CTSF

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Cathepsin F
PDB rendering based on 1m6d.
Available structures: 1m6d
Identifiers
Symbol(s) CTSF; CATSF
External IDs OMIM: 603539 MGI: 1861434 HomoloGene: 31194
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 8722 56464
Ensembl ENSG00000174080 ENSMUSG00000006458
Uniprot Q9UBX1 Q99KQ9
Refseq NM_003793 (mRNA)
NP_003784 (protein)		 NM_019861 (mRNA)
NP_063914 (protein)
Location Chr 11: 66.09 - 66.09 Mb Chr 19: 4.86 - 4.86 Mb
Pubmed search [1] [2]

Cathepsin F, also known as CTSF, is a human gene.[1]

Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally 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 which 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.[1]

[edit] References

  1. ^ a b Entrez Gene: CTSF cathepsin F.

[edit] Further reading

  • Wang B, Shi GP, Yao PM, et al. (1998). "Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization.". J. Biol. Chem. 273 (48): 32000–8. PMID 9822672. 
  • 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. 
  • Santamaría I, Velasco G, Pendás AM, et al. (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. PMID 10318784. 
  • 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. 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. 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. 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. 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. 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. 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. 
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v • d • e
Hydrolase: proteases (EC 3.4)
Exopeptidase 3.4.11-19
Endopeptidase 3.4.21-24
Cathepsin 3.4.18,21,22,23
A - B - C - D - E - F - G - H - K - L1/L2 - S - W - Z