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PADI4

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PADI4
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPADI4, PAD, PAD4, PADI5, PDI4, PDI5, peptidyl arginine deiminase 4
External IDsOMIM: 605347; MGI: 1338898; HomoloGene: 7883; GeneCards: PADI4; OMA:PADI4 - orthologs
EC number3.5.3.15
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012387

NM_011061

RefSeq (protein)

NP_036519

NP_035191

Location (UCSC)Chr 1: 17.31 – 17.36 MbChr 4: 140.47 – 140.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein-arginine deiminase type-4, is a human protein which in humans is encoded by the PADI4 gene.[5][6] The protein as an enzyme, specifically protein-arginine deiminase, a type of hydrolase.

Molecular biology

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The human gene is found on the short arm of Chromosome 1 near the telomere (1p36.13). It is located on the Watson (plus) strand and is 55,806 bases long. The protein is 663 amino acids long with a molecular weight of 74,095 Da.[5]

Function

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This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine to citrulline residues (citrullination). This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response.[6] PADI4 plays a role in the epigenetics,[7] the deimination of arginines on histones H3 and H4 can act antagonistically to arginine methylation.[8]

The protein may be found in oligomers and binds 5 calcium ions per subunit. It catalyses the reaction:

  • Protein L-arginine + H2O = protein L-citrulline + NH3

Subcellular and tissue distribution

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It is normally found in the cytoplasm, nucleus and in cytoplasmic granules of eosinophils and neutrophils. It is not expressed in peripheral monocytes or lymphocytes. It is also expressed in rheumatoid arthritis synovial tissues.

References

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  1. ^ a b c ENSG00000159339 GRCh38: Ensembl release 89: ENSG00000280908, ENSG00000159339Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025330Ensembl, 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. ^ a b Nakashima K, Hagiwara T, Ishigami A, Nagata S, Asaga H, Kuramoto M, et al. (September 1999). "Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)". The Journal of Biological Chemistry. 274 (39): 27786–27792. doi:10.1074/jbc.274.39.27786. PMID 10488123.
  6. ^ a b "Entrez Gene: PADI4 peptidyl arginine deiminase, type IV".
  7. ^ Sams KL, Mukai C, Marks BA, Mittal C, Demeter EA, Nelissen S, et al. (October 2022). "Delayed puberty, gonadotropin abnormalities and subfertility in male Padi2/Padi4 double knockout mice". Reproductive Biology and Endocrinology. 20 (1): 150. doi:10.1186/s12958-022-01018-w. PMC 9555066. PMID 36224627.
  8. ^ Kouzarides T (February 2007). "Chromatin modifications and their function". Cell. 128 (4): 693–705. doi:10.1016/j.cell.2007.02.005. PMID 17320507.

Further reading

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