ID   CATL_SARPE              Reviewed;         339 AA.
AC   Q26636;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Cathepsin L;
DE            EC=3.4.22.15;
DE   Contains:
DE     RecName: Full=Cathepsin L heavy chain;
DE   Contains:
DE     RecName: Full=Cathepsin L light chain;
DE   Flags: Precursor;
OS   Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Boettcherisca.
OX   NCBI_TaxID=7386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-27; 122-135; 139-154;
RP   200-208; 224-239 AND 306-319, FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8195162; DOI=10.1016/s0021-9258(17)36600-0;
RA   Homma K., Kurata S., Natori S.;
RT   "Purification, characterization, and cDNA cloning of procathepsin L from
RT   the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga
RT   peregrina (flesh fly), and its involvement in the differentiation of
RT   imaginal discs.";
RL   J. Biol. Chem. 269:15258-15264(1994).
CC   -!- FUNCTION: Important for the overall degradation of proteins in
CC       lysosomes. Required for differentiation of imaginal disks.
CC       {ECO:0000269|PubMed:8195162}.
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   -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:8195162}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during embryonic development with
CC       higher levels in first instar than in third instar.
CC       {ECO:0000269|PubMed:8195162}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D16533; BAA03970.1; -; mRNA.
DR   PIR; A53810; A53810.
DR   AlphaFoldDB; Q26636; -.
DR   SMR; Q26636; -.
DR   MEROPS; C01.092; -.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:8195162"
FT   PROPEP          18..121
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8195162"
FT                   /id="PRO_0000026269"
FT   CHAIN           122..294
FT                   /note="Cathepsin L heavy chain"
FT                   /id="PRO_0000026270"
FT   PROPEP          295..298
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026271"
FT   CHAIN           299..339
FT                   /note="Cathepsin L light chain"
FT                   /id="PRO_0000026272"
FT   ACT_SITE        146
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..186
FT                   /evidence="ECO:0000250"
FT   DISULFID        177..219
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..328
FT                   /note="Interchain (between heavy and light chains)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  37847 MW;  7401F3281A2FDA33 CRC64;
     MRTVLVALLA LVALTQAISP LDLIKEEWHT YKLQHRKNYA NEVEERFRMK IFNENRHKIA
     KHNQLFAQGK VSYKLGLNKY ADMLHHEFKE TMNGYNHTLR QLMRERTGLV GATYIPPAHV
     TVPKSVDWRE HGAVTGVKDQ GHCGSCWAFS STGALEGQHF RKAGVLVSLS EQNLVDCSTK
     YGNNGCNGGL MDNAFRYIKD NGGIDTEKSY PYEGIDDSCH FNKATIGATD TGFVDIPEGD
     EEKMKKAVAT MGPVSVAIDA SHESFQLYSE GVYNEPECDE QNLDHGVLVV GYGTDESGMD
     YWLVKNSWGT TWGEQGYIKM ARNQNNQCGI ATASSYPTV