PADI1

PADI1
Identifiers
Aliases	PADI1 , HPAD10, PAD1, PDI, PDI1, peptidyl arginine deiminase 1
External IDs	OMIM: 607934; MGI: 1338893; HomoloGene: 7881; GeneCards: PADI1; OMA:PADI1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p36.13 Start 17,205,128 bp [1] End 17,246,007 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4 D3|4 72.62 cM Start 140,540,294 bp [2] End 140,573,089 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in vagina skin of leg skin of abdomen olfactory zone of nasal mucosa placenta tonsil substantia nigra minor salivary glands mucosa of transverse colon rectum Top expressed in cervix lip esophagus hair follicle conjunctival fornix decidua morula skin of back transitional epithelium of urinary bladder trachea More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding hydrolase activity protein-arginine deiminase activity metal ion binding Cellular component nucleus nucleoplasm cytoplasm cytosol Biological process chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 29943 18599 Ensembl ENSG00000142623 ENSG00000281459 ENSMUSG00000025329 UniProt Q9ULC6 Q9Z185 RefSeq (mRNA) NM_013358 NM_011059 RefSeq (protein) NP_037490 NP_035189 Location (UCSC) Chr 1: 17.21 – 17.25 Mb Chr 4: 140.54 – 140.57 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peptidyl arginine deiminase, type I, also known as PADI1, is a protein which in humans is encoded by the PADI1 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 I enzyme is involved in the late stages of epidermal differentiation, where it deiminates filaggrin and keratin K1, which maintains hydration of the stratum corneum, and hence the cutaneous barrier function. This enzyme may also play a role in hair follicle formation. This gene exists in a cluster with four other paralogous genes. ^[5]

References

1. ENSG00000281459 GRCh38: Ensembl release 89: ENSG00000142623, ENSG00000281459 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025329 – 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. "Entrez Gene: PADI1 peptidyl arginine deiminase, type I".
6. Guerrin M, Ishigami A, Méchin MC, Nachat R, Valmary S, Sebbag M, Simon M, Senshu T, Serre G (February 2003). "cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I". The Biochemical Journal. 370 (Pt 1): 167–74. doi:10.1042/BJ20020870. PMC   1223146 . PMID   12416996.

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" (PDF). 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.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Guerrin M, Ishigami A, Méchin MC, et al. (2003). "cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I". Biochem. J. 370 (Pt 1): 167–74. doi:10.1042/BJ20020870. PMC   1223146 . PMID   12416996.
• 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.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• 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.
• 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.
• 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.