OAZ1_RAT
ID OAZ1_RAT Reviewed; 227 AA.
AC P54370;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Ornithine decarboxylase antizyme 1;
DE Short=ODC-Az;
GN Name=Oaz1; Synonyms=Oaz;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12; 35-45 AND 66-78.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7813017; DOI=10.1016/0092-8674(95)90450-6;
RA Matsufuji S., Matsufuji T., Miyazaki Y., Murakami Y., Atkins J.F.,
RA Gesteland R.F., Hayashi S.;
RT "Autoregulatory frameshifting in decoding mammalian ornithine decarboxylase
RT antizyme.";
RL Cell 80:51-60(1995).
RN [2]
RP FUNCTION IN INHIBITION OF POLYAMINE UPTAKE.
RX PubMed=8166639; DOI=10.1042/bj2990019;
RA Mitchell J.L., Judd G.G., Bareyal-Leyser A., Ling S.Y.;
RT "Feedback repression of polyamine transport is mediated by antizyme in
RT mammalian tissue-culture cells.";
RL Biochem. J. 299:19-22(1994).
RN [3]
RP STRUCTURE BY NMR OF 94-218.
RX PubMed=16128579; DOI=10.1021/bi051081k;
RA Hoffman D.W., Carroll D., Martinez N., Hackert M.L.;
RT "Solution structure of a conserved domain of antizyme: a protein regulator
RT of polyamines.";
RL Biochemistry 44:11777-11785(2005).
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. Triggers ODC
CC degradation by inducing the exposure of a cryptic proteasome-
CC interacting surface of ODC. Stabilizes AZIN2 by interfering with its
CC ubiquitination (By similarity). Also inhibits cellular uptake of
CC polyamines by inactivating the polyamine uptake transporter
CC (PubMed:8166639). SMAD1/OAZ1/PSMB4 complex mediates the degradation of
CC the CREBBP/EP300 repressor SNIP1. Involved in the translocation of
CC AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (By
CC similarity). {ECO:0000250|UniProtKB:P54368,
CC ECO:0000269|PubMed:8166639}.
CC -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC homodimerization. Forms a ternary complex with PSMB4 and OAZ1 before
CC PSMB4 is incorporated into the 20S proteasome. Interacts with AZIN2;
CC this interaction disrupts the interaction between the antizyme and
CC ODC1. Interacts with FAM171A1 (By similarity).
CC {ECO:0000250|UniProtKB:P54368}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-68
CC and Asp-69. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.
CC {ECO:0000269|PubMed:7813017};
CC Name=1;
CC IsoId=P54370-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by a ribosomal frameshifting mechanism in response
CC to increased levels of intracellular polyamines.
CC {ECO:0000269|PubMed:7813017}.
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR EMBL; D10706; BAA01549.1; -; mRNA.
DR EMBL; D10706; BAA01550.1; -; mRNA.
DR EMBL; D10706; BAA01551.1; -; mRNA.
DR PIR; A55472; A55472.
DR RefSeq; NP_620781.1; NM_139081.2. [P54370-1]
DR PDB; 1ZO0; NMR; -; A=94-219.
DR PDBsum; 1ZO0; -.
DR AlphaFoldDB; P54370; -.
DR SMR; P54370; -.
DR BioGRID; 247534; 1.
DR STRING; 10116.ENSRNOP00000026341; -.
DR PaxDb; P54370; -.
DR GeneID; 25502; -.
DR KEGG; rno:25502; -.
DR UCSC; RGD:3219; rat. [P54370-1]
DR CTD; 4946; -.
DR RGD; 3219; Oaz1.
DR eggNOG; KOG4387; Eukaryota.
DR InParanoid; P54370; -.
DR OrthoDB; 1403675at2759; -.
DR PhylomeDB; P54370; -.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR EvolutionaryTrace; P54370; -.
DR PRO; PR:P54370; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; ISO:RGD.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.630.60; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029914; ODC-AZ_1.
DR InterPro; IPR002993; ODC_AZ.
DR InterPro; IPR038581; ODC_AZ_sf.
DR PANTHER; PTHR10279; PTHR10279; 1.
DR PANTHER; PTHR10279:SF8; PTHR10279:SF8; 1.
DR Pfam; PF02100; ODC_AZ; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS01337; ODC_AZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Polyamine biosynthesis;
KW Reference proteome; Ribosomal frameshifting; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7813017"
FT CHAIN 2..227
FT /note="Ornithine decarboxylase antizyme 1"
FT /id="PRO_0000220852"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1ZO0"
FT HELIX 154..167
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1ZO0"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:1ZO0"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1ZO0"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1ZO0"
SQ SEQUENCE 227 AA; 25228 MW; EA28FC118ACF41D6 CRC64;
MVKSSLQRIL NSHCFAREKE GDKRSATLHA SRTMPLLSQH SRGGCSSESS RVALHCCSNL
GPGPRWCSDV PHPPLKIPGG RGNSQRDHSL SASILYSDER LNVTEEPTSN DKTRVLSIQC
TLTEAKQVTW RAVWNGGGLY IELPAGPLPE GSKDSFAALL EFAEEQLRAD HVFICFPKNR
EDRAALLRTF SFLGFEIVRP GHPLVPKRPD ACFMVYTLER EDPGEED
