ID   OAZ_CANGA               Reviewed;         255 AA.
AC   Q6FJC4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Ornithine decarboxylase antizyme;
GN   Name=OAZ1; OrderedLocusNames=CAGL0M07403g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that
CC       negatively regulates ODC activity and intracellular polyamine
CC       biosynthesis in response to increased intracellular polyamine levels.
CC       Binds to ODC monomers, inhibiting the assembly of the functional ODC
CC       homodimer, and targets the monomers for ubiquitin-independent
CC       proteolytic destruction by the 26S proteasome.
CC       {ECO:0000250|UniProtKB:Q02803}.
CC   -!- SUBUNIT: Interacts with ODC and thereby sterically blocks ODC
CC       homodimerization. {ECO:0000250|UniProtKB:Q02803}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=A ribosomal frameshift occurs between the codons for Ala-63
CC         and Asp-64. An autoregulatory mechanism enables modulation of
CC         frameshifting according to the cellular concentration of polyamines.;
CC       Name=1;
CC         IsoId=Q6FJC4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62646.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_449670.1; XM_449670.1.
DR   AlphaFoldDB; Q6FJC4; -.
DR   STRING; 5478.XP_449670.1; -.
DR   EnsemblFungi; CAG62646; CAG62646; CAGL0M07403g.
DR   GeneID; 2891719; -.
DR   KEGG; cgr:CAGL0M07403g; -.
DR   eggNOG; ENOG502RZPH; Eukaryota.
DR   HOGENOM; CLU_087076_0_0_1; -.
DR   InParanoid; Q6FJC4; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IEA:EnsemblFungi.
DR   GO; GO:2001125; P:negative regulation of translational frameshifting; IEA:EnsemblFungi.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:EnsemblFungi.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002993; ODC_AZ.
DR   Pfam; PF02100; ODC_AZ; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribosomal frameshifting.
FT   CHAIN           1..255
FT                   /note="Ornithine decarboxylase antizyme"
FT                   /id="PRO_0000220867"
SQ   SEQUENCE   255 AA;  29846 MW;  F831C3E13DA9CBD0 CRC64;
     MEKKVSHVID FLSNDEVQRQ LGDPSISGIS FSFDIRTLLK KHSGGNPQFF NYSMRDSFHE
     WCADIELGAN TNELVTELLW DIIYLTEHQF LLPYYHGEHK KFQKKLVKRV GNHLNSLVNN
     SASKPTGSMT VNVRHVWRNV GDRYTLLYLP LYFKELIWCK ANGSIFHVII PHTKEHVIHE
     HKEWLLAILE MAGYWNLSHV RLYLPRDDLT NIQTLLKNLH WIGANLLPNE NRNECNENDD
     ITLSDETYII LECEC