CATL1_MOUSE
ID CATL1_MOUSE Reviewed; 334 AA.
AC P06797; Q91UZ0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Procathepsin L {ECO:0000305};
DE EC=3.4.22.15 {ECO:0000269|PubMed:8554545};
DE AltName: Full=Cathepsin L1;
DE AltName: Full=Major excreted protein;
DE Short=MEP;
DE AltName: Full=p39 cysteine proteinase;
DE Contains:
DE RecName: Full=Cathepsin L;
DE Contains:
DE RecName: Full=Cathepsin L heavy chain;
DE Contains:
DE RecName: Full=Cathepsin L light chain;
DE Flags: Precursor;
GN Name=Ctsl {ECO:0000312|MGI:MGI:88564}; Synonyms=Ctsl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3689328; DOI=10.1042/bj2460731;
RA Troen B.R., Gal S., Gottesman M.M.;
RT "Sequence and expression of the cDNA for MEP (major excreted protein), a
RT transformation-regulated secreted cathepsin.";
RL Biochem. J. 246:731-735(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2835398; DOI=10.1172/jci113497;
RA Joseph L.J., Chang L.C., Stamenkovich D., Sukhatme V.P.;
RT "Complete nucleotide and deduced amino acid sequences of human and murine
RT preprocathepsin L. An abundant transcript induced by transformation of
RT fibroblasts.";
RL J. Clin. Invest. 81:1621-1629(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3533924; DOI=10.1016/s0021-9258(18)66927-3;
RA Portnoy D.A., Erickson A.H., Kochan J., Ravetch J.V., Unkeless J.C.;
RT "Cloning and characterization of a mouse cysteine proteinase.";
RL J. Biol. Chem. 261:14697-14703(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE, AND GLYCOSYLATION AT ASN-221.
RC TISSUE=Liver;
RX PubMed=2275556; DOI=10.1016/0003-9861(90)90666-m;
RA Stearns N.A., Dong J., Pan J.X., Brenner D.A., Sahagian G.G.;
RT "Comparison of cathepsin L synthesized by normal and transformed cells at
RT the gene, message, protein, and oligosaccharide levels.";
RL Arch. Biochem. Biophys. 283:447-457(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/An;
RX PubMed=10516062; DOI=10.1128/jvi.73.11.9532-9543.1999;
RA Baer G.S., Ebert D.H., Chung C.J., Erickson A.H., Dermody T.S.;
RT "Mutant cells selected during persistent reovirus infection do not express
RT mature cathepsin L and do not support reovirus disassembly.";
RL J. Virol. 73:9532-9543(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 18-34; 273-292 AND 295-313, AND CATALYTIC ACTIVITY.
RX PubMed=8554545; DOI=10.1042/bj3120961;
RA Jean D., Hermann J., Rodrigues-Lima F., Barel M., Balbo M., Frade R.;
RT "Identification on melanoma cells of p39, a cysteine proteinase that
RT cleaves C3, the third component of complement: amino-acid-sequence
RT identities with procathepsin L.";
RL Biochem. J. 312:961-969(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 89-300.
RC STRAIN=BNL;
RX PubMed=3755373;
RA Denhardt D.T., Hamilton R.T., Parfett C.L.J., Edwards D.R., Pierre R.S.,
RA Waterhouse P., Nilson-Hamilton M.;
RT "Close relationship of the major excreted protein of transformed murine
RT fibroblasts to thiol-dependent cathepsins.";
RL Cancer Res. 46:4590-4593(1986).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9545226; DOI=10.1126/science.280.5362.450;
RA Nakagawa T., Roth W., Wong P., Nelson A., Farr A., Deussing J.,
RA Villadangos J.A., Ploegh H., Peters C., Rudensky A.Y.;
RT "Cathepsin L: critical role in Ii degradation and CD4 T cell selection in
RT the thymus.";
RL Science 280:450-453(1998).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10716919; DOI=10.1093/emboj/19.6.1187;
RA Felbor U., Dreier L., Bryant R.A., Ploegh H.L., Olsen B.R., Mothes W.;
RT "Secreted cathepsin L generates endostatin from collagen XVIII.";
RL EMBO J. 19:1187-1194(2000).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH CD74, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, SUBUNIT, AND PROTEOLYTICAL CLEAVAGE.
RX PubMed=11483509; DOI=10.1093/emboj/20.15.4055;
RA Lennon-Dumenil A.M., Roberts R.A., Valentijn K., Driessen C.,
RA Overkleeft H.S., Erickson A., Peters P.J., Bikoff E., Ploegh H.L.,
RA Wolf Bryant P.;
RT "The p41 isoform of invariant chain is a chaperone for cathepsin L.";
RL EMBO J. 20:4055-4064(2001).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12163394; DOI=10.1016/s0002-9440(10)64225-3;
RA Benavides F., Starost M.F., Flores M., Gimenez-Conti I.B., Guenet J.L.,
RA Conti C.J.;
RT "Impaired hair follicle morphogenesis and cycling with abnormal epidermal
RT differentiation in nackt mice, a cathepsin L-deficient mutation.";
RL Am. J. Pathol. 161:693-703(2002).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12021314; DOI=10.1084/jem.20011904;
RA Honey K., Nakagawa T., Peters C., Rudensky A.;
RT "Cathepsin L regulates CD4+ T cell selection independently of its effect on
RT invariant chain: a role in the generation of positively selecting peptide
RT ligands.";
RL J. Exp. Med. 195:1349-1358(2002).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH CD74,
RP AND ACTIVITY REGULATION.
RX PubMed=12417635; DOI=10.1084/jem.20020762;
RA Fiebiger E., Maehr R., Villadangos J., Weber E., Erickson A., Bikoff E.,
RA Ploegh H.L., Lennon-Dumenil A.M.;
RT "Invariant chain controls the activity of extracellular cathepsin L.";
RL J. Exp. Med. 196:1263-1269(2002).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11972068; DOI=10.1073/pnas.092637699;
RA Stypmann J., Glaeser K., Roth W., Tobin D.J., Petermann I., Matthias R.,
RA Moennig G., Haverkamp W., Breithardt G., Schmahl W., Peters C.,
RA Reinheckel T.;
RT "Dilated cardiomyopathy in mice deficient for the lysosomal cysteine
RT peptidase cathepsin L.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6234-6239(2002).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12782676; DOI=10.1172/jci200315990;
RA Friedrichs B., Tepel C., Reinheckel T., Deussing J., von Figura K.,
RA Herzog V., Peters C., Saftig P., Brix K.;
RT "Thyroid functions of mouse cathepsins B, K, and L.";
RL J. Clin. Invest. 111:1733-1745(2003).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12869695; DOI=10.1073/pnas.1531542100;
RA Yasothornsrikul S., Greenbaum D., Medzihradszky K.F., Toneff T., Bundey R.,
RA Miller R., Schilling B., Petermann I., Dehnert J., Logvinova A.,
RA Goldsmith P., Neveu J.M., Lane W.S., Gibson B., Reinheckel T., Peters C.,
RA Bogyo M., Hook V.;
RT "Cathepsin L in secretory vesicles functions as a prohormone-processing
RT enzyme for production of the enkephalin peptide neurotransmitter.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9590-9595(2003).
RN [18]
RP FUNCTION.
RX PubMed=15099520; DOI=10.1016/s1097-2765(04)00209-6;
RA Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A.,
RA Bogyo M., Nepveu A.;
RT "A cathepsin L isoform that is devoid of a signal peptide localizes to the
RT nucleus in S phase and processes the CDP/Cux transcription factor.";
RL Mol. Cell 14:207-219(2004).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Thiol protease important for the overall degradation of
CC proteins in lysosomes (Probable). Involved in the solubilization of
CC cross-linked TG/thyroglobulin and in the subsequent release of thyroid
CC hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in
CC the thyroid follicle lumen (PubMed:12782676). In neuroendocrine
CC chromaffin cells secretory vesicles, catalyzes the prohormone
CC proenkephalin processing to the active enkephalin peptide
CC neurotransmitter (PubMed:12869695). In thymus, regulates CD4(+) T cell
CC positive selection by generating the major histocompatibility complex
CC class II (MHCII) bound peptide ligands presented by cortical thymic
CC epithelial cells (PubMed:12021314). Also mediates invariant chain
CC processing in cortical thymic epithelial cells (PubMed:9545226). Major
CC elastin-degrading enzyme at neutral pH. Accumulates as a mature and
CC active enzyme in the extracellular space of antigen presenting cells
CC (APCs) to regulate degradation of the extracellular matrix in the
CC course of inflammation (PubMed:12417635). Secreted form generates
CC endostatin from COL18A1 (PubMed:10716919). Critical for cardiac
CC morphology and function (PubMed:11972068). Plays an important role in
CC hair follicle morphogenesis and cycling, as well as epidermal
CC differentiation (PubMed:12163394). Required for maximal stimulation of
CC steroidogenesis by TIMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P07154, ECO:0000269|PubMed:10716919,
CC ECO:0000269|PubMed:11972068, ECO:0000269|PubMed:12021314,
CC ECO:0000269|PubMed:12163394, ECO:0000269|PubMed:12417635,
CC ECO:0000269|PubMed:12782676, ECO:0000269|PubMed:12869695,
CC ECO:0000269|PubMed:9545226, ECO:0000305}.
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 Evidence={ECO:0000269|PubMed:8554545};
CC -!- ACTIVITY REGULATION: Long isoform of CD74/Ii chain stabilizes the
CC conformation of mature CTSL by binding to its active site and serving
CC as a chaperone to help maintain a pool of mature enzyme in endocytic
CC compartments and extracellular space of APCs (PubMed:11483509,
CC PubMed:12417635). IFNG enhances the conversion into the CTSL mature and
CC active form (PubMed:11483509). Inhibited by CST6. Inhibited by the
CC glycopeptide antibiotic teicoplanin. Inhibited by amantadine (By
CC similarity). {ECO:0000250|UniProtKB:P07711,
CC ECO:0000269|PubMed:11483509, ECO:0000269|PubMed:12417635}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:10716919};
CC -!- SUBUNIT: Dimer of a heavy and a light chain linked by disulfide bonds
CC (Probable). Interacts with Long isoform of CD74/Ii chain; the
CC interaction stabilizes the conformation of mature CTSL
CC (PubMed:11483509, PubMed:12417635). {ECO:0000269|PubMed:11483509,
CC ECO:0000269|PubMed:12417635, ECO:0000305|PubMed:11483509}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:11483509,
CC ECO:0000269|PubMed:12782676}. Apical cell membrane
CC {ECO:0000269|PubMed:12782676}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12782676}; Extracellular side
CC {ECO:0000269|PubMed:12782676}. Secreted, extracellular space
CC {ECO:0000269|PubMed:12417635}. Secreted {ECO:0000269|PubMed:10716919}.
CC Cytoplasmic vesicle, secretory vesicle, chromaffin granule
CC {ECO:0000250|UniProtKB:P25975}. Note=Localizes to the apical membrane
CC of thyroid epithelial cells. Released at extracellular space by
CC activated dendritic cells and macrophages (PubMed:12417635).
CC {ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:12782676}.
CC -!- TISSUE SPECIFICITY: Expressed in thymus, kidney and liver
CC (PubMed:9545226). Expressed in thyroid epithelial cells. Expressed in
CC cortical thymic epithelial cells (PubMed:9545226). Expressed by antigen
CC presenting cells (APCs) such as dendritic cells and macrophages
CC (PubMed:11483509, PubMed:12417635). {ECO:0000269|PubMed:11483509,
CC ECO:0000269|PubMed:12417635, ECO:0000269|PubMed:12782676,
CC ECO:0000269|PubMed:9545226}.
CC -!- PTM: During export along the endocytic pathway, pro-CTSL undergoes
CC several proteolytic cleavages to generate the CTSL single-chain and
CC two-chain mature forms, composed of a heavy chain linked to a light
CC chain by disulfide bonds (PubMed:11483509). Autocleavage; produces the
CC single-chain CTSL after cleavage of the propeptide. The cleavage can be
CC intermolecular (By similarity). {ECO:0000250|UniProtKB:P07711,
CC ECO:0000269|PubMed:11483509}.
CC -!- DISRUPTION PHENOTYPE: Enlarged thyroid follicles, reduced extension of
CC the thyroid epithelium and increased levels of Tg/thyroglobulin in the
CC thyroid follicles. Lysosomes are enlarged and CTSB/cathepsin B is mis-
CC localized to the apical membrane of thyroid epithelial cells. Serum
CC levels of thyroid hormone thyroxine (T4) are reduced. The phenotype is
CC more severe in CTSK/cathepsin K and CTSL double knockout mice
CC (PubMed:12782676). Mutants possess reduced levels of Met-enkephalin in
CC brain (PubMed:12869695). Mice show impaired CD4(+) T cell selection
CC (PubMed:12021314). They have reduced numbers of CD4(+) T cells in the
CC thymus and periphery and CD8(+) T cells relatively increased
CC (PubMed:9545226). One-year-old mutant mice show ventricular and atrial
CC enlargement associated with a comparatively small increase in relative
CC heart weight and severely impaired myocardial contraction. They show
CC interstitial fibrosis and pleomorphic nuclei (PubMed:11972068).
CC Cardiomyocytes contain multiple large and apparently fused lysosomes
CC characterized by storage of electron-dense heterogeneous material
CC (PubMed:11972068). Mutants have delayed hair follicle morphogenesis and
CC late onset of the first catagen stage. Their skin show mild epidermal
CC hyperplasia and hyperkeratosis, severe hyperplasia of the sebaceous
CC glands, and structural alterations of hair follicles (PubMed:12163394).
CC {ECO:0000269|PubMed:11972068, ECO:0000269|PubMed:12021314,
CC ECO:0000269|PubMed:12163394, ECO:0000269|PubMed:12782676,
CC ECO:0000269|PubMed:12869695, ECO:0000269|PubMed:9545226}.
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; X06086; CAA29470.1; -; mRNA.
DR EMBL; J02583; AAA37445.1; -; mRNA.
DR EMBL; M20495; AAA39984.1; -; Genomic_DNA.
DR EMBL; AF121837; AAD32136.1; -; mRNA.
DR EMBL; AF121838; AAD32137.1; -; mRNA.
DR EMBL; AF121839; AAD32138.1; -; mRNA.
DR EMBL; BC068163; AAH68163.1; -; mRNA.
DR EMBL; X04392; CAA27980.1; -; mRNA.
DR CCDS; CCDS26600.1; -.
DR PIR; S01177; KHMSL.
DR RefSeq; NP_034114.1; NM_009984.4.
DR RefSeq; XP_006517143.1; XM_006517080.1.
DR AlphaFoldDB; P06797; -.
DR SMR; P06797; -.
DR BioGRID; 198975; 4.
DR IntAct; P06797; 5.
DR MINT; P06797; -.
DR STRING; 10090.ENSMUSP00000021933; -.
DR BindingDB; P06797; -.
DR ChEMBL; CHEMBL5291; -.
DR MEROPS; C01.032; -.
DR GlyConnect; 2192; 7 N-Linked glycans (1 site).
DR GlyGen; P06797; 1 site, 7 N-linked glycans (1 site).
DR iPTMnet; P06797; -.
DR PhosphoSitePlus; P06797; -.
DR SwissPalm; P06797; -.
DR EPD; P06797; -.
DR jPOST; P06797; -.
DR PaxDb; P06797; -.
DR PeptideAtlas; P06797; -.
DR PRIDE; P06797; -.
DR ProteomicsDB; 279922; -.
DR DNASU; 13039; -.
DR Ensembl; ENSMUST00000021933; ENSMUSP00000021933; ENSMUSG00000021477.
DR Ensembl; ENSMUST00000222517; ENSMUSP00000152169; ENSMUSG00000021477.
DR GeneID; 13039; -.
DR KEGG; mmu:13039; -.
DR UCSC; uc007qyw.1; mouse.
DR CTD; 1514; -.
DR MGI; MGI:88564; Ctsl.
DR VEuPathDB; HostDB:ENSMUSG00000021477; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; P06797; -.
DR OMA; CSHPQGN; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P06797; -.
DR TreeFam; TF313739; -.
DR BioCyc; MetaCyc:MON-14812; -.
DR BRENDA; 3.4.22.15; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR BioGRID-ORCS; 13039; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ctsl; mouse.
DR PRO; PR:P06797; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P06797; protein.
DR Bgee; ENSMUSG00000021477; Expressed in ectoplacental cone and 272 other tissues.
DR ExpressionAtlas; P06797; baseline and differential.
DR Genevisible; P06797; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042583; C:chromaffin granule; ISS:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:BHF-UCL.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0043204; C:perikaryon; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0005773; C:vacuole; ISS:BHF-UCL.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:BHF-UCL.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0016807; F:cysteine-type carboxypeptidase activity; IDA:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:BHF-UCL.
DR GO; GO:0030984; F:kininogen binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISS:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO:MGI.
DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IMP:UniProtKB.
DR GO; GO:0048102; P:autophagic cell death; ISS:BHF-UCL.
DR GO; GO:0043373; P:CD4-positive, alpha-beta T cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0007154; P:cell communication; ISS:BHF-UCL.
DR GO; GO:0009267; P:cellular response to starvation; ISS:BHF-UCL.
DR GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
DR GO; GO:0046697; P:decidualization; IGI:MGI.
DR GO; GO:0060309; P:elastin catabolic process; IMP:UniProtKB.
DR GO; GO:0034230; P:enkephalin processing; ISS:UniProtKB.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; ISO:MGI.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISO:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; ISS:BHF-UCL.
DR GO; GO:0010259; P:multicellular organism aging; ISS:BHF-UCL.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0021675; P:nerve development; ISS:BHF-UCL.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:BHF-UCL.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:UniProtKB.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; ISS:BHF-UCL.
DR GO; GO:0009749; P:response to glucose; ISS:BHF-UCL.
DR GO; GO:0034698; P:response to gonadotropin; ISS:BHF-UCL.
DR GO; GO:0014070; P:response to organic cyclic compound; ISS:BHF-UCL.
DR GO; GO:0060008; P:Sertoli cell differentiation; ISS:BHF-UCL.
DR GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
DR GO; GO:0006590; P:thyroid hormone generation; IMP:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
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 Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:8554545"
FT PROPEP 18..113
FT /note="Activation peptide"
FT /id="PRO_0000026248"
FT CHAIN 114..333
FT /note="Cathepsin L"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT /id="PRO_0000450792"
FT CHAIN 114..288
FT /note="Cathepsin L heavy chain"
FT /id="PRO_0000026249"
FT PROPEP 289..290
FT /id="PRO_0000026250"
FT CHAIN 291..334
FT /note="Cathepsin L light chain"
FT /id="PRO_0000026251"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT ACT_SITE 276
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT SITE 106..107
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT SITE 107..108
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT SITE 112..113
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT SITE 113..114
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054,
FT ECO:0000269|PubMed:2275556"
FT DISULFID 135..178
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT DISULFID 169..211
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT DISULFID 269..322
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT CONFLICT 58
FT /note="M -> I (in Ref. 2; AAA39984/AAD32136/AAD32137/
FT AAD32138)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> R (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37547 MW; FE6747043307AD98 CRC64;
MNLLLLLAVL CLGTALATPK FDQTFSAEWH QWKSTHRRLY GTNEEEWRRA IWEKNMRMIQ
LHNGEYSNGQ HGFSMEMNAF GDMTNEEFRQ VVNGYRHQKH KKGRLFQEPL MLKIPKSVDW
REKGCVTPVK NQGQCGSCWA FSASGCLEGQ MFLKTGKLIS LSEQNLVDCS HAQGNQGCNG
GLMDFAFQYI KENGGLDSEE SYPYEAKDGS CKYRAEFAVA NDTGFVDIPQ QEKALMKAVA
TVGPISVAMD ASHPSLQFYS SGIYYEPNCS SKNLDHGVLL VGYGYEGTDS NKNKYWLVKN
SWGSEWGMEG YIKIAKDRDN HCGLATAASY PVVN
