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 27-MAR-2024, entry version 65. 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}. 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; 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 Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A. DR InterPro; IPR000668; Peptidase_C1A_C. DR InterPro; IPR039417; Peptidase_C1A_papain-like. DR InterPro; IPR013201; Prot_inhib_I29. DR PANTHER; PTHR12411:SF741; CATHEPSIN K; 1. DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1. 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; Cysteine proteinases; 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 //