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PADI3
Identifiers
Aliases	PADI3, PAD3, PDI3, peptidyl arginine deiminase 3, UHS1
External IDs	OMIM: 606755; MGI: 1338891; HomoloGene: 7882; GeneCards: PADI3; OMA:PADI3 - orthologs
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.5.3.15 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 1 (human) Band 1p36.13 Start 17,249,098 bp End 17,284,233 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 D3|4 72.5 cM Start 140,512,676 bp End 140,537,959 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in urinary bladder testicle olfactory zone of nasal mucosa vagina tonsil skin of abdomen gallbladder gonad prostate skin of leg Top expressed in lip hair follicle skin of back embryo granulocyte skin of abdomen morula transitional epithelium of urinary bladder epiblast Gonadal ridge More reference expression data BioGPS More reference expression data
Gene ontology Molecular function hydrolase activity calcium ion binding identical protein binding protein-arginine deiminase activity Cellular component cytosol nucleus cytoplasm Biological process chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51702 18601 Ensembl ENSG00000280549 ENSG00000142619 ENSMUSG00000025328 UniProt Q9ULW8 Q9Z184 RefSeq (mRNA) NM_016233 NM_011060 RefSeq (protein) NP_057317 NP_035190 Location (UCSC) Chr 1: 17.25 – 17.28 Mb Chr 4: 140.51 – 140.54 Mb PubMed search
Wikidata
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Peptidyl arginine deiminase, type III, also known as PADI3, is a protein which in humans is encoded by the PADI3 gene.

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 III enzyme modulates hair structural proteins, such as filaggrin in the hair follicle and trichohyalin in the inner root sheath, during hair follicle formation. Together with the type I enzyme, this enzyme may also play a role in terminal differentiation of the epidermis. This gene exists in a cluster with four other paralogous genes.

See also

• Protein-arginine deiminase

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. 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.
• Rus'd AA, Ikejiri Y, Ono H, et al. (1999). "Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse". Eur. J. Biochem. 259 (3): 660–9. doi:10.1046/j.1432-1327.1999.00083.x. PMID 10092850.
• Kanno T, Kawada A, Yamanouchi J, et al. (2000). "Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin". J. Invest. Dermatol. 115 (5): 813–23. doi:10.1046/j.1523-1747.2000.00131.x. PMID 11069618.
• 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.
• 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.
• Iida A, Nakamura Y (2004). "Identification of 45 novel SNPs in the 83-kb region containing peptidylarginine deiminase types 1 and 3 loci on chromosomal band 1p36.13". J. Hum. Genet. 49 (7): 387–90. doi:10.1007/s10038-004-0156-1. PMID 15150696.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Nachat R, Méchin MC, Takahara H, et al. (2005). "Peptidylarginine deiminase isoforms 1-3 are expressed in the epidermis and involved in the deimination of K1 and filaggrin". J. Invest. Dermatol. 124 (2): 384–93. doi:10.1111/j.0022-202X.2004.23568.x. PMID 15675958.
• Méchin MC, Enji M, Nachat R, et al. (2005). "The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations". Cell. Mol. Life Sci. 62 (17): 1984–95. doi:10.1007/s00018-005-5196-y. PMC 11139075. PMID 16091842. S2CID 23610590.
• Dong S, Kanno T, Yamaki A, et al. (2006). "NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes". Biochem. J. 397 (3): 449–59. doi:10.1042/BJ20051939. PMC 1533312. PMID 16671893.
• 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.