OAZ1

OAZ1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4ZGY, 4ZGZ, 5BWA
Identifiers
Aliases	OAZ1, AZI, OAZ, ornithine decarboxylase antizyme 1, AZ1
External IDs	OMIM: 601579; MGI: 109433; HomoloGene: 7455; GeneCards: OAZ1; OMA:OAZ1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.3 Start 2,269,509 bp[1] End 2,273,490 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 39.72 cM Start 80,662,490 bp[2] End 80,665,124 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Pons blood pylorus pars compacta renal medulla superior vestibular nucleus monocyte cardia postcentral gyrus parotid gland Top expressed in bone marrow neural layer of retina secondary oocyte proximal tubule zygote right kidney Mesencephalon quadriceps femoris muscle neural tube thymus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ornithine decarboxylase inhibitor activity protein binding Cellular component cytosol nucleus cytoplasm Biological process positive regulation of intracellular protein transport polyamine biosynthetic process negative regulation of polyamine transmembrane transport negative regulation of catalytic activity regulation of cellular amino acid metabolic process positive regulation of protein catabolic process polyamine metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4946 18245 Ensembl ENSG00000104904 ENSMUSG00000035242 UniProt P54368 P54369 RefSeq (mRNA) NM_004152 NM_001301020 NM_001301034 NM_008753 RefSeq (protein) NP_001287949 NP_004143 NP_001287963 NP_032779 Location (UCSC) Chr 19: 2.27 – 2.27 Mb Chr 10: 80.66 – 80.67 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ornithine decarboxylase antizyme is an enzyme that in humans is encoded by the OAZ1 gene.[5][6][7]

Ornithine decarboxylase catalyzes the conversion of ornithine to putrescine in the first and apparently rate-limiting step in polyamine biosynthesis. The ornithine decarboxylase antizymes play a role in the regulation of polyamine synthesis by binding to and inhibiting ornithine decarboxylase. Antizyme expression is auto-regulated by polyamine-enhanced translational frameshifting. The antizyme encoded by this gene inhibits ornithine decarboxylase and accelerates its degradation.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000104904 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000035242 – 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. Tewari DS, Qian Y, Thornton RD, Pieringer J, Taub R, Mochan E, Tewari M (Feb 1995). "Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme". Biochim Biophys Acta. 1209 (2): 293–5. doi:10.1016/0167-4838(94)90199-6. PMID 7811704.
6. Matsufuji S, Inazawa J, Hayashi T, Miyazaki Y, Ichiba T, Furusaka A, Matsufuji T, Atkins JF, Gesteland RF, Murakami Y, Hayashi S (Mar 1997). "Assignment of the human antizyme gene (OAZ) to chromosome 19p13.3 by fluorescence in situ hybridization". Genomics. 38 (1): 102–104. doi:10.1006/geno.1996.0601. PMID 8954789.
7. "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

Further reading

• Coffino P (2000). "Polyamines in spermiogenesis: not now, darling". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4421–4423. Bibcode:2000PNAS...97.4421C. doi:10.1073/pnas.97.9.4421. PMC 34313. PMID 10781034.
• Savage RE, Nofzinger K, Bedell C, et al. (1989). "Chloroform-induced multiple forms of ornithine decarboxylase: differential sensitivity of forms to enhancement by diethyl maleate and inhibition by ODC-antizyme". Journal of Toxicology and Environmental Health. 27 (1): 57–64. doi:10.1080/15287398909531278. PMID 2724368.
• Matsufuji S, Matsufuji T, Miyazaki Y, et al. (1995). "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme". Cell. 80 (1): 51–60. doi:10.1016/0092-8674(95)90450-6. PMC 7133313. PMID 7813017.
• Mamroud-Kidron E, Omer-Itsicovich M, Bercovich Z, et al. (1995). "A unified pathway for the degradation of ornithine decarboxylase in reticulocyte lysate requires interaction with the polyamine-induced protein, ornithine decarboxylase antizyme". Eur. J. Biochem. 226 (2): 547–554. doi:10.1111/j.1432-1033.1994.tb20079.x. PMID 8001569.
• Ichiba T, Matsufuji S, Miyazaki Y, et al. (1994). "Functional regions of ornithine decarboxylase antizyme". Biochem. Biophys. Res. Commun. 200 (3): 1721–1727. doi:10.1006/bbrc.1994.1651. PMID 8185631.
• Yang D, Takii T, Hayashi H, et al. (1997). "Molcecular cloning of human antizyme cDNA". Biochem. Mol. Biol. Int. 38 (5): 957–64. PMID 9132164.
• Hayashi T, Matsufuji S, Hayashi S (1998). "Characterization of the human antizyme gene". Gene. 203 (2): 131–139. doi:10.1016/S0378-1119(97)00504-0. PMID 9426243.
• Zhu C, Lang DW, Coffino P (1999). "Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport". J. Biol. Chem. 274 (37): 26425–26430. doi:10.1074/jbc.274.37.26425. PMID 10473601.
• Chen H, MacDonald A, Coffino P (2003). "Structural elements of antizymes 1 and 2 are required for proteasomal degradation of ornithine decarboxylase". J. Biol. Chem. 277 (48): 45957–45961. doi:10.1074/jbc.M206799200. PMID 12359729.
• Ike A, Yamada S, Tanaka H, et al. (2003). "Structure and promoter activity of the gene encoding ornithine decarboxylase antizyme expressed exclusively in haploid germ cells in testis (OAZt/Oaz3)". Gene. 298 (2): 183–193. doi:10.1016/S0378-1119(02)00978-2. PMID 12426106.
• 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): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–535. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824.
• Mangold U, Leberer E (2005). "Regulation of all members of the antizyme family by antizyme inhibitor". Biochem. J. 385 (Pt 1): 21–8. doi:10.1042/BJ20040547. PMC 1134669. PMID 15355308.
• Choi KS, Suh YH, Kim WH, et al. (2005). "Stable siRNA-mediated silencing of antizyme inhibitor: regulation of ornithine decarboxylase activity". Biochem. Biophys. Res. Commun. 328 (1): 206–212. doi:10.1016/j.bbrc.2004.11.172. PMID 15670771.
• Ku M, Howard S, Ni W, et al. (2006). "OAZ regulates bone morphogenetic protein signaling through Smad6 activation". J. Biol. Chem. 281 (8): 5277–5287. doi:10.1074/jbc.M510004200. PMID 16373339.
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–814. doi:10.1016/j.cell.2006.03.032. PMID 16713569. S2CID 13709685.
• Tsuji T, Katsurano M, Ibaragi S, et al. (2007). "Ornithine decarboxylase antizyme upregulates DNA-dependent protein kinase and enhances the nonhomologous end-joining repair of DNA double-strand breaks in human oral cancer cells". Biochemistry. 46 (31): 8920–8932. doi:10.1021/bi7000328. PMID 17630775.