ID   OAZ_SCHPO               Reviewed;         226 AA.
AC   Q9USQ5; P78878;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Ornithine decarboxylase antizyme;
DE            Short=ODC-Az;
GN   Name=spa1; Synonyms=spa; ORFNames=SPBC577.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=10775274; DOI=10.1093/emboj/19.8.1907;
RA   Ivanov I.P., Matsufuji S., Murakami Y., Gesteland R.F., Atkins J.F.;
RT   "Conservation of polyamine regulation by translational frameshifting from
RT   yeast to mammals.";
RL   EMBO J. 19:1907-1917(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   SIMILARITY TO OAZ.
RX   PubMed=10871270; DOI=10.1093/bioinformatics/16.5.478;
RA   Zhu C., Karplus K., Grate L., Coffino P.;
RT   "A homolog of mammalian antizyme is present in fission yeast
RT   Schizosaccharomyces pombe but not detected in budding yeast Saccharomyces
RT   cerevisiae.";
RL   Bioinformatics 16:478-481(2000).
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 Ser-67
CC         and Glu-68. An autoregulatory mechanism enables modulation of
CC         frameshifting according to the cellular concentration of polyamines.;
CC       Name=1;
CC         IsoId=Q9USQ5-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR   EMBL; AF217277; AAF68268.1; -; mRNA.
DR   EMBL; D89228; BAA13889.1; ALT_SEQ; mRNA.
DR   EMBL; CU329671; CAB54822.2; -; Genomic_DNA.
DR   PIR; T40558; T40558.
DR   PIR; T43062; T43062.
DR   RefSeq; NP_595312.1; NM_001021219.2.
DR   AlphaFoldDB; Q9USQ5; -.
DR   BioGRID; 277398; 13.
DR   STRING; 4896.SPBC577.14c.1; -.
DR   MaxQB; Q9USQ5; -.
DR   PaxDb; Q9USQ5; -.
DR   EnsemblFungi; SPBC577.14c.1; SPBC577.14c.1:pep; SPBC577.14c. [Q9USQ5-1]
DR   GeneID; 2540881; -.
DR   KEGG; spo:SPBC577.14c; -.
DR   PomBase; SPBC577.14c; spa1.
DR   VEuPathDB; FungiDB:SPBC577.14c; -.
DR   eggNOG; KOG4387; Eukaryota.
DR   HOGENOM; CLU_1225409_0_0_1; -.
DR   OMA; PRWISDS; -.
DR   Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR   PRO; PR:Q9USQ5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0006591; P:ornithine metabolic process; IC:PomBase.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010967; P:regulation of polyamine biosynthetic process; TAS:PomBase.
DR   Gene3D; 3.40.630.60; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002993; ODC_AZ.
DR   InterPro; IPR038581; ODC_AZ_sf.
DR   PANTHER; PTHR10279; PTHR10279; 1.
DR   Pfam; PF02100; ODC_AZ; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Ribosomal frameshifting.
FT   CHAIN           1..226
FT                   /note="Ornithine decarboxylase antizyme"
FT                   /id="PRO_0000220870"
FT   CONFLICT        100
FT                   /note="P -> A (in Ref. 1; BAA13889)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25873 MW;  A66743BD94A19ACD CRC64;
     MAFRNRMYQL SNVDDADADI LNSHFAPNPR GQNHTHGRRR NTLALCTTKD QMFVYGSTPA
     GGAEWCSEAL ERSRPRAAFK QQRRRHVPRW ISDSFRTCLP KPSGILKEQT VNEEEGNSRH
     RGKYDCDERI GVAESMNYWH GIVRTEEDGS KTLFLIPESW EDVHLKEGLV AIIDLAVDRL
     HCSKLVLFVD KNNSSLPYLV KSLHWVGFEP LPHLNCSDHA LFGMEL