ID   CATLL_PHACE             Reviewed;         324 AA.
AC   O97397; P81520;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Cathepsin L-like proteinase;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Phaedon cochleariae (Mustard beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX   NCBI_TaxID=80249;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Larval gut;
RX   PubMed=10612046; DOI=10.1016/s0965-1748(99)00104-6;
RA   Girard C., Jouanin L.;
RT   "Molecular cloning of cDNAs encoding a range of digestive enzymes from a
RT   phytophagous beetle, Phaedon cochleariae.";
RL   Insect Biochem. Mol. Biol. 29:1129-1142(1999).
CC   -!- TISSUE SPECIFICITY: Expressed in larval carcasses and gut, and adult
CC       gut. {ECO:0000269|PubMed:10612046}.
CC   -!- DEVELOPMENTAL STAGE: Larvae and adult, but not eggs.
CC       {ECO:0000269|PubMed:10612046}.
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; Y17903; CAA76927.1; -; mRNA.
DR   AlphaFoldDB; O97397; -.
DR   SMR; O97397; -.
DR   MEROPS; C01.143; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; 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   2: Evidence at transcript level;
KW   Digestion; Disulfide bond; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..?
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000223699"
FT   CHAIN           ?..324
FT                   /note="Cathepsin L-like proteinase"
FT                   /id="PRO_0000223700"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250"
FT   DISULFID        131..174
FT                   /evidence="ECO:0000250"
FT   DISULFID        165..206
FT                   /evidence="ECO:0000250"
FT   DISULFID        263..312
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35468 MW;  5E0F191D2C84067F CRC64;
     MKLIIALAAL IVVINAASDQ ELWADFKKTH ARTYKSLREE KLRFNIFQDT LRQIAEHNVK
     YENGESTYYL AINKFSDITD EEFRDMLMKN EASRPNLEGL EVADLTVGAA PESIDWRSKG
     VVLPVRNQGE CGSCWALSTA AAIESQSAIK SGSKVPLSPQ QLVDCSTSYG NHGCNGGFAV
     NGFEYVKDNG LESDADYPYS GKEDKCKAND KSRSVVELTG YKKVTASETS LKEAVGTIGP
     ISAVVFGKPM KSYGGGIFDD SSCLGDNLHH GVNVVGYGIE NGQKYWIIKN TWGADWGESG
     YIRLIRDTDH SCGVEKMASY PILA