Cathepsin F

Cathepsin F
PDB rendering based on 1m6d.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1D5U​, 1M6D​
Identifiers
Symbols	CTSF ; CATSF; CLN13
External IDs	OMIM: 603539 MGI: 1861434 HomoloGene: 31194 IUPHAR: 2347 ChEMBL: 2517 GeneCards: CTSF Gene
EC number	3.4.22.41
Gene ontology Molecular function • cysteine-type endopeptidase activity Cellular component • extracellular space • lysosome • lysosomal lumen • extracellular exosome • extracellular vesicle Biological process • proteolysis • antigen processing and presentation of exogenous peptide antigen via MHC class II • proteolysis involved in cellular protein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8722	56464
Ensembl	ENSG00000174080	ENSMUSG00000083282
UniProt	Q9UBX1	Q9R013
RefSeq (mRNA)	NM_003793	NM_019861
RefSeq (protein)	NP_003784	NP_063914
Location (UCSC)	Chr 11: 66.56 – 66.57 Mb	Chr 19: 4.86 – 4.86 Mb
PubMed search

Cathepsin F is a protein that in humans is encoded by the CTSF gene.^[1][2][3]

Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids that contains a 19-residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W.^[3]

References

1. Wang B, Shi GP, Yao PM, Li Z, Chapman HA, Bromme D (Dec 1998). "Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization". J Biol Chem 273 (48): 32000–8. doi:10.1074/jbc.273.48.32000. PMID 9822672.
2. Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C (Jun 1999). "Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain". J Biol Chem 274 (20): 13800–9. doi:10.1074/jbc.274.20.13800. PMID 10318784.
3. "Entrez Gene: CTSF cathepsin F".

Further reading

• Nägler DK, Sulea T, Ménard R (1999). "Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen.". Biochem. Biophys. Res. Commun. 257 (2): 313–8. doi:10.1006/bbrc.1999.0461. PMID 10198209.
• Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins.". Biochem. Biophys. Res. Commun. 259 (2): 401–7. doi:10.1006/bbrc.1999.0700. PMID 10362521.
• Wex T, Wex H, Brömme D (2000). "The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene.". Biol. Chem. 380 (12): 1439–42. doi:10.1515/BC.1999.185. PMID 10661872.
• Shi GP, Bryant RA, Riese R; et al. (2000). "Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages.". J. Exp. Med. 191 (7): 1177–86. doi:10.1084/jem.191.7.1177. PMC 2193169. PMID 10748235.
• Deussing J, Tisljar K, Papazoglou A, Peters C (2000). "Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene.". Gene 251 (2): 165–73. doi:10.1016/S0378-1119(00)00196-7. PMID 10876093.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Oörni K, Sneck M, Brömme D; et al. (2004). "Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro.". J. Biol. Chem. 279 (33): 34776–84. doi:10.1074/jbc.M310814200. PMID 15184381.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K; et al. (2006). "Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer.". BMC Cancer 5 (1): 68. doi:10.1186/1471-2407-5-68. PMC 1175083. PMID 15989693.
• Kaakinen R, Lindstedt KA, Sneck M; et al. (2007). "Angiotensin II increases expression and secretion of cathepsin F in cultured human monocyte-derived macrophages: an angiotensin II type 2 receptor-mediated effect.". Atherosclerosis 192 (2): 323–7. doi:10.1016/j.atherosclerosis.2006.08.001. PMID 16963053.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.018