CST2

Cystatin SA
Identifiers
Symbols	CST2 ; MGC71924
External IDs	OMIM: 123856 HomoloGene: 55573 GeneCards: CST2 Gene
Gene ontology Molecular function • cysteine-type endopeptidase inhibitor activity • protein binding Cellular component • extracellular space Biological process • detection of chemical stimulus involved in sensory perception of bitter taste • negative regulation of endopeptidase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1470	n/a
Ensembl	ENSG00000170369	n/a
UniProt	P09228	n/a
RefSeq (mRNA)	NM_001322	n/a
RefSeq (protein)	NP_001313	n/a
Location (UCSC)	Chr 20: 23.82 – 23.83 Mb	n/a
PubMed search		n/a

Cystatin-SA is a protein that in humans is encoded by the CST2 gene.^[1]

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, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes a secreted thiol protease inhibitor found at high levels in saliva, tears and seminal plasma.^[1]

References

1. "Entrez Gene: CST2 cystatin SA".

External links

• The MEROPS online database for peptidases and their inhibitors: I25.009

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.
• Abrahamson M, Jonsdottir S, Olafsson I; et al. (1992). "Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis". Hum. Genet. 89 (4): 377–80. doi:10.1007/BF00194306. PMID 1352269.
• Takahashi M, Honda Y, Ogawa K, Barka T (1993). "Immunofluorescence localization of cystatins in human lacrimal gland and in the exorbital lacrimal gland of the rat". Acta ophthalmologica 70 (5): 625–31. doi:10.1111/j.1755-3768.1992.tb02143.x. PMID 1471486.
• Isemura S, Saitoh E, Sanada K, Minakata K (1992). "Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of phosphorylation sites of cystatin S". J. Biochem. 110 (4): 648–54. PMID 1778989.
• Bobek LA, Aguirre A, Levine MJ (1991). "Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry". Biochem. J. 278 (3): 627–35. PMC 1151393. PMID 1898352.
• Abrahamson M, Olafsson I, Palsdottir A; et al. (1990). "Structure and expression of the human cystatin C gene". Biochem. J. 268 (2): 287–94. PMC 1131430. PMID 2363674.
• Levy E, Lopez-Otin C, Ghiso J; et al. (1989). "Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases". J. Exp. Med. 169 (5): 1771–8. doi:10.1084/jem.169.5.1771. PMC 2189307. PMID 2541223.
• Saitoh E, Sabatini LM, Eddy RL; et al. (1989). "The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20". Biochem. Biophys. Res. Commun. 162 (3): 1324–31. doi:10.1016/0006-291X(89)90818-8. PMID 2764935.
• 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.
• Isemura S, Saitoh E, Sanada K (1988). "Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva". J. Biochem. 102 (4): 693–704. PMID 3436950.
• Saitoh E, Kim HS, Smithies O, Maeda N (1988). "Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three members of the cystatin gene family". Gene 61 (3): 329–38. doi:10.1016/0378-1119(87)90196-X. PMID 3446578.
• Abrahamson M, Grubb A, Olafsson I, Lundwall A (1987). "Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C". FEBS Lett. 216 (2): 229–33. doi:10.1016/0014-5793(87)80695-6. PMID 3495457.
• Grubb A, Löfberg H (1982). "Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis". Proc. Natl. Acad. Sci. U.S.A. 79 (9): 3024–7. doi:10.1073/pnas.79.9.3024. PMC 346341. PMID 6283552.
• Brzin J, Popovic T, Turk V; et al. (1984). "Human cystatin, a new protein inhibitor of cysteine proteinases". Biochem. Biophys. Res. Commun. 118 (1): 103–9. doi:10.1016/0006-291X(84)91073-8. PMID 6365094.
• Turk V, Brzin J, Longer M; et al. (1984). "Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white". Hoppe-Seyler's Z. Physiol. Chem. 364 (11): 1487–96. doi:10.1515/bchm2.1983.364.2.1487. PMID 6662498.
• Dickinson DP, Thiesse M, Dempsey LD, Millar SJ (1993). "Genomic cloning, physical mapping, and expression of human type 2 cystatin genes". Crit. Rev. Oral Biol. Med. 4 (3–4): 573–80. PMID 7690606.
• Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ (1995). "Direct mapping of seven genes encoding human type 2 cystatins to a single site located at 20p11.2". Genomics 24 (1): 172–5. doi:10.1006/geno.1994.1595. PMID 7896273.
• 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.
• Janowski R, Kozak M, Jankowska E; et al. (2001). "Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping". Nat. Struct. Biol. 8 (4): 316–20. doi:10.1038/86188. PMID 11276250.