CST7 (gene)

CST7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CH9
Identifiers
Aliases	CST7, CMAP, cystatin F
External IDs	MGI: 1298217 HomoloGene: 37832 GeneCards: CST7
Gene ontology Molecular function • peptidase inhibitor activity • endopeptidase inhibitor activity • protein binding • cysteine-type endopeptidase inhibitor activity Cellular component • cytoplasm • extracellular region Biological process • negative regulation of peptidase activity • immune response • negative regulation of endopeptidase activity Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	8530	13011
Ensembl	ENSG00000077984	ENSMUSG00000068129
UniProt	O76096	O89098
RefSeq (mRNA)	NM_003650	NM_009977
RefSeq (protein)	NP_003641.3	NP_034107.2
Location (UCSC)	Chr 20: 24.95 – 24.96 Mb	Chr 2: 150.57 – 150.58 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Cystatin-F is a protein that in humans is encoded by the CST7 gene.^[3][4][5]

The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. This gene encodes a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Expression of the protein has been observed in various human cancer cell lines established from malignant tumors.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Ni J, Fernandez MA, Danielsson L, Chillakuru RA, Zhang J, Grubb A, Su J, Gentz R, Abrahamson M (Oct 1998). "Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor". J Biol Chem. 273 (38): 24797–804. doi:10.1074/jbc.273.38.24797. PMID 9733783.
4. Halfon S, Ford J, Foster J, Dowling L, Lucian L, Sterling M, Xu Y, Weiss M, Ikeda M, Liggett D, Helms A, Caux C, Lebecque S, Hannum C, Menon S, McClanahan T, Gorman D, Zurawski G (Aug 1998). "Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells". J Biol Chem. 273 (26): 16400–8. doi:10.1074/jbc.273.26.16400. PMID 9632704.
5. "Entrez Gene: CST7 cystatin F (leukocystatin)".

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External links

• The MEROPS online database for peptidases and their inhibitors: I25.007

Further reading

• Brown WM, Dziegielewska KM (1997). "Friends and relations of the cystatin superfamily--new members and their evolution.". Protein Sci. 6 (1): 5–12. doi:10.1002/pro.5560060102. PMC 2143511. PMID 9007972.
• Saitoh E, Isemura S, Sanada K, et al. (1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes.". Biol. Chem. Hoppe-Seyler. 369 Suppl: 191–7. PMID 3202964.
• Thiesse M, Millar SJ, Dickinson DP (1994). "The human type 2 cystatin gene family consists of eight to nine members, with at least seven genes clustered at a single locus on human chromosome 20.". DNA Cell Biol. 13 (2): 97–116. doi:10.1089/dna.1994.13.97. PMID 8179826.
• Morita M, Yoshiuchi N, Arakawa H, Nishimura S (1999). "CMAP: a novel cystatin-like gene involved in liver metastasis.". Cancer Res. 59 (1): 151–8. PMID 9892200.
• Morita M, Hara Y, Tamai Y, et al. (2001). "Genomic construct and mapping of the gene for CMAP (leukocystatin/cystatin F, CST7) and identification of a proximal novel gene, BSCv (C20orf3).". Genomics. 67 (1): 87–91. doi:10.1006/geno.2000.6237. PMID 10945474.
• Journet A, Chapel A, Kieffer S, et al. (2001). "Towards a human repertoire of monocytic lysosomal proteins.". Electrophoresis. 21 (16): 3411–9. doi:10.1002/1522-2683(20001001)21:16<3411::AID-ELPS3411>3.0.CO;2-M. PMID 11079561.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Nathanson CM, Wassélius J, Wallin H, Abrahamson M (2003). "Regulated expression and intracellular localization of cystatin F in human U937 cells.". Eur. J. Biochem. 269 (22): 5502–11. doi:10.1046/j.1432-1033.2002.03252.x. PMID 12423348.
• 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.
• Cappello F, Gatti E, Camossetto V, et al. (2004). "Cystatin F is secreted, but artificial modification of its C-terminus can induce its endocytic targeting.". Exp. Cell Res. 297 (2): 607–18. doi:10.1016/j.yexcr.2004.03.048. PMID 15212960.
• 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.
• Langerholc T, Zavasnik-Bergant V, Turk B, et al. (2005). "Inhibitory properties of cystatin F and its localization in U937 promonocyte cells.". FEBS J. 272 (6): 1535–45. doi:10.1111/j.1742-4658.2005.04594.x. PMID 15752368.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Schüttelkopf AW, Hamilton G, Watts C, van Aalten DM (2006). "Structural basis of reduction-dependent activation of human cystatin F.". J. Biol. Chem. 281 (24): 16570–5. doi:10.1074/jbc.M601033200. PMID 16601115.