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Showing Protein Procathepsin L (HMDBP13477)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13477
Secondary Accession Numbers None
Name Procathepsin L
Synonyms
  1. Cathepsin L1
  2. Major excreted protein
  3. p39 cysteine proteinase
  4. MEP
Gene Name CTSL
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (PubMed:12869695). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells (PubMed:12021314). Also mediates invariant chain processing in cortical thymic epithelial cells (PubMed:9545226). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (PubMed:12417635). Secreted form generates endostatin from COL18A1 (PubMed:10716919). Critical for cardiac morphology and function (PubMed:11972068). Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (PubMed:12163394). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
Pathways
  • Antigen processing and presentation
  • Apoptosis
  • Autophagy - animal
  • Fluid shear stress and atherosclerosis
  • Lysosome
  • Phagosome
  • Proteoglycans in cancer
  • Rheumatoid arthritis
Reactions Not Available
GO Classification
Biological Process
spermatogenesis
protein autoprocessing
multicellular organismal aging
elastin catabolic process
cell communication
collagen catabolic process
response to glucocorticoid stimulus
decidualization
immune response
negative regulation of keratinocyte proliferation
cellular response to starvation
male gonad development
proteolysis
response to glucose stimulus
nerve development
thyroid hormone generation
hair follicle morphogenesis
response to organic cyclic compound
autophagic cell death
antigen processing and presentation of peptide antigen
CD4-positive, alpha-beta T cell lineage commitment
enkephalin processing
proteolysis involved in cellular protein catabolic process
response to gonadotropin
Sertoli cell differentiation
zymogen activation
Cellular Component
cytoplasm
nucleolus
nucleus
chromaffin granule
perikaryon
lysosome
collagen-containing extracellular matrix
extracellular space
microvillus
apical plasma membrane
external side of plasma membrane
neuron projection
cytoplasmic vesicle
vacuole
Molecular Function
endopeptidase activity
protein-containing complex binding
cysteine-type endopeptidase activity
aminopeptidase activity
peptide binding
histone binding
cysteine-type carboxypeptidase activity
kininogen binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 334
Molecular Weight 37547.185
Theoretical pI 6.834
Pfam Domain Function
Signals
  • 1-17;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P06797
UniProtKB/Swiss-Prot Entry Name CATL1_MOUSE
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP: Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. J Clin Invest. 1988 May;81(5):1621-9. [PubMed:2835398 ]
  3. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  4. Troen BR, Gal S, Gottesman MM: Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. Biochem J. 1987 Sep 15;246(3):731-5. doi: 10.1042/bj2460731. [PubMed:3689328 ]
  5. Portnoy DA, Erickson AH, Kochan J, Ravetch JV, Unkeless JC: Cloning and characterization of a mouse cysteine proteinase. J Biol Chem. 1986 Nov 5;261(31):14697-703. [PubMed:3533924 ]
  6. Stearns NA, Dong JM, Pan JX, Brenner DA, Sahagian GG: Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels. Arch Biochem Biophys. 1990 Dec;283(2):447-57. doi: 10.1016/0003-9861(90)90666-m. [PubMed:2275556 ]
  7. Baer GS, Ebert DH, Chung CJ, Erickson AH, Dermody TS: Mutant cells selected during persistent reovirus infection do not express mature cathepsin L and do not support reovirus disassembly. J Virol. 1999 Nov;73(11):9532-43. doi: 10.1128/JVI.73.11.9532-9543.1999. [PubMed:10516062 ]
  8. Jean D, Hermann J, Rodrigues-Lima F, Barel M, Balbo M, Frade R: Identification on melanoma cells of p39, a cysteine proteinase that cleaves C3, the third component of complement: amino-acid-sequence identities with procathepsin L. Biochem J. 1995 Dec 15;312 ( Pt 3):961-9. doi: 10.1042/bj3120961. [PubMed:8554545 ]
  9. Nakagawa T, Roth W, Wong P, Nelson A, Farr A, Deussing J, Villadangos JA, Ploegh H, Peters C, Rudensky AY: Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science. 1998 Apr 17;280(5362):450-3. doi: 10.1126/science.280.5362.450. [PubMed:9545226 ]
  10. Felbor U, Dreier L, Bryant RA, Ploegh HL, Olsen BR, Mothes W: Secreted cathepsin L generates endostatin from collagen XVIII. EMBO J. 2000 Mar 15;19(6):1187-94. doi: 10.1093/emboj/19.6.1187. [PubMed:10716919 ]
  11. Lennon-Dumenil AM, Roberts RA, Valentijn K, Driessen C, Overkleeft HS, Erickson A, Peters PJ, Bikoff E, Ploegh HL, Wolf Bryant P: The p41 isoform of invariant chain is a chaperone for cathepsin L. EMBO J. 2001 Aug 1;20(15):4055-64. doi: 10.1093/emboj/20.15.4055. [PubMed:11483509 ]
  12. Benavides F, Starost MF, Flores M, Gimenez-Conti IB, Guenet JL, Conti CJ: Impaired hair follicle morphogenesis and cycling with abnormal epidermal differentiation in nackt mice, a cathepsin L-deficient mutation. Am J Pathol. 2002 Aug;161(2):693-703. doi: 10.1016/S0002-9440(10)64225-3. [PubMed:12163394 ]
  13. Honey K, Nakagawa T, Peters C, Rudensky A: Cathepsin L regulates CD4+ T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands. J Exp Med. 2002 May 20;195(10):1349-58. doi: 10.1084/jem.20011904. [PubMed:12021314 ]
  14. Fiebiger E, Maehr R, Villadangos J, Weber E, Erickson A, Bikoff E, Ploegh HL, Lennon-Dumenil AM: Invariant chain controls the activity of extracellular cathepsin L. J Exp Med. 2002 Nov 4;196(9):1263-9. doi: 10.1084/jem.20020762. [PubMed:12417635 ]
  15. Friedrichs B, Tepel C, Reinheckel T, Deussing J, von Figura K, Herzog V, Peters C, Saftig P, Brix K: Thyroid functions of mouse cathepsins B, K, and L. J Clin Invest. 2003 Jun;111(11):1733-45. doi: 10.1172/JCI15990. [PubMed:12782676 ]
  16. Yasothornsrikul S, Greenbaum D, Medzihradszky KF, Toneff T, Bundey R, Miller R, Schilling B, Petermann I, Dehnert J, Logvinova A, Goldsmith P, Neveu JM, Lane WS, Gibson B, Reinheckel T, Peters C, Bogyo M, Hook V: Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9590-5. doi: 10.1073/pnas.1531542100. Epub 2003 Jul 17. [PubMed:12869695 ]
  17. Goulet B, Baruch A, Moon NS, Poirier M, Sansregret LL, Erickson A, Bogyo M, Nepveu A: A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol Cell. 2004 Apr 23;14(2):207-19. doi: 10.1016/s1097-2765(04)00209-6. [PubMed:15099520 ]
  18. Uematsu R, Furukawa J, Nakagawa H, Shinohara Y, Deguchi K, Monde K, Nishimura S: High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis. Mol Cell Proteomics. 2005 Dec;4(12):1977-89. doi: 10.1074/mcp.M500203-MCP200. Epub 2005 Sep 16. [PubMed:16170054 ]