PADI4

From Wikipedia, the free encyclopedia

Peptidyl arginine deiminase, type IV

PDB rendering based on 1wd8.

Available structures: 1wd8, 1wd9, 1wda, 2dew, 2dex, 2dey, 2dw5

Identifiers

Symbol(s)

PADI4; PAD; PADI5; PDI4; PDI5

External IDs

OMIM: 605347 MGI: 1338898 HomoloGene: 7883

Gene ontology
Molecular Function:	• protein-arginine deiminase activity • calcium ion binding • hydrolase activity
Cellular Component:	• nucleus
Biological Process:	• transcription • regulation of transcription, DNA-dependent • protein modification process • chromatin modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012387 (mRNA)
NP_036519 (protein)

XM_991479 (mRNA)
XP_996573 (protein)

Location

Chr 1: 17.51 - 17.56 Mb

Chr 4: 140.02 - 140.05 Mb

Pubmed search

[1]

[2]

Peptidyl arginine deiminase, type IV, also known as PADI4, is a human gene.^[1]

This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine residues to citrulline residues. This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response.^[1]

[edit] References

^ ^a ^b Entrez Gene: PADI4 peptidyl arginine deiminase, type IV.

[edit] Further reading

Nakashima K, Hagiwara T, Ishigami A, et al. (1999). "Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3).". J. Biol. Chem. 274 (39): 27786-92. PMID 10488123.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546-60. PMID 11042152.
Asaga H, Nakashima K, Senshu T, et al. (2001). "Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils.". J. Leukoc. Biol. 70 (1): 46-51. PMID 11435484.
Nakashima K, Hagiwara T, Yamada M (2003). "Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes.". J. Biol. Chem. 277 (51): 49562-8. doi:10.1074/jbc.M208795200. PMID 12393868.
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. PMID 12477932.
Suzuki A, Yamada R, Chang X, et al. (2003). "Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis.". Nat. Genet. 34 (4): 395-402. doi:10.1038/ng1206. PMID 12833157.
Barton A, Bowes J, Eyre S, et al. (2004). "A functional haplotype of the PADI4 gene associated with rheumatoid arthritis in a Japanese population is not associated in a United Kingdom population.". Arthritis Rheum. 50 (4): 1117-21. doi:10.1002/art.20169. PMID 15077293.
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.
Arita K, Hashimoto H, Shimizu T, et al. (2004). "Structural basis for Ca(2+)-induced activation of human PAD4.". Nat. Struct. Mol. Biol. 11 (8): 777-83. doi:10.1038/nsmb799. PMID 15247907.
Hoppe B, Heymann GA, Tolou F, et al. (2005). "High variability of peptidylarginine deiminase 4 (PADI4) in a healthy white population: characterization of six new variants of PADI4 exons 2-4 by a novel haplotype-specific sequencing-based approach.". J. Mol. Med. 82 (11): 762-7. doi:10.1007/s00109-004-0584-6. PMID 15338034.
Cuthbert GL, Daujat S, Snowden AW, et al. (2004). "Histone deimination antagonizes arginine methylation.". Cell 118 (5): 545-53. doi:10.1016/j.cell.2004.08.020. PMID 15339660.
Wang Y, Wysocka J, Sayegh J, et al. (2004). "Human PAD4 regulates histone arginine methylation levels via demethylimination.". Science 306 (5694): 279-83. doi:10.1126/science.1101400. PMID 15345777.
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. PMID 15489334.
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.
Lee YH, Coonrod SA, Kraus WL, et al. (2005). "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination.". Proc. Natl. Acad. Sci. U.S.A. 102 (10): 3611-6. doi:10.1073/pnas.0407159102. PMID 15731352.
Kearney PL, Bhatia M, Jones NG, et al. (2005). "Kinetic characterization of protein arginine deiminase 4: a transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis.". Biochemistry 44 (31): 10570-82. doi:10.1021/bi050292m. PMID 16060666.
Ikari K, Kuwahara M, Nakamura T, et al. (2005). "Association between PADI4 and rheumatoid arthritis: a replication study.". Arthritis Rheum. 52 (10): 3054-7. doi:10.1002/art.21309. PMID 16200584.
Chang X, Han J (2006). "Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors.". Mol. Carcinog. 45 (3): 183-96. doi:10.1002/mc.20169. PMID 16355400.
Plenge RM, Padyukov L, Remmers EF, et al. (2006). "Replication of putative candidate-gene associations with rheumatoid arthritis in >4,000 samples from North America and Sweden: association of susceptibility with PTPN22, CTLA4, and PADI4.". Am. J. Hum. Genet. 77 (6): 1044-60. doi:10.1086/498651. PMID 16380915.
Hoppe B, Häupl T, Gruber R, et al. (2006). "Detailed analysis of the variability of peptidylarginine deiminase type 4 in German patients with rheumatoid arthritis: a case-control study.". Arthritis Res. Ther. 8 (2): R34. doi:10.1186/ar1889. PMID 16469113.