View source for Cathepsin F

{{Infobox_gene}}
'''Cathepsin F''' is a [[protein]] that in humans is encoded by the ''CTSF'' [[gene]].<ref name="pmid9822672">{{cite journal | vauthors = Wang B, Shi GP, Yao PM, Li Z, Chapman HA, Bromme D | title = Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization | journal = J Biol Chem | volume = 273 | issue = 48 | pages = 32000–8 |date=Dec 1998 | pmid = 9822672 | pmc =  | doi =  10.1074/jbc.273.48.32000}}</ref><ref name="pmid10318784">{{cite journal | vauthors = Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C | title = Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain | journal = J Biol Chem | volume = 274 | issue = 20 | pages = 13800–9 |date=Jun 1999 | pmid = 10318784 | pmc =  | doi =  10.1074/jbc.274.20.13800}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CTSF cathepsin F| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8722| accessdate = }}</ref>

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| section_title = 
| summary_text = 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.<ref name="entrez"/>
}}

==References==
{{reflist}}

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

==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C01.018 C01.018]
{{PDB Gallery|geneid=8722}}

{{Cysteine proteases}}
{{Enzymes}}
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[[Category:Peptidase]]
[[Category:EC 3.4.22]]
[[Category:Cathepsins]]


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