PADI2

Protein-arginine deiminase type-2 is an enzyme that in humans is encoded by the PADI2 gene.[5][6]

PADI2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4N20, 4N22, 4N24, 4N25, 4N26, 4N28, 4N2A, 4N2B, 4N2C, 4N2D, 4N2E, 4N2F, 4N2G, 4N2H, 4N2I, 4N2K, 4N2L, 4N2M, 4N2N
Identifiers
Aliases	PADI2, PAD-H19, PAD2, PDI2, peptidyl arginine deiminase 2
External IDs	OMIM: 607935 MGI: 1338892 HomoloGene: 7214 GeneCards: PADI2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.13 Start 17,066,761 bp[1] End 17,119,451 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 D3|4 73.01 cM Start 140,906,344 bp[2] End 140,952,586 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • calcium ion binding • estrogen receptor binding • hydrolase activity • protein-arginine deiminase activity • protein homodimerization activity • metal ion binding Cellular component • extracellular exosome • transcriptionally active chromatin • cytoplasm • cytosol • extracellular region • cell nucleus • azurophil granule lumen Biological process • negative regulation of chemokine-mediated signaling pathway • protein citrullination • chromatin-mediated maintenance of transcription • histone H3-R26 citrullination • substantia nigra development • intracellular estrogen receptor signaling pathway • regulation of chromatin disassembly • negative regulation of lymphocyte chemotaxis • chromatin organization • neutrophil degranulation • cellular response to leukemia inhibitory factor • histone citrullination Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11240	18600
Ensembl	ENSG00000117115	ENSMUSG00000028927
UniProt	Q9Y2J8	Q08642
RefSeq (mRNA)	NM_007365	NM_008812
RefSeq (protein)	NP_031391	NP_032838
Location (UCSC)	Chr 1: 17.07 – 17.12 Mb	Chr 4: 140.91 – 140.95 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000117115 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028927 - 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. 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.
6. "Entrez Gene: PADI2 peptidyl arginine deiminase, type II".

Further reading

• Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ (2004). "PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease". BioEssays. 25 (11): 1106–18. doi:10.1002/bies.10357. PMID 14579251.
• Chavanas S, Méchin MC, Nachat R, et al. (2006). "Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis". J. Dermatol. Sci. 44 (2): 63–72. doi:10.1016/j.jdermsci.2006.07.004. PMID 16973334.
• Moscarello MA, Mastronardi FG, Wood DD (2007). "The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis". Neurochem. Res. 32 (2): 251–6. doi:10.1007/s11064-006-9144-5. PMC 1794624. PMID 17031564.
• Nagase T, Ishikawa K, Suyama M, et al. (1999). "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". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
• Venter JC, Adams MD, Myers EW, et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. doi:10.1126/science.1058040. PMID 11181995.
• Ishigami A, Ohsawa T, Asaga H, et al. (2002). "Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin". Arch. Biochem. Biophys. 407 (1): 25–31. doi:10.1016/S0003-9861(02)00516-7. PMID 12392711.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chavanas S, Méchin MC, Takahara H, et al. (2004). "Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6". Gene. 330: 19–27. doi:10.1016/j.gene.2003.12.038. PMID 15087120.
• Sambandam T, Belousova M, Accaviti-Loper MA, et al. (2005). "Increased peptidylarginine deiminase type II in hypoxic astrocytes". Biochem. Biophys. Res. Commun. 325 (4): 1324–9. doi:10.1016/j.bbrc.2004.10.173. PMID 15555572.
• Nakayama-Hamada M, Suzuki A, Kubota K, et al. (2005). "Comparison of enzymatic properties between hPADI2 and hPADI4". Biochem. Biophys. Res. Commun. 327 (1): 192–200. doi:10.1016/j.bbrc.2004.11.152. PMID 15629448.
• Ishigami A, Ohsawa T, Hiratsuka M, et al. (2005). "Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease". J. Neurosci. Res. 80 (1): 120–8. doi:10.1002/jnr.20431. PMID 15704193.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
• Bhattacharya SK, Crabb JS, Bonilha VL, et al. (2006). "Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis". Invest. Ophthalmol. Vis. Sci. 47 (6): 2508–14. doi:10.1167/iovs.05-1499. PMID 16723463.
• Mastronardi FG, Noor A, Wood DD, et al. (2007). "Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated". J. Neurosci. Res. 85 (9): 2006–16. doi:10.1002/jnr.21329. PMID 17469138.