSS RSNTPTSLGK EVNNIPKNFD WREKGAVTEV
     KNQGMCGSCW AFSTTGNVES QWFRKTGKLL SLSEQQLVDC DGLDDGCNGG LPSNAYESII
     KMGGLMLEDN YPYDAKNEKC HLKTDGVAVY INSSVNLTQD ETELAAWLYH NSTISVGMNA
     LLLQFYQHGI SHPWWIFCSK YLLDHAVLLV GYGVSEKNEP FWIVKNSWGV EWGENGYFRM
     YRGDGSCGIN TVATSAMIY