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   16-JUN-2009, entry version 55.
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; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Puerto Rican;
RX   MEDLINE=95140043; 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.,
RA   Hole N., 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: Specificity close to that of papain. As
CC       compared to cathepsin B, cathepsin L exhibits higher activity
CC       toward protein substrates, but has little activity on Z-Arg-Arg-
CC       NHMec, and no peptidyl-dipeptidase activity.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U07345; AAC46485.1; -; mRNA.
DR   HSSP; Q9UBX1; 1M6D.
DR   MEROPS; C01.018; -.
DR   BRENDA; 3.4.22.15; 1460.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; Peptidase_C1A; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   ProDom; PD000158; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 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; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL        1      ?       Potential.
FT   PROPEP        ?    104       Activation peptide (Potential).
FT                                /FTId=PRO_0000026279.
FT   CHAIN       105    319       Cathepsin L.
FT                                /FTId=PRO_0000026280.
FT   ACT_SITE    129    129       By similarity.
FT   ACT_SITE    265    265       By similarity.
FT   ACT_SITE    286    286       By similarity.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    216    216       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    231    231       N-linked (GlcNAc...) (Potential).
FT   DISULFID    126    167       By similarity.
FT   DISULFID    160    200       By similarity.
FT   DISULFID    258    307       By similarity.
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
//