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
Gene location (Human)
Chr.	Chromosome 19 (human)
End	2,273,490 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	80,665,124 bp
RNA expression pattern
	Top expressed in
	pons; ; blood; ; pylorus; ; renal medulla; ; superior vestibular nucleus; ; monocyte; ; cardia; ; postcentral gyrus; ; parotid gland; ; cancellous bone;
	Top expressed in
	bone marrow; ; secondary oocyte; ; proximal tubule; ; mesencephalon; ; quadriceps femoris muscle; ; neural tube; ; thymus; ; heart; ; blastocyst; ; olfactory bulb;
	More reference expression data
	; ;
	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
	4946
	18245
	ENSG00000104904
	ENSMUSG00000035242
	P54368
	P54369
	NM_004152 ; NM_001301020
	NM_001301034 ; NM_008753
	NP_001287949 ; NP_004143
	NP_001287963 ; NP_032779
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 25, 2022

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]

Related Research Articles

<span class="mw-page-title-main">Ornithine decarboxylase</span>

The enzyme ornithine decarboxylase catalyzes the decarboxylation of ornithine to form putrescine. This reaction is the committed step in polyamine synthesis. In humans, this protein has 461 amino acids and forms a homodimer.

<span class="mw-page-title-main">Antizyme RNA frameshifting stimulation element</span> Structural element

Antizyme RNA frameshifting stimulation element is a structural element which is found in antizyme mRNA and is known to promote frameshifting. Antizyme genes have two partially overlapping open reading frames, the second, which encodes the functional (antizyme) protein requires +1 translational frameshifting. This frameshift is stimulated by a pseudoknot present 3' of the frameshift site in the antizyme mRNA. The frameshifting efficiency is dependent on the concentration of polyamines in the cell, when the polyamine concentration is high frameshifting is more likely to occur which leads to an increase in the quantity of functional antizyme produced. The functional antizyme acts to reduce ornithine decarboxylase (ODC) activity which leads to a drop in polyamines present in the cell. Therefore, this family can be thought of as a biosensor for intracellular free polyamines that functions via a negative feedback loop.

In molecular biology, Ornithine decarboxylase antizyme (ODC-AZ) is an ornithine decarboxylase inhibitor. It binds to, and destabilises, ornithine decarboxylase (ODC), a key enzyme in polyamine synthesis. ODC is then rapidly degraded. It was first characterized in 1981. The expression of ODC-AZ requires programmed, ribosomal frameshifting which is modulated according to the cellular concentration of polyamines. High levels of polyamines induce a +1 ribosomal frameshift in the translation of mRNA for the antizyme leading to the expression of a full-length protein. At least two forms of ODC-AZ exist in mammals and the protein has been found in Drosophila as well as in Saccharomyces yeast.

Ornithine decarboxylase is an enzyme that in humans is encoded by the ODC1 gene.

Acyl-CoA-binding protein in humans belongs to the family of Acyl-CoA-binding proteins.

<span class="mw-page-title-main">ADAMTS1</span> Protein-coding gene in the species Homo sapiens

A disintegrin and metalloproteinase with thrombospondin motifs 1 is an enzyme that in humans is encoded by the ADAMTS1 gene.

DnaJ homolog subfamily A member 1 is a protein that in humans is encoded by the DNAJA1 gene.

Eukaryotic translation initiation factor 2 subunit 2 (eIF2β) is a protein that in humans is encoded by the EIF2S2 gene.

40S ribosomal protein S13 is a protein that in humans is encoded by the RPS13 gene.

Pancreatic secretory granule membrane major glycoprotein GP2 is a protein that in humans is encoded by the GP2 gene.

Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 also known as membrane-associated guanylate kinase inverted 2 (MAGI-2) and atrophin-1-interacting protein 1 (AIP-1) is an enzyme that in humans is encoded by the MAGI2 gene.

Cathepsin W is a protein that in humans is encoded by the CTSW gene.

Serpin B13 is a protein that in humans is encoded by the SERPINB13 gene.

Antizyme inhibitor 2 (AzI2) also erroneously known as arginine decarboxylase (ADC) is a protein that in humans is encoded by the AZIN2 gene. In contrast to initial suggestions, Antizyme inhibitor 2 does not act as arginine decarboxylase (ADC) in mammalian cells

Zinc finger protein 267 is a protein that in humans is encoded by the ZNF267 gene.

cAMP-dependent protein kinase inhibitor gamma is a protein that in humans is encoded by the PKIG gene.

GSK-3-binding protein FRAT2 is a protein that in humans is encoded by the FRAT2 gene.

Antizyme inhibitor 1 is a protein that in humans is encoded by the AZIN1 gene.

Ornithine decarboxylase antizyme 2 is an enzyme that in humans is encoded by the OAZ2 gene.

Zinc finger protein 23 is a protein that in humans is encoded by the ZNF23 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000104904 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000035242 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000104904 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid7811704-5] 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.

[pmid8954789-6] 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.

[entrez-7] 1 2 "Entrez Gene: OAZ1 ornithine decarboxylase antizyme 1".

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OAZ1

Related Research Articles

References

Further reading