OAZ3_MOUSE
ID OAZ3_MOUSE Reviewed; 243 AA.
AC Q9R109; Q9WVT4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ornithine decarboxylase antizyme 3;
DE Short=AZ3;
DE Short=ODC-Az 3;
DE AltName: Full=OAZ-t;
GN Name=Oaz3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10781085; DOI=10.1073/pnas.070055897;
RA Ivanov I.P., Rohrwasser A., Terreros D.A., Gesteland R.F., Atkins J.F.;
RT "Discovery of a spermatogenesis stage-specific ornithine decarboxylase
RT antizyme: antizyme 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4808-4813(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=10792465; DOI=10.1046/j.1365-2443.2000.00324.x;
RA Tosaka Y., Tanaka H., Yano Y., Masai K., Nozaki M., Yomogida K., Otani S.,
RA Nojima H., Nishimune Y.;
RT "Identification and characterization of testis specific ornithine
RT decarboxylase antizyme (OAZ-t) gene: expression in haploid germ cells and
RT polyamine-induced frameshifting.";
RL Genes Cells 5:265-276(2000).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GGN.
RX PubMed=15642376; DOI=10.1016/j.febslet.2004.10.112;
RA Zhang J., Wang Y., Zhou Y., Cao Z., Huang P., Lu B.;
RT "Yeast two-hybrid screens imply that GGNBP1, GGNBP2 and OAZ3 are potential
RT interaction partners of testicular germ cell-specific protein GGN1.";
RL FEBS Lett. 579:559-566(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH AZIN2.
RX PubMed=16916800; DOI=10.1074/jbc.m602840200;
RA Lopez-Contreras A.J., Lopez-Garcia C., Jimenez-Cervantes C., Cremades A.,
RA Penafiel R.;
RT "Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor
RT devoid of ornithine and arginine decarboxylating activity.";
RL J. Biol. Chem. 281:30896-30906(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH AZIN2.
RX PubMed=18062773; DOI=10.1042/bj20071423;
RA Snapir Z., Keren-Paz A., Bercovich Z., Kahana C.;
RT "ODCp, a brain- and testis-specific ornithine decarboxylase paralogue,
RT functions as an antizyme inhibitor, although less efficiently than AzI1.";
RL Biochem. J. 410:613-619(2008).
RN [6]
RP FUNCTION.
RX PubMed=18508777; DOI=10.1074/jbc.m801024200;
RA Lopez-Contreras A.J., Ramos-Molina B., Cremades A., Penafiel R.;
RT "Antizyme inhibitor 2 (AZIN2/ODCp) stimulates polyamine uptake in mammalian
RT cells.";
RL J. Biol. Chem. 283:20761-20769(2008).
RN [7]
RP FUNCTION, INTERACTION WITH AZIN2, AND TISSUE SPECIFICITY.
RX PubMed=18973822; DOI=10.1016/j.biocel.2008.09.029;
RA Lopez-Contreras A.J., Ramos-Molina B., Martinez-de-la-Torre M.,
RA Penafiel-Verdu C., Puelles L., Cremades A., Penafiel R.;
RT "Expression of antizyme inhibitor 2 in male haploid germinal cells suggests
RT a role in spermiogenesis.";
RL Int. J. Biochem. Cell Biol. 41:1070-1078(2009).
RN [8]
RP FUNCTION.
RX PubMed=19449338; DOI=10.1002/jcb.22168;
RA Lopez-Contreras A.J., Sanchez-Laorden B.L., Ramos-Molina B.,
RA de la Morena M.E., Cremades A., Penafiel R.;
RT "Subcellular localization of antizyme inhibitor 2 in mammalian cells:
RT Influence of intrinsic sequences and interaction with antizymes.";
RL J. Cell. Biochem. 107:732-740(2009).
RN [9]
RP FUNCTION.
RX PubMed=24967154; DOI=10.1016/j.fob.2014.05.004;
RA Ramos-Molina B., Lambertos A., Lopez-Contreras A.J., Kasprzak J.M.,
RA Czerwoniec A., Bujnicki J.M., Cremades A., Penafiel R.;
RT "Structural and degradative aspects of ornithine decarboxylase antizyme
RT inhibitor 2.";
RL FEBS Open Bio 4:510-521(2014).
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 homodimers. Does not target the ODC monomers for
CC degradation, which allows a protein synthesis-independent restoration
CC of ODC activity (PubMed:16916800, PubMed:18508777, PubMed:18973822).
CC Stabilizes AZIN2 by interfering with its ubiquitination
CC (PubMed:18062773). Involved in the translocation of AZNI2 from ER-Golgi
CC intermediate compartment (ERGIC) to the cytosol (PubMed:19449338).
CC Probably plays a key role in spermatogenesis by regulating the
CC intracellular concentration of polyamines in haploid germ cells
CC (PubMed:24967154). {ECO:0000269|PubMed:16916800,
CC ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18508777,
CC ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:19449338,
CC ECO:0000269|PubMed:24967154}.
CC -!- SUBUNIT: Interacts with ODC1 and thereby sterically blocks ODC
CC homodimerization (By similarity). Interacts with AZIN2; this
CC interaction disrupts the interaction between the antizyme and ODC1
CC (PubMed:16916800, PubMed:18062773, PubMed:18973822). Interacts with GGN
CC (PubMed:15642376). {ECO:0000250|UniProtKB:P54368,
CC ECO:0000269|PubMed:15642376, ECO:0000269|PubMed:16916800,
CC ECO:0000269|PubMed:18062773, ECO:0000269|PubMed:18973822}.
CC -!- INTERACTION:
CC Q9R109; Q8BVM4: Azin2; NbExp=2; IntAct=EBI-4370103, EBI-9656869;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642376}. Cytoplasm
CC {ECO:0000269|PubMed:15642376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-86
CC and Glu-87. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=Q9R109-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Testis specific. Expressed throughout the
CC differentiation process from spermatids to spermatozoa in the inner
CC part of the seminiferous tubules. {ECO:0000269|PubMed:18973822}.
CC -!- DEVELOPMENTAL STAGE: Expression starts early in spermiogenesis and
CC finishes in the late spermatid phase.
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD51735.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD51735.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=BAA81913.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA81913.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA81913.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AF175297; AAD51735.1; ALT_SEQ; mRNA.
DR EMBL; AB016275; BAA81913.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS84654.1; -. [Q9R109-1]
DR RefSeq; NP_058597.2; NM_016901.3. [Q9R109-1]
DR AlphaFoldDB; Q9R109; -.
DR SMR; Q9R109; -.
DR BioGRID; 207485; 1.
DR IntAct; Q9R109; 2.
DR MINT; Q9R109; -.
DR STRING; 10090.ENSMUSP00000139408; -.
DR iPTMnet; Q9R109; -.
DR PhosphoSitePlus; Q9R109; -.
DR PaxDb; Q9R109; -.
DR PRIDE; Q9R109; -.
DR ProteomicsDB; 294264; -. [Q9R109-1]
DR Antibodypedia; 34072; 90 antibodies from 20 providers.
DR DNASU; 53814; -.
DR Ensembl; ENSMUST00000199678; ENSMUSP00000143080; ENSMUSG00000028141. [Q9R109-1]
DR GeneID; 53814; -.
DR KEGG; mmu:53814; -.
DR UCSC; uc008qgh.3; mouse. [Q9R109-1]
DR CTD; 51686; -.
DR MGI; MGI:1858170; Oaz3.
DR VEuPathDB; HostDB:ENSMUSG00000028141; -.
DR eggNOG; KOG4387; Eukaryota.
DR GeneTree; ENSGT00940000161581; -.
DR InParanoid; Q9R109; -.
DR OMA; SITCKEQ; -.
DR OrthoDB; 1403675at2759; -.
DR TreeFam; TF314741; -.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR BioGRID-ORCS; 53814; 4 hits in 22 CRISPR screens.
DR ChiTaRS; Oaz3; mouse.
DR PRO; PR:Q9R109; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R109; protein.
DR Bgee; ENSMUSG00000028141; Expressed in seminiferous tubule of testis and 94 other tissues.
DR ExpressionAtlas; Q9R109; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR GO; GO:0071532; F:ankyrin repeat binding; ISO:MGI.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:UniProtKB.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:InterPro.
DR Gene3D; 3.40.630.60; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029913; ODC-AZ_3.
DR InterPro; IPR002993; ODC_AZ.
DR InterPro; IPR038581; ODC_AZ_sf.
DR PANTHER; PTHR10279; PTHR10279; 1.
DR PANTHER; PTHR10279:SF9; PTHR10279:SF9; 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 Cytoplasm; Nucleus; Phosphoprotein; Polyamine biosynthesis;
KW Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..243
FT /note="Ornithine decarboxylase antizyme 3"
FT /id="PRO_0000220860"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1BPI0"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1BPI0"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1BPI0"
SQ SEQUENCE 243 AA; 28228 MW; 146EAE4F9C465FD6 CRC64;
MPCNRSRPSL YSLSYIKRGK TRNYLYPFWS PFAYYLYCYK YRITLREKML PCCYKSITYK
EQEDLTLRPH CCLPCSCLPC SCLQCSESLG GLQVGRSTAQ EKDHSQLKEL YSAGNLTVLS
TDPLLHQDPV QLDFHFRLTP HSSAHWHGLL CDHRLFLDIP YQALDQGNRE SLTATLEYVE
EKTNVDSVFV NFQIDRKDRG ALLRAFSYMG FEVVRPDHPA LPPWDNVIFM VYPLERDLGH
PGQ
