PRDX6: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Peroxiredoxin-6''' is a [[protein]] that in humans is encoded by the ''PRDX6'' [[gene]].<ref name="pmid11233154">{{cite journal | author = Phelan SA | title = AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant | journal = Antioxid Redox Signal | volume = 1 | issue = 4 | pages = 571–84 |date=Mar 2001 | pmid = 11233154 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRDX6 peroxiredoxin 6| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588| accessdate = }}</ref> It is a member of the [[peroxiredoxin]] family of antioxidant enzymes.
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.<ref name="entrez" />
| image = PBB_Protein_PRDX6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1prx.
| PDB = {{PDB2|1prx}}
| Name = Peroxiredoxin 6
| HGNCid = 16753
| Symbol = PRDX6
| AltSymbols =; 1-Cys; AOP2; KIAA0106; MGC46173; NSGPx; PRX; aiPLA2; p29
| OMIM = 602316
| ECnumber = 
| Homologene = 3606
| MGIid = 894320
| GeneAtlas_image1 = PBB_GE_PRDX6_200845_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRDX6_200844_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004623 |text = phospholipase A2 activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0009395 |text = phospholipid catabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9588
    | Hs_Ensembl = ENSG00000117592
    | Hs_RefseqProtein = NP_004896
    | Hs_RefseqmRNA = NM_004905
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 171713028
    | Hs_GenLoc_end = 171724569
    | Hs_Uniprot = P30041
    | Mm_EntrezGene = 11758
    | Mm_Ensembl = ENSMUSG00000026701
    | Mm_RefseqmRNA = XM_001000157
    | Mm_RefseqProtein = XP_001000157
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 163076789
    | Mm_GenLoc_end = 163087843
    | Mm_Uniprot = Q53ZU7
  }}
}}
'''Peroxiredoxin 6''', also known as '''PRDX6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX6 peroxiredoxin 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
===Model organisms===
{{PBB_Summary
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
| section_title =  
|+ ''Prdx6'' knockout mouse phenotype
| summary_text = The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX6 peroxiredoxin 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588| accessdate = }}</ref>
|-
}}
! Characteristic!! Phenotype
 
|-
| [[Homozygote]] viability || bgcolor="#488ED3"|Normal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#488ED3"|Normal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Tail epidermis wholemount || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBMD/salmonella-challenge/ |title=''Salmonella'' infection data for Prdx6 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBMD/citrobacter-challenge/ |title=''Citrobacter'' infection data for Prdx6 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of PRDX6 function. A conditional [[knockout mouse]] line, called ''Prdx6<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Prdx6 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4431891 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the [[Wellcome Trust Sanger Institute]].<ref name="pmid21677750">{{Cite journal
| last1 = Skarnes |first1 =W. C.
| doi = 10.1038/nature10163
| last2 = Rosen | first2 = B.
| last3 = West | first3 = A. P.
| last4 = Koutsourakis | first4 = M.
| last5 = Bushell | first5 = W.
| last6 = Iyer | first6 = V.
| last7 = Mujica | first7 = A. O.
| last8 = Thomas | first8 = M.
| last9 = Harrow | first9 = J.
| last10 = Cox | first10 = T.
| last11 = Jackson | first11 = D.
| last12 = Severin | first12 = J.
| last13 = Biggs | first13 = P.
| last14 = Fu | first14 = J.
| last15 = Nefedov | first15 = M.
| last16 = De Jong | first16 = P. J.
| last17 = Stewart | first17 = A. F.
| last18 = Bradley | first18 = A.
| title = A conditional knockout resource for the genome-wide study of mouse gene function
| journal = Nature
| volume = 474
| issue = 7351
| pages = 337–342
| year = 2011
| pmid = 21677750
| pmc =3572410
}}</ref><ref name="mouse_library">{{cite journal |author=Dolgin E |title=Mouse library set to be knockout |journal=Nature |volume=474 |issue=7351 |pages=262–3 |date=June 2011 |pmid=21677718 |doi=10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal |vauthors=Collins FS, Rossant J, Wurst W |title=A mouse for all reasons |journal=Cell |volume=128 |issue=1 |pages=9–13 |date=January 2007 |pmid=17218247 |doi=10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal|vauthors=van der Weyden L, White JK, Adams DJ, Logan DW | title=The mouse genetics toolkit: revealing function and mechanism. | journal=Genome Biol | year= 2011 | volume= 12 | issue= 6 | pages= 224 | pmid=21722353 | doi=10.1186/gb-2011-12-6-224  | pmc=3218837}}</ref> Twenty five tests were carried out on [[mutant]] mice but no significant abnormalities were observed.<ref name="mgp_reference" />


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  |vauthors=Manevich Y, Fisher AB |title=Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism |journal=Free Radic. Biol. Med. |volume=38 |issue= 11 |pages= 1422–32 |year= 2005 |pmid= 15890616 |doi= 10.1016/j.freeradbiomed.2005.02.011 }}
| citations =
*{{cite journal  | author=Akesson B |title=Work in progress. Occurrence of phospholipase A1 and A2 in human decidua |journal=Prostaglandins |volume=9 |issue= 5 |pages= 667–73 |year= 1975 |pmid= 240188 |doi=10.1016/0090-6980(75)90106-9  | last2=Gustavii  | first2=B  }}
*{{cite journal  | author=Phelan SA |title=AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant. |journal=Antioxid. Redox Signal. |volume=1 |issue= 4 |pages= 571-84 |year= 2001 |pmid= 11233154 |doi= }}
*{{cite journal  | author=Hochstrasser DF |title=Human liver protein map: a reference database established by microsequencing and gel comparison |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992–1001 |year= 1993 |pmid= 1286669 |doi=10.1002/elps.11501301201 | author2=Frutiger S | author3=Paquet N | display-authors=3  | last4=Bairoch  | first4=Amos  | last5=Ravier  | first5=Florence  | last6=Pasquali  | first6=Christian  | last7=Sanchez  | first7=Jean-Charles  | last8=Tissot  | first8=Jean-Daniel  | last9=Bjellqvist  | first9=Bengt }}
*{{cite journal  | author=Manevich Y, Fisher AB |title=Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. |journal=Free Radic. Biol. Med. |volume=38 |issue= 11 |pages= 1422-32 |year= 2005 |pmid= 15890616 |doi= 10.1016/j.freeradbiomed.2005.02.011 }}
*{{cite journal  |vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4 }}
*{{cite journal  | author=Akesson B |title=Work in progress. Occurrence of phospholipase A1 and A2 in human decidua. |journal=Prostaglandins |volume=9 |issue= 5 |pages= 667-73 |year= 1975 |pmid= 240188 |doi=  }}
*{{cite journal  |vauthors=Yeats DA, Bakhle YS |title=Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity |journal=Biochim. Biophys. Acta |volume=1003 |issue= 2 |pages= 189–95 |year= 1989 |pmid= 2730891 |doi=  10.1016/0005-2760(89)90254-3}}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi=  }}
*{{cite journal  | author=Nagase T |title=Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1 |journal=DNA Res. |volume=2 |issue= 1 |pages= 37–43 |year= 1995 |pmid= 7788527 |doi=10.1093/dnares/2.1.37 | author2=Miyajima N  | author3=Tanaka A  | display-authors=3  | last4=Sazuka  | first4=T  | last5=Seki  | first5=N  | last6=Sato  | first6=S  | last7=Tabata  | first7=S  | last8=Ishikawa  | first8=K  | last9=Kawarabayasi  | first9=Y }}
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi=  }}
*{{cite journal  | author=Golaz O |title=Plasma and red blood cell protein maps: update 1993 |journal=Electrophoresis |volume=14 |issue= 11 |pages= 1223–31 |year= 1994 |pmid= 8313871 |doi=10.1002/elps.11501401183 | author2=Hughes GJ | author3=Frutiger S | display-authors=3  | last4=Paquet  | first4=Nicole  | last5=Bairoch  | first5=Amos  | last6=Pasquali  | first6=Christian  | last7=Sanchez  | first7=Jean-Charles  | last8=Tissot  | first8=Jean-D. | last9=Appel  | first9=Ron D. }}
*{{cite journal  | author=Yeats DA, Bakhle YS |title=Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity. |journal=Biochim. Biophys. Acta |volume=1003 |issue= 2 |pages= 189-95 |year= 1989 |pmid= 2730891 |doi=  }}
*{{cite journal  | author=Kim TS |title=Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2542–50 |year= 1997 |pmid= 8999971 |doi=10.1074/jbc.272.4.2542 | author2=Sundaresh CS  | author3=Feinstein SI  | display-authors=3  | last4=Dodia  | first4=C  | last5=Skach  | first5=WR  | last6=Jain  | first6=MK  | last7=Nagase  | first7=T | last8=Seki | first8=N  | last9=Ishikawa  | first9=K  }}
*{{cite journal  | author=Nagase T, Miyajima N, Tanaka A, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=2 |issue= 1 |pages= 37-43 |year= 1995 |pmid= 7788527 |doi= }}
*{{cite journal |vauthors=Frank S, Munz B, Werner S |title=The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene |journal=Oncogene |volume=14 |issue= 8 |pages= 915–21 |year= 1997 |pmid= 9050990 |doi= 10.1038/sj.onc.1200905 }}
*{{cite journal | author=Golaz O, Hughes GJ, Frutiger S, ''et al.'' |title=Plasma and red blood cell protein maps: update 1993. |journal=Electrophoresis |volume=14 |issue= 11 |pages= 1223-31 |year= 1994 |pmid= 8313871 |doi=  }}
*{{cite journal  |vauthors=Kang SW, Baines IC, Rhee SG |title=Characterization of a mammalian peroxiredoxin that contains one conserved cysteine |journal=J. Biol. Chem. |volume=273 |issue= 11 |pages= 6303–11 |year= 1998 |pmid= 9497358 |doi=10.1074/jbc.273.11.6303  }}
*{{cite journal  | author=Kim TS, Sundaresh CS, Feinstein SI, ''et al.'' |title=Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2542-50 |year= 1997 |pmid= 8999971 |doi=  }}
*{{cite journal  | author=Choi HJ |title=Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution |journal=Nat. Struct. Biol. |volume=5 |issue= 5 |pages= 400–6 |year= 1998 |pmid= 9587003 |doi=10.1038/nsb0598-400 | author2=Kang SW  | author3=Yang CH  | display-authors=3  | last4=Rhee  | first4=Sue Goo  | last5=Ryu  | first5=Seong-Eon  }}
*{{cite journal | author=Frank S, Munz B, Werner S |title=The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. |journal=Oncogene |volume=14 |issue= 8 |pages= 915-21 |year= 1997 |pmid= 9050990 |doi= 10.1038/sj.onc.1200905 }}
*{{cite journal  | author=Chen JW |title=1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28421–7 |year= 2000 |pmid= 10893423 |doi= 10.1074/jbc.M005073200 | author2=Dodia C  | author3=Feinstein SI  | display-authors=3  | last4=Jain  | first4=MK  | last5=Fisher  | first5=AB }}
*{{cite journal  | author=Kang SW, Baines IC, Rhee SG |title=Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. |journal=J. Biol. Chem. |volume=273 |issue= 11 |pages= 6303-11 |year= 1998 |pmid= 9497358 |doi= }}
*{{cite journal  |vauthors=Fatma N, Singh DP, Shinohara T, Chylack LT |title=Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48899–907 |year= 2002 |pmid= 11677226 |doi= 10.1074/jbc.M100733200 }}
*{{cite journal | author=Choi HJ, Kang SW, Yang CH, ''et al.'' |title=Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. |journal=Nat. Struct. Biol. |volume=5 |issue= 5 |pages= 400-6 |year= 1998 |pmid= 9587003 |doi=  }}
*{{cite journal  | author=Wagner E |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777–85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525  | pmc=1222825  | author2=Luche S  | author3=Penna L  | display-authors=3  | last4=Chevallet  | first4=Mireille  | last5=Van Dorsselaer  | first5=Alain  | last6=Leize-Wagner  | first6=Emmanuelle  | last7=Rabilloud  | first7=Thierry }}
*{{cite journal | author=Chen JW, Dodia C, Feinstein SI, ''et al.'' |title=1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28421-7 |year= 2000 |pmid= 10893423 |doi= 10.1074/jbc.M005073200 }}
*{{cite journal  | author=Leavey PJ |title=A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45181–7 |year= 2003 |pmid= 12121978 |doi= 10.1074/jbc.M202869200  | author2=Gonzalez-Aller C  | author3=Thurman G  | display-authors=3  | last4=Kleinberg  | first4=M  | last5=Rinckel  | first5=L  | last6=Ambruso  | first6=DW  | last7=Freeman  | first7=S  | last8=Kuypers  | first8=FA  | last9=Ambruso  | first9=DR }}
*{{cite journal  | author=Fatma N, Singh DP, Shinohara T, Chylack LT |title=Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48899-907 |year= 2002 |pmid= 11677226 |doi= 10.1074/jbc.M100733200 }}
*{{cite journal  | author=Manevich Y |title=1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 18 |pages= 11599–604 |year= 2002 |pmid= 12193653 |doi= 10.1073/pnas.182384499  | pmc=129315  | author2=Sweitzer T  | author3=Pak JH  | display-authors=3  | last4=Feinstein  | first4=SI  | last5=Muzykantov  | first5=V  | last6=Fisher  | first6=AB }}
*{{cite journal  | author=Wagner E, Luche S, Penna L, ''et al.'' |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777-85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  | author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Leavey PJ, Gonzalez-Aller C, Thurman G, ''et al.'' |title=A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45181-7 |year= 2003 |pmid= 12121978 |doi= 10.1074/jbc.M202869200 }}
*{{cite journal  | author=Krapfenbauer K |title=Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders |journal=Brain Res. |volume=967 |issue= 1–2 |pages= 152–60 |year= 2003 |pmid= 12650976 |doi=10.1016/S0006-8993(02)04243-9  | author2=Engidawork E  | author3=Cairns N  | display-authors=3  | last4=Fountoulakis  | first4=M  | last5=Lubec  | first5=G  }}
*{{cite journal | author=Manevich Y, Sweitzer T, Pak JH, ''et al.'' |title=1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 18 |pages= 11599-604 |year= 2002 |pmid= 12193653 |doi= 10.1073/pnas.182384499 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Krapfenbauer K, Engidawork E, Cairns N, ''et al.'' |title=Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. |journal=Brain Res. |volume=967 |issue= 1-2 |pages= 152-60 |year= 2003 |pmid= 12650976 |doi= }}
}}
{{refend}}
{{refend}}


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[[Category:Genes mutated in mice]]
[[Category:EC 1.11.1]]
[[Category:EC 3.1.1]]

Revision as of 18:39, 7 September 2017

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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

Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene.[1][2] It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.[2]

Model organisms

Model organisms have been used in the study of PRDX6 function. A conditional knockout mouse line, called Prdx6tm1a(EUCOMM)Wtsi[7][8] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[9][10][11]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[5][12] Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.[5]

References

  1. ↑ Phelan SA (Mar 2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant". Antioxid Redox Signal. 1 (4): 571–84. PMID 11233154.
  2. ↑ 2.0 2.1 "Entrez Gene: PRDX6 peroxiredoxin 6".
  3. ↑ "Salmonella infection data for Prdx6". Wellcome Trust Sanger Institute.
  4. ↑ "Citrobacter infection data for Prdx6". Wellcome Trust Sanger Institute.
  5. ↑ 5.0 5.1 5.2 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  6. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  7. ↑ "International Knockout Mouse Consortium".
  8. ↑ "Mouse Genome Informatics".
  9. ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  10. ↑ Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  11. ↑ Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  12. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

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