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{{AE}} Henry A. Hoff
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'''Cystatin-SA''' is a [[protein]] that in humans is encoded by the ''CST2'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CST2 cystatin SA| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1470| accessdate = }}</ref>
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"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."<ref name=RefSeq2008>{{ cite book
| update_citations = yes
|author=RefSeq
}}
|title=CST2 cystatin SA [ Homo sapiens (human) ]
|publisher=National Center for Biotechnology Information, U.S. National Library of Medicine
|location=8600 Rockville Pike, Bethesda MD, 20894 USA
|date=July 2008
|url=https://www.ncbi.nlm.nih.gov/gene/1470
|accessdate=2017-02-04 }}</ref>
 
==Gene==


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
===Transcriptions===
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Cystatin SA
| HGNCid = 2474
| Symbol = CST2
| AltSymbols =; MGC71924
| OMIM = 123856
| ECnumber = 
| Homologene = 55573
| MGIid = 
| GeneAtlas_image1 = PBB_GE_CST2_208555_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1470
    | Hs_Ensembl = ENSG00000170369
    | Hs_RefseqProtein = NP_001313
    | Hs_RefseqmRNA = NM_001322
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 23752406
    | Hs_GenLoc_end = 23755368
    | Hs_Uniprot = P09228
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Cystatin SA''', also known as '''CST2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CST2 cystatin SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1470| accessdate = }}</ref>


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The "four cystatin genes [GeneID: 1469 CST1, GeneID: 1470 [[CST2]], GeneID: 1471 [[Cystatin C|CST3]], and GeneID: 1472 [[CST4]]] contain the ATA-box sequence (ATAAA) in their 5'-flanking regions; however, the CAT-box sequence (CAT), a binding site of the transcription factor, CTF, is found only in the 5'-flanking region of the S-type cystatin genes."<ref name=Saitoh>{{ cite journal
{{PBB_Summary
|author=Eiichi Saitoh and Satoko Isemura
| section_title =
|title=Molecular Biology of Human Salivary Cysteine Proteinase Inhibitors
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CST2 cystatin SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1470| accessdate = }}</ref>
|journal=Critical Reviews in Oral Biology and Medicine
}}
|date=January 1, 1993
|volume=4
|issue=3/4
|pages=487-93
|url=http://cro.sagepub.com/content/4/3/487.full.pdf
|arxiv=
|bibcode=
|doi=10.1177/10454411930040033301
|pmid=
|accessdate=2013-06-28 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=I25.009 I25.009]
* {{UCSC gene info|CST2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Brown WM, Dziegielewska KM |title=Friends and relations of the cystatin superfamily--new members and their evolution. |journal=Protein Sci. |volume=6 |issue= 1 |pages= 5-12 |year= 1997 |pmid= 9007972 |doi=  }}
*{{cite journal  | vauthors=Brown WM, Dziegielewska KM |title=Friends and relations of the cystatin superfamily--new members and their evolution |journal=Protein Sci. |volume=6 |issue= 1 |pages= 5–12 |year= 1997 |pmid= 9007972 |doi=10.1002/pro.5560060102  | pmc=2143511 }}
*{{cite journal  | author=Abrahamson M, Jonsdottir S, Olafsson I, ''et al.'' |title=Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis. |journal=Hum. Genet. |volume=89 |issue= 4 |pages= 377-80 |year= 1992 |pmid= 1352269 |doi=  }}
*{{cite journal  | vauthors=Abrahamson M, Jonsdottir S, Olafsson I |title=Hereditary cystatin C amyloid angiopathy: identification of the disease-causing mutation and specific diagnosis by polymerase chain reaction based analysis |journal=Hum. Genet. |volume=89 |issue= 4 |pages= 377–80 |year= 1992 |pmid= 1352269 |doi=10.1007/BF00194306 |display-authors=etal}}
*{{cite journal  | author=Takahashi M, Honda Y, Ogawa K, Barka T |title=Immunofluorescence localization of cystatins in human lacrimal gland and in the exorbital lacrimal gland of the rat. |journal=Acta ophthalmologica |volume=70 |issue= 5 |pages= 625-31 |year= 1993 |pmid= 1471486 |doi=  }}
*{{cite journal  | vauthors=Takahashi M, Honda Y, Ogawa K, Barka T |title=Immunofluorescence localization of cystatins in human lacrimal gland and in the exorbital lacrimal gland of the rat |journal=Acta Ophthalmologica |volume=70 |issue= 5 |pages= 625–31 |year= 1993 |pmid= 1471486 |doi=10.1111/j.1755-3768.1992.tb02143.x }}
*{{cite journal  | author=Isemura S, Saitoh E, Sanada K, Minakata K |title=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. |journal=J. Biochem. |volume=110 |issue= 4 |pages= 648-54 |year= 1992 |pmid= 1778989 |doi=  }}
*{{cite journal  | vauthors=Isemura S, Saitoh E, Sanada K, Minakata K |title=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 |journal=J. Biochem. |volume=110 |issue= 4 |pages= 648–54 |year= 1992 |pmid= 1778989 |doi=  }}
*{{cite journal  | author=Bobek LA, Aguirre A, Levine MJ |title=Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry. |journal=Biochem. J. |volume=278 ( Pt 3) |issue=  |pages= 627-35 |year= 1991 |pmid= 1898352 |doi=  }}
*{{cite journal  | vauthors=Bobek LA, Aguirre A, Levine MJ |title=Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry |journal=Biochem. J. |volume=278 |issue=  3|pages= 627–35 |year= 1991 |pmid= 1898352 |doi= | pmc=1151393 }}
*{{cite journal  | author=Abrahamson M, Olafsson I, Palsdottir A, ''et al.'' |title=Structure and expression of the human cystatin C gene. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 287-94 |year= 1990 |pmid= 2363674 |doi=  }}
*{{cite journal  | vauthors=Abrahamson M, Olafsson I, Palsdottir A |title=Structure and expression of the human cystatin C gene |journal=Biochem. J. |volume=268 |issue= 2 |pages= 287–94 |year= 1990 |pmid= 2363674 |doi=  | pmc=1131430  |display-authors=etal}}
*{{cite journal  | author=Levy E, Lopez-Otin C, Ghiso J, ''et al.'' |title=Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases. |journal=J. Exp. Med. |volume=169 |issue= 5 |pages= 1771-8 |year= 1989 |pmid= 2541223 |doi= }}
*{{cite journal  | vauthors=Levy E, Lopez-Otin C, Ghiso J |title=Stroke in Icelandic patients with hereditary amyloid angiopathy is related to a mutation in the cystatin C gene, an inhibitor of cysteine proteases |journal=J. Exp. Med. |volume=169 |issue= 5 |pages= 1771–8 |year= 1989 |pmid= 2541223 |doi=10.1084/jem.169.5.1771  | pmc=2189307  |display-authors=etal}}
*{{cite journal  | author=Saitoh E, Sabatini LM, Eddy RL, ''et al.'' |title=The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20. |journal=Biochem. Biophys. Res. Commun. |volume=162 |issue= 3 |pages= 1324-31 |year= 1989 |pmid= 2764935 |doi= }}
*{{cite journal  | vauthors=Saitoh E, Sabatini LM, Eddy RL |title=The human cystatin C gene (CST3) is a member of the cystatin gene family which is localized on chromosome 20 |journal=Biochem. Biophys. Res. Commun. |volume=162 |issue= 3 |pages= 1324–31 |year= 1989 |pmid= 2764935 |doi=10.1016/0006-291X(89)90818-8  |display-authors=etal}}
*{{cite journal  | author=Saitoh E, Isemura S, Sanada K, ''et al.'' |title=Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes. |journal=Biol. Chem. Hoppe-Seyler |volume=369 Suppl |issue=  |pages= 191-7 |year= 1989 |pmid= 3202964 |doi=  }}
*{{cite journal  | vauthors=Saitoh E, Isemura S, Sanada K |title=Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes |journal=Biol. Chem. Hoppe-Seyler |volume=369 Suppl |issue=  |pages= 191–7 |year= 1989 |pmid= 3202964 |doi=  |display-authors=etal}}
*{{cite journal  | author=Isemura S, Saitoh E, Sanada K |title=Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva. |journal=J. Biochem. |volume=102 |issue= 4 |pages= 693-704 |year= 1988 |pmid= 3436950 |doi=  }}
*{{cite journal  | vauthors=Isemura S, Saitoh E, Sanada K |title=Characterization and amino acid sequence of a new acidic cysteine proteinase inhibitor (cystatin SA) structurally closely related to cystatin S, from human whole saliva |journal=J. Biochem. |volume=102 |issue= 4 |pages= 693–704 |year= 1988 |pmid= 3436950 |doi=  }}
*{{cite journal  | author=Saitoh E, Kim HS, Smithies O, Maeda N |title=Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three members of the cystatin gene family. |journal=Gene |volume=61 |issue= 3 |pages= 329-38 |year= 1988 |pmid= 3446578 |doi=  }}
*{{cite journal  | vauthors=Saitoh E, Kim HS, Smithies O, Maeda N |title=Human cysteine-proteinase inhibitors: nucleotide sequence analysis of three members of the cystatin gene family |journal=Gene |volume=61 |issue= 3 |pages= 329–38 |year= 1988 |pmid= 3446578 |doi=10.1016/0378-1119(87)90196-X }}
*{{cite journal  | author=Abrahamson M, Grubb A, Olafsson I, Lundwall A |title=Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. |journal=FEBS Lett. |volume=216 |issue= 2 |pages= 229-33 |year= 1987 |pmid= 3495457 |doi=  }}
*{{cite journal  | vauthors=Abrahamson M, Grubb A, Olafsson I, Lundwall A |title=Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C |journal=FEBS Lett. |volume=216 |issue= 2 |pages= 229–33 |year= 1987 |pmid= 3495457 |doi=10.1016/0014-5793(87)80695-6 }}
*{{cite journal  | author=Grubb A, Löfberg H |title=Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 9 |pages= 3024-7 |year= 1982 |pmid= 6283552 |doi= }}
*{{cite journal  | vauthors=Grubb A, Löfberg H |title=Human gamma-trace, a basic microprotein: amino acid sequence and presence in the adenohypophysis |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 9 |pages= 3024–7 |year= 1982 |pmid= 6283552 |doi=10.1073/pnas.79.9.3024  | pmc=346341  }}
*{{cite journal  | author=Brzin J, Popovic T, Turk V, ''et al.'' |title=Human cystatin, a new protein inhibitor of cysteine proteinases. |journal=Biochem. Biophys. Res. Commun. |volume=118 |issue= 1 |pages= 103-9 |year= 1984 |pmid= 6365094 |doi= }}
*{{cite journal  | vauthors=Brzin J, Popovic T, Turk V |title=Human cystatin, a new protein inhibitor of cysteine proteinases |journal=Biochem. Biophys. Res. Commun. |volume=118 |issue= 1 |pages= 103–9 |year= 1984 |pmid= 6365094 |doi=10.1016/0006-291X(84)91073-8  |display-authors=etal}}
*{{cite journal  | author=Turk V, Brzin J, Longer M, ''et al.'' |title=Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white. |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=364 |issue= 11 |pages= 1487-96 |year= 1984 |pmid= 6662498 |doi=  }}
*{{cite journal  | vauthors=Turk V, Brzin J, Longer M |title=Protein inhibitors of cysteine proteinases. III. Amino-acid sequence of cystatin from chicken egg white |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=364 |issue= 11 |pages= 1487–96 |year= 1984 |pmid= 6662498 |doi=  10.1515/bchm2.1983.364.2.1487|display-authors=etal}}
*{{cite journal  | author=Dickinson DP, Thiesse M, Dempsey LD, Millar SJ |title=Genomic cloning, physical mapping, and expression of human type 2 cystatin genes. |journal=Crit. Rev. Oral Biol. Med. |volume=4 |issue= 3-4 |pages= 573-80 |year= 1993 |pmid= 7690606 |doi=  }}
*{{cite journal  | vauthors=Dickinson DP, Thiesse M, Dempsey LD, Millar SJ |title=Genomic cloning, physical mapping, and expression of human type 2 cystatin genes |journal=Crit. Rev. Oral Biol. Med. |volume=4 |issue= 3–4 |pages= 573–80 |year= 1993 |pmid= 7690606 |doi=  }}
*{{cite journal  | author=Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ |title=Direct mapping of seven genes encoding human type 2 cystatins to a single site located at 20p11.2. |journal=Genomics |volume=24 |issue= 1 |pages= 172-5 |year= 1995 |pmid= 7896273 |doi= 10.1006/geno.1994.1595 }}
*{{cite journal  | vauthors=Dickinson DP, Zhao Y, Thiesse M, Siciliano MJ |title=Direct mapping of seven genes encoding human type 2 cystatins to a single site located at 20p11.2 |journal=Genomics |volume=24 |issue= 1 |pages= 172–5 |year= 1995 |pmid= 7896273 |doi= 10.1006/geno.1994.1595 }}
*{{cite journal  | author=Thiesse M, Millar SJ, Dickinson DP |title=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. |journal=DNA Cell Biol. |volume=13 |issue= 2 |pages= 97-116 |year= 1994 |pmid= 8179826 |doi=  }}
*{{cite journal  | vauthors=Thiesse M, Millar SJ, Dickinson DP |title=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 |journal=DNA Cell Biol. |volume=13 |issue= 2 |pages= 97–116 |year= 1994 |pmid= 8179826 |doi=10.1089/dna.1994.13.97 }}
*{{cite journal  | author=Janowski R, Kozak M, Jankowska E, ''et al.'' |title=Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. |journal=Nat. Struct. Biol. |volume=8 |issue= 4 |pages= 316-20 |year= 2001 |pmid= 11276250 |doi= 10.1038/86188 }}
*{{cite journal  | vauthors=Janowski R, Kozak M, Jankowska E |title=Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping |journal=Nat. Struct. Biol. |volume=8 |issue= 4 |pages= 316–20 |year= 2001 |pmid= 11276250 |doi= 10.1038/86188 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 16:01, 20 November 2019

Associate Editor(s)-in-Chief: Henry A. Hoff

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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."[2]

Gene

Transcriptions

The "four cystatin genes [GeneID: 1469 CST1, GeneID: 1470 CST2, GeneID: 1471 CST3, and GeneID: 1472 CST4] contain the ATA-box sequence (ATAAA) in their 5'-flanking regions; however, the CAT-box sequence (CAT), a binding site of the transcription factor, CTF, is found only in the 5'-flanking region of the S-type cystatin genes."[3]

References

  1. ↑ "Entrez Gene: CST2 cystatin SA".
  2. ↑ RefSeq (July 2008). CST2 cystatin SA [ Homo sapiens (human) ]. 8600 Rockville Pike, Bethesda MD, 20894 USA: National Center for Biotechnology Information, U.S. National Library of Medicine. Retrieved 2017-02-04.
  3. ↑ Eiichi Saitoh and Satoko Isemura (January 1, 1993). "Molecular Biology of Human Salivary Cysteine Proteinase Inhibitors" (PDF). Critical Reviews in Oral Biology and Medicine. 4 (3/4): 487–93. doi:10.1177/10454411930040033301. Retrieved 2013-06-28.

External links

Further reading



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