CST7 (gene)

CST7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CH9
Identifiers
Aliases	CST7 , CMAP, cystatin F
External IDs	OMIM: 603253 MGI: 1298217 HomoloGene: 37832 GeneCards: CST7
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20p11.21 Start 24,949,269 bp [1] End 24,959,928 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2|2 G3 Start 150,412,335 bp [2] End 150,420,864 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in blood bone marrow bone marrow cells cancellous bone spleen right lung upper lobe of left lung lymph node gallbladder appendix Top expressed in morula bone marrow blood spleen thymus subcutaneous adipose tissue dermis blastocyst jejunum body of femur More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase inhibitor activity endopeptidase inhibitor activity protein binding protease binding cysteine-type endopeptidase inhibitor activity protein homodimerization activity Cellular component cytoplasm extracellular region extracellular space lysosome endosome late endosome multivesicular body endoplasmic reticulum Golgi apparatus cytoplasmic vesicle Biological process negative regulation of peptidase activity immune response negative regulation of cysteine-type endopeptidase activity negative regulation of endopeptidase activity positive regulation of myelination inhibition of cysteine-type endopeptidase activity negative regulation of microglial cell activation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8530 13011 Ensembl ENSG00000077984 ENSMUSG00000068129 UniProt O76096 O89098 RefSeq (mRNA) NM_003650 NM_009977 RefSeq (protein) NP_003641 NP_034107 Location (UCSC) Chr 20: 24.95 – 24.96 Mb Chr 2: 150.41 – 150.42 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cystatin-F is a protein that in humans is encoded by the CST7 gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000077984 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000068129 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: CST7 cystatin F (leukocystatin)".

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External links

• The MEROPS online database for peptidases and their inhibitors: I25.007
• Human CST7 genome location and CST7 gene details page in the UCSC Genome Browser .

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. S2CID   22312806.
• Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...9916899M. 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. S2CID   46239078.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.