ID   CATL_BRUPA              Reviewed;         395 AA.
AC   O17473;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cathepsin L-like;
DE            EC=3.4.22.15;
DE   Flags: Precursor;
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Selzer P.M., Huong X., Britton C., McKerrow J.H.;
RT   "Cathepsin L-like cysteine protease from Brugia pahangi third stage
RT   larvae.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   3D-STRUCTURE MODELING OF 182-395, AND DISULFIDE BONDS.
RA   Selzer P.M., Chen X., Cohen F.E., McKerrow J.H.;
RT   "Molecular model of Brugia pahangi third-stage larvae cysteine protease.";
RL   Submitted (JUL-1998) to the PDB data bank.
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   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AF031819; AAB86867.1; -; mRNA.
DR   AlphaFoldDB; O17473; -.
DR   SMR; O17473; -.
DR   MEROPS; C01.070; -.
DR   PRIDE; O17473; -.
DR   Proteomes; UP000038020; Genome Assembly.
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; 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.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..181
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026293"
FT   CHAIN           182..395
FT                   /note="Cathepsin L-like"
FT                   /id="PRO_0000026294"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        342
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250"
FT   DISULFID        203..246
FT                   /evidence="ECO:0000269|Ref.2"
FT   DISULFID        237..278
FT                   /evidence="ECO:0000269|Ref.2"
FT   DISULFID        337..385
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   395 AA;  44549 MW;  6EC65C20333BE2D1 CRC64;
     MWTIAQLAVF AILALADFAV AGEIEQLKEV LGKFNKDYKQ GNMTRLASDF RSALKEYGDG
     QQGESTVVQE FLKKTEDNGE QRAMEKLETE WKDYVTALGK HYDQKENNFR MAIFESNELM
     TERINKKYEQ GLVSYTTALN DLADLTDEEF MVRNGLRLPN QTDLRGKRQT SEFYRYDKSE
     RLPDQVDWRT KGAVTPVRNQ GECGSCYAFA TAAALEAYHK QMTGRLLDLS PQNIVDCTRN
     LGNNGCSGGY MPTAFQYASR YGIAMESRYP YVGTEQRCRW QQSIAVVTDN GFNEIQPGDE
     LALKHAVAKR GPVVVGISGS KRSFRFYKDG VYSEGNCGRP DHAVLAVGYG THPSYGDYWI
     VKNSWGTDWG KDGYVYMARN RGNMCHIASA ASFPI