ID   OAZ2_PONAB              Reviewed;         189 AA.
AC   Q5R680;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Ornithine decarboxylase antizyme 2;
DE            Short=AZ2;
DE            Short=ODC-Az 2;
GN   Name=OAZ2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Involved in the translocation of AZIN2
CC       from ER-Golgi intermediate compartment (ERGIC) to the cytosol (By
CC       similarity). {ECO:0000250|UniProtKB:O08608,
CC       ECO:0000250|UniProtKB:O95190}.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:O95190,
CC       ECO:0000250|UniProtKB:P54368}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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=Q5R680-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; CR860615; CAH92736.1; -; mRNA.
DR   RefSeq; NP_001126596.1; NM_001133124.1. [Q5R680-1]
DR   AlphaFoldDB; Q5R680; -.
DR   SMR; Q5R680; -.
DR   STRING; 9601.ENSPPYP00000007433; -.
DR   GeneID; 100173592; -.
DR   KEGG; pon:100173592; -.
DR   CTD; 4947; -.
DR   eggNOG; KOG4387; Eukaryota.
DR   InParanoid; Q5R680; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISS: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   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Polyamine biosynthesis; Reference proteome;
KW   Ribosomal frameshifting.
FT   CHAIN           1..189
FT                   /note="Ornithine decarboxylase antizyme 2"
FT                   /id="PRO_0000250713"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08608"
SQ   SEQUENCE   189 AA;  21011 MW;  66390D87EB30CB8F CRC64;
     MINTQDSSIL PLSNCPQLQC CRHIVPGPLW CSDAPHPLSK IPGGRGGGRD PSLSALIYKD
     EKLTVTQDLP VNDGKPHIVH FQYEVTEVKV SSWDAVLSSQ SLFVEIPDGL LADGSKEGLL
     ALLEFAEEKM KVNYVFICFR KGREDRAPLL KTFSFLGFEI VRPGHPCVPS RPDVMFMVYP
     LDQNLSDED