OAZ_CAEEL
ID OAZ_CAEEL Reviewed; 159 AA.
AC Q9NHZ6; A8WIR2; O44900;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ornithine decarboxylase antizyme;
DE Short=ODC-Az;
GN Name=oaz-1 {ECO:0000312|WormBase:ZK484.1a};
GN ORFNames=ZK484.1 {ECO:0000312|WormBase:ZK484.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND RIBOSOMAL FRAMESHIFTING.
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 GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 homodimer, and targets the monomers for ubiquitin-
CC independent proteolytic destruction by the 26S proteasome.
CC {ECO:0000250|UniProtKB:P54368}.
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=2;
CC Comment=A ribosomal frameshift occurs between the codons for Phe-42
CC and Asp-43. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.
CC {ECO:0000269|PubMed:10775274};
CC Name=a {ECO:0000312|WormBase:ZK484.1a};
CC IsoId=Q9NHZ6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:ZK484.1b};
CC IsoId=Q9NHZ6-2; Sequence=VSP_032960;
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR EMBL; AF217278; AAF68269.1; -; mRNA.
DR EMBL; FO080687; CCD65806.1; -; Genomic_DNA.
DR EMBL; FO080687; CCD65807.1; -; Genomic_DNA.
DR PIR; T32868; T32868.
DR RefSeq; NP_001122567.1; NM_001129095.1.
DR RefSeq; NP_001122568.1; NM_001129096.2.
DR AlphaFoldDB; Q9NHZ6; -.
DR SMR; Q9NHZ6; -.
DR BioGRID; 37744; 5.
DR IntAct; Q9NHZ6; 1.
DR STRING; 6239.ZK484.1a; -.
DR EPD; Q9NHZ6; -.
DR PaxDb; Q9NHZ6; -.
DR PeptideAtlas; Q9NHZ6; -.
DR EnsemblMetazoa; ZK484.1a.1; ZK484.1a.1; WBGene00022748. [Q9NHZ6-1]
DR EnsemblMetazoa; ZK484.1b.1; ZK484.1b.1; WBGene00022748. [Q9NHZ6-2]
DR UCSC; ZK484.1b.2; c. elegans. [Q9NHZ6-1]
DR WormBase; ZK484.1a; CE41745; WBGene00022748; oaz-1. [Q9NHZ6-1]
DR WormBase; ZK484.1b; CE41746; WBGene00022748; oaz-1. [Q9NHZ6-2]
DR eggNOG; KOG4387; Eukaryota.
DR HOGENOM; CLU_146905_0_0_1; -.
DR InParanoid; Q9NHZ6; -.
DR OMA; SSDWCCH; -.
DR OrthoDB; 1621739at2759; -.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR PRO; PR:Q9NHZ6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022748; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
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: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; 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.
DR PROSITE; PS01337; ODC_AZ; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..159
FT /note="Ornithine decarboxylase antizyme"
FT /id="PRO_0000220861"
FT VAR_SEQ 43..159
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_032960"
SQ SEQUENCE 159 AA; 17710 MW; 984ECC2A0C40DAD0 CRC64;
MSSILSSNFT NKSNQLVNES AVDSSLTASP CSTQPGDVGW CFDAPHGVLT KLPNETRAIV
SAVSPNWRVT SIGEKTLAIM IPHDQPVLGI SKKNFVDLLE FAEDKLEMER VLAVFEKARI
NPTEGFPRTL RYVGFRPYAI DEHPVHLPAE KYFIMSYKV
