ID   OAZ2_MOUSE              Reviewed;         189 AA.
AC   O08608;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Ornithine decarboxylase antizyme 2;
DE            Short=AZ2;
DE            Short=ODC-Az 2;
DE   AltName: Full=Seizure-related protein 15;
GN   Name=Oaz2; Synonyms=Sez15;
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 [MRNA].
RX   PubMed=9782076; DOI=10.1006/geno.1998.5434;
RA   Ivanov I.P., Gesteland R.F., Atkins J.F.;
RT   "A second mammalian antizyme: conservation of programmed ribosomal
RT   frameshifting.";
RL   Genomics 52:119-129(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-189.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
RA   Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA   Sugaya E.;
RT   "Molecular characterization of seizure-related genes isolated by
RT   differential screening.";
RL   Biochem. Biophys. Res. Commun. 219:795-799(1996).
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.
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   [5]
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   [6]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-186.
RX   PubMed=19725046; DOI=10.1002/jcb.22334;
RA   Murai N., Shimizu A., Murakami Y., Matsufuji S.;
RT   "Subcellular localization and phosphorylation of antizyme 2.";
RL   J. Cell. Biochem. 108:1012-1021(2009).
RN   [7]
RP   FUNCTION.
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 homodimers. Does not target the ODC monomers for
CC       degradation, which allows a protein synthesis-independent restoration
CC       of ODC activity (PubMed:16916800, PubMed:18508777, PubMed:24967154).
CC       Involved in the translocation of AZIN2 from ER-Golgi intermediate
CC       compartment (ERGIC) to the cytosol (PubMed:19449338).
CC       {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18508777,
CC       ECO:0000269|PubMed:19449338, ECO:0000269|PubMed:24967154}.
CC   -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC       homodimerization (By similarity). Interacts with AZIN2; this
CC       interaction disrupts the interaction between the antizyme and ODC1
CC       (PubMed:16916800). {ECO:0000250|UniProtKB:P54368,
CC       ECO:0000269|PubMed:16916800}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19725046}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=A ribosomal frameshift occurs between the codons for Ser-32
CC         and Asp-33. An autoregulatory mechanism enables modulation of
CC         frameshifting according to the cellular concentration of polyamines.;
CC       Name=1;
CC         IsoId=O08608-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; AF057298; AAD03266.1; -; mRNA.
DR   EMBL; D78643; BAA19569.1; -; mRNA.
DR   CCDS; CCDS57683.1; -. [O08608-1]
DR   RefSeq; NP_035082.1; NM_010952.3. [O08608-1]
DR   AlphaFoldDB; O08608; -.
DR   SMR; O08608; -.
DR   IntAct; O08608; 1.
DR   STRING; 10090.ENSMUSP00000136914; -.
DR   iPTMnet; O08608; -.
DR   PhosphoSitePlus; O08608; -.
DR   MaxQB; O08608; -.
DR   PaxDb; O08608; -.
DR   PRIDE; O08608; -.
DR   ProteomicsDB; 287879; -. [O08608-1]
DR   Antibodypedia; 42839; 91 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000153700; ENSMUSP00000136914; ENSMUSG00000040652. [O08608-1]
DR   GeneID; 18247; -.
DR   KEGG; mmu:18247; -.
DR   UCSC; uc009qdu.2; mouse. [O08608-1]
DR   CTD; 4947; -.
DR   MGI; MGI:109492; Oaz2.
DR   VEuPathDB; HostDB:ENSMUSG00000040652; -.
DR   eggNOG; KOG4387; Eukaryota.
DR   GeneTree; ENSGT00940000157725; -.
DR   InParanoid; O08608; -.
DR   OMA; IVHFRYE; -.
DR   OrthoDB; 1403675at2759; -.
DR   PhylomeDB; O08608; -.
DR   TreeFam; TF314741; -.
DR   Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR   BioGRID-ORCS; 18247; 0 hits in 57 CRISPR screens.
DR   ChiTaRS; Oaz2; mouse.
DR   PRO; PR:O08608; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O08608; protein.
DR   Bgee; ENSMUSG00000040652; Expressed in lung and 60 other tissues.
DR   ExpressionAtlas; O08608; baseline and differential.
DR   Genevisible; O08608; 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:0008073; F:ornithine decarboxylase inhibitor activity; IGI: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; IPR029916; ODC-AZ_2.
DR   InterPro; IPR002993; ODC_AZ.
DR   InterPro; IPR038581; ODC_AZ_sf.
DR   PANTHER; PTHR10279; PTHR10279; 1.
DR   PANTHER; PTHR10279:SF6; PTHR10279:SF6; 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   Nucleus; Phosphoprotein; Polyamine biosynthesis; Reference proteome;
KW   Ribosomal frameshifting.
FT   CHAIN           1..189
FT                   /note="Ornithine decarboxylase antizyme 2"
FT                   /id="PRO_0000220858"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:19725046"
SQ   SEQUENCE   189 AA;  21025 MW;  7B8C08843686163B CRC64;
     MINTQDSSIL PLSKCPQLQC CRHIVPGPLW CSDAPHPLSK IPGGRGGGRD PSLSALIYKD
     EKLTVTQDLP VNDGKPHIVH FQYEVTEVKV SSWDAVLSSQ SLFVEIPDGL LADGSKEGLL
     ALLEFAEEKM KVNYVFICFR KGREDRAPLL KTFSFLGFEI VRPGHPCVPS RPDVMFMVYP
     LDQNLSDED