(data stored in ACNUC8465 zone)

SWISSPROT: OAZ_CANGA

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   10-APR-2019, entry version 58.
DE   RecName: Full=Ornithine decarboxylase antizyme;
GN   Name=OAZ1; OrderedLocusNames=CAGL0M07403g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       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       {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
CC         Ala-63 and Asp-64. An autoregulatory mechanism enables
CC         modulation of frameshifting according to the cellular
CC         concentration of polyamines.;
CC       Name=1;
CC         IsoId=Q6FJC4-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
DR   EMBL; CR380959; CAG62646.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_449670.1; XM_449670.1.
DR   STRING; 5478.XP_449670.1; -.
DR   EnsemblFungi; CAG62646; CAG62646; CAGL0M07403g.
DR   GeneID; 2891719; -.
DR   KEGG; cgr:CAGL0M07403g; -.
DR   EuPathDB; FungiDB:CAGL0M07403g; -.
DR   eggNOG; ENOG410IZ51; Eukaryota.
DR   eggNOG; ENOG4111C3N; LUCA.
DR   HOGENOM; HOG000184836; -.
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;
DR   PRODOM; Q6FJC4.
DR   SWISS-2DPAGE; Q6FJC4.
KW   Complete proteome; Reference proteome; Ribosomal frameshifting.
FT   CHAIN         1    255       Ornithine decarboxylase antizyme.
FT                                /FTId=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
//

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