Cathepsin F

{{Short description|Protein-coding gene in the species Homo sapiens (Humans)}} {{cs1 config|name-list-style=vanc|display-authors=6}} {{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 | date = Dec 1998 | title = Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization | journal = The Journal of Biological Chemistry | volume = 273 | issue = 48 | pages = 32000–32008 | doi = 10.1074/jbc.273.48.32000 | pmid = 9822672 | doi-access = free }}</ref><ref name="pmid10318784">{{cite journal | vauthors = Santamaria I, Velasco G, Pendas AM, Paz A, Lopez-Otin C | date = Jun 1999 | 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 = The Journal of Biological Chemistry | volume = 274 | issue = 20 | pages = 13800–13809 | doi = 10.1074/jbc.274.20.13800 | pmid = 10318784 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CTSF cathepsin F| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=8722}}</ref>

Cysteine cathepsins are a family of cysteine proteases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal peptide, 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"/>

== In non-human species == === Immunodiagnosis of ''Opisthorchis viverrini'' === ''Opisthorchis viverrini'', a parasite, is typically detected by stool examination, specifically by counting eggs. However, this non-invasive, "gold standard" method can be unreliable in light infection and labor-intensive. An ELISA assay that detects the presence of the parasite's cathepsin F protein may be used as an alternative way to test for the parasite's presence.<ref>{{cite journal | vauthors = Teimoori S, Arimatsu Y, Laha T, Kaewkes S, Sereerak P, Tangkawattana S, Brindley PJ, Sripa B | date = December 2015 | title = Immunodiagnosis of opisthorchiasis using parasite cathepsin F | journal = Parasitology Research | volume = 114 | issue = 12 | pages = 4571–4578 | doi = 10.1007/s00436-015-4703-9 | pmc = 4917378 | pmid = 26344868 }}</ref>

=== Discovery in Yesso scallop (''Mizuhopecten yessoensis'') === The Yesso scallop (''Mizuhopecten yessoensis''), was found in 2018 to express Cathepsin F in response to bacterial infection. The Yesso scallop has been suffering from high mortality due to bacterial diseases. Understanding the workings of its innate immune system, in various embryonic developmental stages, may help the associated aquaculture industry.<ref>{{cite journal | vauthors = Guo H, Li Y, Zhang M, Li R, Li W, Lou J, Bao Z, Wang Y | date = September 2018 | title = Expression of Cathepsin F in response to bacterial challenges in Yesso scallop Patinopecten yessoensis | journal = Fish & Shellfish Immunology | volume = 80 | pages = 141–147 | doi = 10.1016/j.fsi.2018.06.005 | pmid = 29879509 | bibcode = 2018FSI....80..141G | s2cid = 47014597 }}</ref>

== References == {{reflist}}

== Further reading == {{refbegin | 2}} * {{cite journal | vauthors = Nägler DK, Sulea T, Ménard R | year = 1999 | 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 = Biochemical and Biophysical Research Communications | volume = 257 | issue = 2 | pages = 313–318 | doi = 10.1006/bbrc.1999.0461 | pmid = 10198209 | bibcode = 1999BBRC..257..313N }} * {{cite journal | vauthors = Wex T, Levy B, Wex H, Brömme D | year = 1999 | title = Human cathepsins F and W: A new subgroup of cathepsins. | journal = Biochemical and Biophysical Research Communications | volume = 259 | issue = 2 | pages = 401–407 | doi = 10.1006/bbrc.1999.0700 | pmid = 10362521 | bibcode = 1999BBRC..259..401W }} * {{cite journal | vauthors = Wex T, Wex H, Brömme D | year = 2000 | title = The human cathepsin F gene--a fusion product between an ancestral cathepsin and cystatin gene. | journal = Biological Chemistry | volume = 380 | issue = 12 | pages = 1439–1442 | doi = 10.1515/BC.1999.185 | pmid = 10661872 | s2cid = 28469574 }} * {{cite journal | vauthors = Shi GP, Bryant RA, Riese R, Verhelst S, Driessen C, Li Z, Bromme D, Ploegh HL, Chapman HA | date = April 2000 | title = Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages | journal = The Journal of Experimental Medicine | volume = 191 | issue = 7 | pages = 1177–1186 | doi = 10.1084/jem.191.7.1177 | pmc = 2193169 | pmid = 10748235 }} * {{cite journal | vauthors = Deussing J, Tisljar K, Papazoglou A, Peters C | year = 2000 | title = Mouse cathepsin F: cDNA cloning, genomic organization and chromosomal assignment of the gene. | journal = Gene | volume = 251 | issue = 2 | pages = 165–173 | doi = 10.1016/S0378-1119(00)00196-7 | pmid = 10876093 }} * {{cite journal | vauthors = Oörni K, Sneck M, Brömme D, Pentikäinen MO, Lindstedt KA, Mäyränpää M, Aitio H, Kovanen PT | date = August 2004 | 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 = The Journal of Biological Chemistry | volume = 279 | issue = 33 | pages = 34776–34784 | doi = 10.1074/jbc.M310814200 | pmid = 15184381 | doi-access = free }} * {{cite journal | vauthors = Vazquez-Ortiz G, Pina-Sanchez P, Vazquez K, Duenas A, Taja L, Mendoza P, Garcia JA, Salcedo M | date = June 2005 | title = Overexpression of cathepsin F, matrix metalloproteinases 11 and 12 in cervical cancer | journal = BMC Cancer | volume = 5 | issue = 1 | article-number = 68 | doi = 10.1186/1471-2407-5-68 | pmc = 1175083 | pmid = 15989693 | doi-access = free }} * {{cite journal | vauthors = Kaakinen R, Lindstedt KA, Sneck M, Kovanen PT, Oörni K | date = June 2007 | 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 = 323–327 | doi = 10.1016/j.atherosclerosis.2006.08.001 | pmid = 16963053 }} {{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]{{Dead link|date=January 2026 |bot=InternetArchiveBot }} {{PDB Gallery|geneid=8722}}

Category:Proteases Category:EC 3.4.22 Category:Cathepsins