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{{Infobox_gene}}
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'''Protein-arginine deiminase type-2''' is an [[enzyme]] that in humans is encoded by the ''PADI2'' [[gene]].<ref name="pmid2768262">{{cite journal | vauthors = Watanabe K, Senshu T | title = Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase | journal = J Biol Chem | volume = 264 | issue = 26 | pages = 15255–60 |date=Oct 1989 | pmid = 2768262 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PADI2 peptidyl arginine deiminase, type II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11240| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Peptidyl arginine deiminase, type II
| HGNCid = 18341
| Symbol = PADI2
| AltSymbols =; KIAA0994; PAD-H19; PAD2; PDI2
| OMIM = 607935
| ECnumber = 
| Homologene = 7214
| MGIid = 1338892
| GeneAtlas_image1 = PBB_GE_PADI2_209791_at_tn.png
| Function = {{GNF_GO|id=GO:0004668 |text = protein-arginine deiminase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =  
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 11240
    | Hs_Ensembl = ENSG00000117115
    | Hs_RefseqProtein = NP_031391
    | Hs_RefseqmRNA = NM_007365
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 17265843
    | Hs_GenLoc_end = 17318517
    | Hs_Uniprot = Q9Y2J8
    | Mm_EntrezGene = 18600
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_001004735
    | Mm_RefseqProtein = XP_001004735
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Peptidyl arginine deiminase, type II''', also known as '''PADI2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PADI2 peptidyl arginine deiminase, type II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11240| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes.<ref name="entrez">{{cite web | title = Entrez Gene: PADI2 peptidyl arginine deiminase, type II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11240| accessdate = }}</ref>
| summary_text = This gene encodes a member of the [[Peptide|peptidyl]] [[arginine deiminase]] family of enzymes, which catalyze the post-[[Translation (biology)|translational]] deimination of proteins by converting [[arginine]] residues into [[citrulline]]s in the presence of [[calcium ions]]. The family members have distinct [[substrate (biochemistry)|substrate]] specificities and tissue-specific [[Gene expression|expression]] patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include [[myelin]] basic protein in the [[central nervous system]] and [[vimentin]] in [[skeletal muscle]] and [[macrophages]].  
 
This enzyme is thought to play a role in the onset and progression of [[neurodegenerative]] human disorders, including [[Alzheimer]] disease and [[multiple sclerosis]], and it has also been implicated in [[Glaucoma|glaucoma pathogenesis]]. This gene exists in a cluster with four other [[paralogous]] genes.<ref name="entrez">{{cite web | title = Entrez Gene: PADI2 peptidyl arginine deiminase, type II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11240| accessdate = }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ |title=PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. |journal=Bioessays |volume=25 |issue= 11 |pages= 1106-18 |year= 2004 |pmid= 14579251 |doi= 10.1002/bies.10357 }}
*{{cite journal  | vauthors=Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ |title=PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. |journal=BioEssays |volume=25 |issue= 11 |pages= 1106–18 |year= 2004 |pmid= 14579251 |doi= 10.1002/bies.10357 }}
*{{cite journal | author=Chavanas S, Méchin MC, Nachat R, ''et al.'' |title=Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. |journal=J. Dermatol. Sci. |volume=44 |issue= 2 |pages= 63-72 |year= 2006 |pmid= 16973334 |doi= 10.1016/j.jdermsci.2006.07.004 }}
*{{cite journal   |vauthors=Chavanas S, Méchin MC, Nachat R, etal |title=Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis. |journal=J. Dermatol. Sci. |volume=44 |issue= 2 |pages= 63–72 |year= 2006 |pmid= 16973334 |doi= 10.1016/j.jdermsci.2006.07.004 }}
*{{cite journal  | author=Moscarello MA, Mastronardi FG, Wood DD |title=The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis. |journal=Neurochem. Res. |volume=32 |issue= 2 |pages= 251-6 |year= 2007 |pmid= 17031564 |doi= 10.1007/s11064-006-9144-5 }}
*{{cite journal  | vauthors=Moscarello MA, Mastronardi FG, Wood DD |title=The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis. |journal=Neurochem. Res. |volume=32 |issue= 2 |pages= 251–6 |year= 2007 |pmid= 17031564 |doi= 10.1007/s11064-006-9144-5  | pmc=1794624 }}
*{{cite journal | author=Watanabe K, Senshu T |title=Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase. |journal=J. Biol. Chem. |volume=264 |issue= 26 |pages= 15255-60 |year= 1989 |pmid= 2768262 |doi=  }}
*{{cite journal   |vauthors=Nagase T, Ishikawa K, Suyama M, etal |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63–70 |year= 1999 |pmid= 10231032 |doi=10.1093/dnares/6.1.63 }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 1 |pages= 63-70 |year= 1999 |pmid= 10231032 |doi=  }}
*{{cite journal   |vauthors=Venter JC, Adams MD, Myers EW, etal |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304–51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal | author=Venter JC, Adams MD, Myers EW, ''et al.'' |title=The sequence of the human genome. |journal=Science |volume=291 |issue= 5507 |pages= 1304-51 |year= 2001 |pmid= 11181995 |doi= 10.1126/science.1058040 }}
*{{cite journal   |vauthors=Ishigami A, Ohsawa T, Asaga H, etal |title=Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. |journal=Arch. Biochem. Biophys. |volume=407 |issue= 1 |pages= 25–31 |year= 2002 |pmid= 12392711 |doi=10.1016/S0003-9861(02)00516-7 }}
*{{cite journal | author=Ishigami A, Ohsawa T, Asaga H, ''et al.'' |title=Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. |journal=Arch. Biochem. Biophys. |volume=407 |issue= 1 |pages= 25-31 |year= 2002 |pmid= 12392711 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{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   |vauthors=Chavanas S, Méchin MC, Takahara H, etal |title=Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. |journal=Gene |volume=330 |issue=  |pages= 19–27 |year= 2004 |pmid= 15087120 |doi= 10.1016/j.gene.2003.12.038 }}
*{{cite journal | author=Chavanas S, Méchin MC, Takahara H, ''et al.'' |title=Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. |journal=Gene |volume=330 |issue=  |pages= 19-27 |year= 2004 |pmid= 15087120 |doi= 10.1016/j.gene.2003.12.038 }}
*{{cite journal   |vauthors=Sambandam T, Belousova M, Accaviti-Loper MA, etal |title=Increased peptidylarginine deiminase type II in hypoxic astrocytes. |journal=Biochem. Biophys. Res. Commun. |volume=325 |issue= 4 |pages= 1324–9 |year= 2005 |pmid= 15555572 |doi= 10.1016/j.bbrc.2004.10.173 }}
*{{cite journal | author=Sambandam T, Belousova M, Accaviti-Loper MA, ''et al.'' |title=Increased peptidylarginine deiminase type II in hypoxic astrocytes. |journal=Biochem. Biophys. Res. Commun. |volume=325 |issue= 4 |pages= 1324-9 |year= 2005 |pmid= 15555572 |doi= 10.1016/j.bbrc.2004.10.173 }}
*{{cite journal   |vauthors=Nakayama-Hamada M, Suzuki A, Kubota K, etal |title=Comparison of enzymatic properties between hPADI2 and hPADI4. |journal=Biochem. Biophys. Res. Commun. |volume=327 |issue= 1 |pages= 192–200 |year= 2005 |pmid= 15629448 |doi= 10.1016/j.bbrc.2004.11.152 }}
*{{cite journal | author=Nakayama-Hamada M, Suzuki A, Kubota K, ''et al.'' |title=Comparison of enzymatic properties between hPADI2 and hPADI4. |journal=Biochem. Biophys. Res. Commun. |volume=327 |issue= 1 |pages= 192-200 |year= 2005 |pmid= 15629448 |doi= 10.1016/j.bbrc.2004.11.152 }}
*{{cite journal   |vauthors=Ishigami A, Ohsawa T, Hiratsuka M, etal |title=Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. |journal=J. Neurosci. Res. |volume=80 |issue= 1 |pages= 120–8 |year= 2005 |pmid= 15704193 |doi= 10.1002/jnr.20431 }}
*{{cite journal | author=Ishigami A, Ohsawa T, Hiratsuka M, ''et al.'' |title=Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. |journal=J. Neurosci. Res. |volume=80 |issue= 1 |pages= 120-8 |year= 2005 |pmid= 15704193 |doi= 10.1002/jnr.20431 }}
*{{cite journal   |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal   |vauthors=Bhattacharya SK, Crabb JS, Bonilha VL, etal |title=Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. |journal=Invest. Ophthalmol. Vis. Sci. |volume=47 |issue= 6 |pages= 2508–14 |year= 2006 |pmid= 16723463 |doi= 10.1167/iovs.05-1499 }}
*{{cite journal | author=Bhattacharya SK, Crabb JS, Bonilha VL, ''et al.'' |title=Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis. |journal=Invest. Ophthalmol. Vis. Sci. |volume=47 |issue= 6 |pages= 2508-14 |year= 2006 |pmid= 16723463 |doi= 10.1167/iovs.05-1499 }}
*{{cite journal   |vauthors=Mastronardi FG, Noor A, Wood DD, etal |title=Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated. |journal=J. Neurosci. Res. |volume=85 |issue= 9 |pages= 2006–16 |year= 2007 |pmid= 17469138 |doi= 10.1002/jnr.21329 }}
*{{cite journal | author=Mastronardi FG, Noor A, Wood DD, ''et al.'' |title=Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated. |journal=J. Neurosci. Res. |volume=85 |issue= 9 |pages= 2006-16 |year= 2007 |pmid= 17469138 |doi= 10.1002/jnr.21329 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 17:29, 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
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Wikidata
View/Edit Human

Protein-arginine deiminase type-2 is an enzyme that in humans is encoded by the PADI2 gene.[1][2]

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages.

This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes.[2]

References

  1. ↑ Watanabe K, Senshu T (Oct 1989). "Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase". J Biol Chem. 264 (26): 15255–60. PMID 2768262.
  2. ↑ 2.0 2.1 "Entrez Gene: PADI2 peptidyl arginine deiminase, type II".

Further reading



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