OAZ1_MOUSE
ID OAZ1_MOUSE Reviewed; 227 AA.
AC P54369; O08610;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ornithine decarboxylase antizyme 1;
DE Short=ODC-Az;
GN Name=Oaz1; Synonyms=Oaz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9428668; DOI=10.1111/j.1432-1033.1997.0223a.x;
RA Nilsson J., Koskiniemi S., Persson K., Grahn B., Holm I.;
RT "Polyamines regulate both transcription and translation of the gene
RT encoding ornithine decarboxylase antizyme in mouse.";
RL Eur. J. Biochem. 250:223-231(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Kankare K., Uusi-Oukari M., Janne O.A.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH AZIN2.
RX PubMed=16916800; DOI=10.1074/jbc.m602840200;
RA Lopez-Contreras A.J., Lopez-Garcia C., Jimenez-Cervantes C., Cremades A.,
RA Penafiel R.;
RT "Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor
RT devoid of ornithine and arginine decarboxylating activity.";
RL J. Biol. Chem. 281:30896-30906(2006).
RN [4]
RP FUNCTION, AND INTERACTION WITH AZIN2.
RX PubMed=18062773; DOI=10.1042/bj20071423;
RA Snapir Z., Keren-Paz A., Bercovich Z., Kahana C.;
RT "ODCp, a brain- and testis-specific ornithine decarboxylase paralogue,
RT functions as an antizyme inhibitor, although less efficiently than AzI1.";
RL Biochem. J. 410:613-619(2008).
RN [5]
RP FUNCTION.
RX PubMed=18508777; DOI=10.1074/jbc.m801024200;
RA Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.;
RT "Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian
RT cells.";
RL J. Biol. Chem. 283:20761-20769(2008).
RN [6]
RP FUNCTION.
RX PubMed=19449338; DOI=10.1002/jcb.22168;
RA Lopez-Contreras A.J., Sanchez-Laorden B.L., Ramos-Molina B.,
RA de la Morena M.E., Cremades A., Penafiel R.;
RT "Subcellular localization of antizyme inhibitor 2 in mammalian cells:
RT Influence of intrinsic sequences and interaction with antizymes.";
RL J. Cell. Biochem. 107:732-740(2009).
RN [7]
RP INTERACTION WITH AZIN2.
RX PubMed=24967154; DOI=10.1016/j.fob.2014.05.004;
RA Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M.,
RA Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.;
RT "Structural and degradative aspects of ornithine decarboxylase antizyme
RT inhibitor 2.";
RL FEBS Open Bio 4:510-521(2014).
CC -!- FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that
CC negatively regulates ODC activity and intracellular polyamine
CC biosynthesis and uptake in response to increased intracellular
CC polyamine levels. Binds to ODC monomers, inhibiting the assembly of the
CC functional ODC homodimer, and targets the monomers for ubiquitin-
CC independent proteolytic destruction by the 26S proteasome
CC (PubMed:16916800, PubMed:18508777). Triggers ODC degradation by
CC inducing the exposure of a cryptic proteasome-interacting surface of
CC ODC (By similarity). Stabilizes AZIN2 by interfering with its
CC ubiquitination (PubMed:18062773). Also inhibits cellular uptake of
CC polyamines by inactivating the polyamine uptake transporter.
CC SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC repressor SNIP1. Involved in the translocation of AZIN2 from ER-Golgi
CC intermediate compartment (ERGIC) to the cytosol (PubMed:19449338).
CC {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:16916800,
CC ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777,
CC ECO:0000269|PubMed:19449338}.
CC -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC homodimerization (By similarity). Forms a ternary complex with PSMB4
CC and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By
CC similarity). Interacts with AZIN2; this interaction disrupts the
CC interaction between the antizyme and ODC1 (PubMed:16916800,
CC PubMed:18062773, PubMed:24967154). Interacts with FAM171A1 (By
CC similarity). {ECO:0000250|UniProtKB:P54368,
CC ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18062773,
CC ECO:0000269|PubMed:24967154}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-68
CC and Asp-69. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=P54369-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR EMBL; U52822; AAB96329.1; -; mRNA.
DR EMBL; U52823; AAB96330.1; -; Genomic_DNA.
DR EMBL; U84291; AAC53307.1; -; Genomic_DNA.
DR CCDS; CCDS56736.1; -. [P54369-1]
DR PIR; PC4378; PC4378.
DR RefSeq; NP_032779.2; NM_008753.4. [P54369-1]
DR AlphaFoldDB; P54369; -.
DR SMR; P54369; -.
DR IntAct; P54369; 1.
DR STRING; 10090.ENSMUSP00000137400; -.
DR iPTMnet; P54369; -.
DR PhosphoSitePlus; P54369; -.
DR PaxDb; P54369; -.
DR PRIDE; P54369; -.
DR ProteomicsDB; 289958; -. [P54369-1]
DR Antibodypedia; 1951; 118 antibodies from 25 providers.
DR DNASU; 18245; -.
DR Ensembl; ENSMUST00000180036; ENSMUSP00000137400; ENSMUSG00000035242. [P54369-1]
DR GeneID; 18245; -.
DR KEGG; mmu:18245; -.
DR UCSC; uc033frg.1; mouse. [P54369-1]
DR CTD; 4946; -.
DR MGI; MGI:109433; Oaz1.
DR VEuPathDB; HostDB:ENSMUSG00000035242; -.
DR eggNOG; KOG4387; Eukaryota.
DR GeneTree; ENSGT00940000159808; -.
DR InParanoid; P54369; -.
DR OMA; TRIFNVQ; -.
DR OrthoDB; 1403675at2759; -.
DR PhylomeDB; P54369; -.
DR TreeFam; TF314741; -.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR BioGRID-ORCS; 18245; 10 hits in 57 CRISPR screens.
DR ChiTaRS; Oaz1; mouse.
DR PRO; PR:P54369; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P54369; protein.
DR Bgee; ENSMUSG00000035242; Expressed in bone marrow and 64 other tissues.
DR ExpressionAtlas; P54369; baseline and differential.
DR Genevisible; P54369; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.630.60; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029914; ODC-AZ_1.
DR InterPro; IPR002993; ODC_AZ.
DR InterPro; IPR038581; ODC_AZ_sf.
DR PANTHER; PTHR10279; PTHR10279; 1.
DR PANTHER; PTHR10279:SF8; PTHR10279:SF8; 1.
DR Pfam; PF02100; ODC_AZ; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS01337; ODC_AZ; 1.
PE 1: Evidence at protein level;
KW Polyamine biosynthesis; Reference proteome; Ribosomal frameshifting;
KW Transport.
FT CHAIN 1..227
FT /note="Ornithine decarboxylase antizyme 1"
FT /id="PRO_0000220851"
FT CONFLICT 69
FT /note="D -> C (in Ref. 1; AAB96330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25133 MW; C2D0E1614C5F28A5 CRC64;
MVKSSLQRIL NSHCFAREKE GDKRSATLHA SRTMPLLSQH SRGGCSSESS RVALNCCSNL
GPGPRWCSDV PHPPLKIPGG RGNSQRDHSL SASILYSDER LNVTEEPTSN DKTRVLSIQS
TLTEAKQVTW RAVWSGGGLY IELPAGPLPE GSKDSFAALL EFAEEQLQAD HVFICFPKNR
EDRAALLRTF SFLGFEIVRP GHPLVPKRPD ACFMVYTLER EDPGEED
