PADI2

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)
End	17,119,451 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	140,679,897 bp
RNA expression pattern
	Top expressed in
	internal globus pallidus; ; inferior olivary nucleus; ; inferior ganglion of vagus nerve; ; middle frontal gyrus; ; external globus pallidus; ; subthalamic nucleus; ; gastrocnemius muscle; ; tibialis anterior muscle; ; optic nerve; ; ventral tegmental area;
	Top expressed in
	saccule; ; lacrimal gland; ; digastric muscle; ; retinal pigment epithelium; ; sternocleidomastoid muscle; ; stria vascularis; ; triceps brachii muscle; ; ankle; ; vastus lateralis muscle; ; utricle;
	More reference expression data
	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; cytoplasm; cytosol; extracellular region; nucleus; azurophil granule lumen;
Biological process	negative regulation of chemokine-mediated signaling pathway; substantia nigra development; intracellular estrogen receptor signaling pathway; negative regulation of lymphocyte chemotaxis; chromatin organization; neutrophil degranulation; cellular response to leukemia inhibitory factor;
	Sources:Amigo / QuickGO
Orthologs
	11240
	18600
	ENSG00000117115
	ENSMUSG00000028927
	Q9Y2J8
	Q08642
	NM_007365
	NM_008812
	NP_031391
	NP_032838
	Wikidata
View/Edit Human	View/Edit Mouse

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

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[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000117115 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028927 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1016/S0021-9258(19)84818-4. PMID 2768262.
^ ^a ^b "Entrez Gene: PADI2 peptidyl arginine deiminase, type II".

Further reading[edit]

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. S2CID 22194514.
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. Bibcode:2001Sci...291.1304V. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 45747014.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. 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. S2CID 27139497.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000117115 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid2768262-5] 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. doi:10.1016/S0021-9258(19)84818-4. PMID 2768262.

[entrez-6] "Entrez Gene: PADI2 peptidyl arginine deiminase, type II".

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PADI2

References[edit]

Further reading[edit]

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