ID   OAZ2_DANRE              Reviewed;         218 AA.
AC   Q9YI97; Q6PGU0; Q9IBH4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ornithine decarboxylase antizyme 2;
DE   AltName: Full=ODC antizyme, long form;
DE            Short=ODC-Az-L;
GN   Name=oaz1b; Synonyms=oaz2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], RIBOSOMAL FRAMESHIFT, FUNCTION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=10600644; DOI=10.1042/bj3450099;
RA   Saito T., Hascilowicz T., Ohkido I., Kikuchi Y., Okamoto H., Hayashi S.,
RA   Murakami Y., Matsufuji S.;
RT   "Two zebrafish (Danio rerio) antizymes with different expression and
RT   activities.";
RL   Biochem. J. 345:99-106(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) 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. {ECO:0000269|PubMed:10600644}.
CC   -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC       homodimerization. {ECO:0000250|UniProtKB:P54368}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=A ribosomal frameshift occurs between the codons for Ser-60
CC         and Asp-61. An autoregulatory mechanism enables modulation of
CC         frameshifting according to the cellular concentration of polyamines.
CC         {ECO:0000269|PubMed:10600644};
CC       Name=1;
CC         IsoId=Q9YI97-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in 24 hours embryos, with
CC       highest levels in telencephalon, lens, retina, cerebellum and hindbrain
CC       primordia. {ECO:0000269|PubMed:10600644}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in both embryos and adults.
CC       {ECO:0000269|PubMed:10600644}.
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; AB017118; BAA74771.1; -; mRNA.
DR   EMBL; AB017118; BAA74772.1; ALT_SEQ; mRNA.
DR   EMBL; BC056833; AAH56833.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_919413.2; NM_194432.3.
DR   AlphaFoldDB; Q9YI97; -.
DR   SMR; Q9YI97; -.
DR   GeneID; 259193; -.
DR   KEGG; dre:259193; -.
DR   CTD; 259193; -.
DR   ZFIN; ZDB-GENE-020731-5; oaz1b.
DR   InParanoid; Q9YI97; -.
DR   OrthoDB; 1403675at2759; -.
DR   PhylomeDB; Q9YI97; -.
DR   PRO; PR:Q9YI97; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; IBA:GO_Central.
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; IBA:GO_Central.
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:SF11; PTHR10279:SF11; 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   Polyamine biosynthesis; Reference proteome; Ribosomal frameshifting.
FT   CHAIN           1..218
FT                   /note="Ornithine decarboxylase antizyme 2"
FT                   /id="PRO_0000220855"
FT   CONFLICT        44
FT                   /note="P -> L (in Ref. 2; AAH56833)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  24245 MW;  A5BF83E381AC402A CRC64;
     MVKSNLQRIL NSHCFAREKE GKKQCESSIM EALSSSITDR MASPTVCCSS TTGPGPLWCS
     DAPHPPLKIP GGRGNGARDH PSTTQTLYSD RKLTVTEEPA GPGRPQILHF QSRPAAARLI
     QWEAVLRGDG LFVEIPCEPF PDGSKESFIS LLEFAEEHLK VVSVFVCFYK NREDRVKLVR
     TFSFLGFEMV KPGHALVPAR PDVLFMAYNF DRDSSDED