ID   OAZ_YEAST               Reviewed;         292 AA.
AC   Q02803; D6W3W2;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Ornithine decarboxylase antizyme;
DE            Short=ODC-Az;
GN   Name=OAZ1; OrderedLocusNames=YPL052W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   RIBOSOMAL FRAMESHIFT, FUNCTION, AND INTERACTION WITH SPE1.
RX   PubMed=15538383; DOI=10.1038/sj.emboj.7600473;
RA   Palanimurugan R., Scheel H., Hofmann K., Dohmen R.J.;
RT   "Polyamines regulate their synthesis by inducing expression and blocking
RT   degradation of ODC antizyme.";
RL   EMBO J. 23:4857-4867(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=18089576; DOI=10.1074/jbc.m708088200;
RA   Porat Z., Landau G., Bercovich Z., Krutauz D., Glickman M., Kahana C.;
RT   "Yeast antizyme mediates degradation of yeast ornithine decarboxylase by
RT   yeast but not by mammalian proteasome: new insights on yeast antizyme.";
RL   J. Biol. Chem. 283:4528-4534(2008).
RN   [6]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=21900894; DOI=10.1038/nature10393;
RA   Kurian L., Palanimurugan R., Goedderz D., Dohmen R.J.;
RT   "Polyamine sensing by nascent ornithine decarboxylase antizyme stimulates
RT   decoding of its mRNA.";
RL   Nature 477:490-494(2011).
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       (PubMed:15538383). Binds to ODC/SPE1 monomers, inhibiting the assembly
CC       of the functional ODC homodimer, and targets the monomers for
CC       ubiquitin-independent proteolytic destruction by the 26S proteasome
CC       (PubMed:18089576). {ECO:0000269|PubMed:15538383,
CC       ECO:0000269|PubMed:18089576}.
CC   -!- SUBUNIT: Interacts with ODC/SPE1 and thereby sterically blocks ODC
CC       homodimerization. {ECO:0000269|PubMed:15538383}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=1;
CC         Comment=A ribosomal frameshift occurs between the codons for Ala-69
CC         and Asp-70. An autoregulatory mechanism enables modulation of
CC         frameshifting according to the cellular concentration of polyamines.
CC         {ECO:0000269|PubMed:15538383, ECO:0000269|PubMed:21900894};
CC       Name=1;
CC         IsoId=Q02803-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; U39205; AAB68313.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY558331; AAS56657.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006949; DAA11378.1; -; Genomic_DNA.
DR   PIR; S61090; S61090.
DR   RefSeq; NP_015273.2; NM_001183866.4. [Q02803-1]
DR   AlphaFoldDB; Q02803; -.
DR   BioGRID; 36128; 49.
DR   DIP; DIP-5057N; -.
DR   STRING; 4932.YPL052W; -.
DR   iPTMnet; Q02803; -.
DR   MaxQB; Q02803; -.
DR   PaxDb; Q02803; -.
DR   PRIDE; Q02803; -.
DR   EnsemblFungi; YPL052W_mRNA; YPL052W; YPL052W. [Q02803-1]
DR   GeneID; 856055; -.
DR   KEGG; sce:YPL052W; -.
DR   SGD; S000005973; OAZ1.
DR   VEuPathDB; FungiDB:YPL052W; -.
DR   eggNOG; ENOG502RZPH; Eukaryota.
DR   HOGENOM; CLU_087076_0_0_1; -.
DR   InParanoid; Q02803; -.
DR   OMA; NLHWIGA; -.
DR   BioCyc; YEAST:G3O-33965-MON; -.
DR   PRO; PR:Q02803; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02803; protein.
DR   GO; GO:0005737; C:cytoplasm; IC:SGD.
DR   GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:SGD.
DR   GO; GO:2001125; P:negative regulation of translational frameshifting; IMP:SGD.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:SGD.
PE   1: Evidence at protein level;
KW   Reference proteome; Ribosomal frameshifting.
FT   CHAIN           1..292
FT                   /note="Ornithine decarboxylase antizyme"
FT                   /id="PRO_0000220871"
SQ   SEQUENCE   292 AA;  34045 MW;  4B596F4EDEC5EE71 CRC64;
     MYEVIQKRKT KIINVLQSPE LMRLIEDPSN LGISLHFPVS SLLKSNKCTP MPKLSTYSLA
     SGGFKDWCAD IPLDVPPEID IIDFYWDVIL CMESQFILDY NVPSKNKGNN QKSVAKLLKN
     KLVNDMKTTL KRLIYNENTK QYKNNNSHDG YNWRKLGSQY FILYLPLFTQ ELIWCKLNEN
     YFHVVLPSLL NSRNVHDNHS TYINKDWLLA LLELTSNLNQ NFKFEYMKLR LYILRDDLIN
     NGLDLLKNLN WVGGKLIKNE DREVLLNSTD LATDSISHLL GDENFVILEF EC