OAZ3_RAT
ID OAZ3_RAT Reviewed; 243 AA.
AC A1BPI0; F1LSS2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Ornithine decarboxylase antizyme 3 {ECO:0000250|UniProtKB:Q9R109};
DE Short=AZ3 {ECO:0000250|UniProtKB:Q9R109};
DE Short=ODC-Az 3;
GN Name=Oaz3 {ECO:0000312|RGD:1599278};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=17040916; DOI=10.1074/jbc.m606010200;
RA Fitzgerald C., Sikora C., Lawson V., Dong K., Cheng M., Oko R.,
RA van der Hoorn F.A.;
RT "Mammalian transcription in support of hybrid mRNA and protein synthesis in
RT testis and lung.";
RL J. Biol. Chem. 281:38172-38180(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2), SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), TISSUE
RP SPECIFICITY, AND INTERACTION WITH PPP1R16A.
RX PubMed=21712390; DOI=10.1074/jbc.m111.274647;
RA Ruan Y., Cheng M., Ou Y., Oko R., van der Hoorn F.A.;
RT "Ornithine decarboxylase antizyme Oaz3 modulates protein phosphatase
RT activity.";
RL J. Biol. Chem. 286:29417-29427(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-9 AND SER-12, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Stabilizes AZIN2 by interfering with its
CC ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi
CC intermediate compartment (ERGIC) to the cytosol. Probably plays a key
CC role in spermatogenesis by regulating the intracellular concentration
CC of polyamines in haploid germ cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9R109, ECO:0000250|UniProtKB:Q9UMX2}.
CC -!- FUNCTION: [Isoform 2]: Does not possess antizyme activity. Modulates
CC PPP1CB activity through its interaction with PPP1R16A.
CC {ECO:0000269|PubMed:21712390}.
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 (By
CC similarity). Interacts with GGN (By similarity). Isoform 2 interacts
CC with PPP1R16A; Modulates PPP1CB activity (PubMed:21712390).
CC {ECO:0000250|UniProtKB:P54368, ECO:0000250|UniProtKB:Q9R109,
CC ECO:0000250|UniProtKB:Q9UMX2, ECO:0000269|PubMed:21712390}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000250|UniProtKB:Q9R109}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9R109}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:21712390}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Ribosomal frameshifting; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=A1BPI0-1; Sequence=Displayed;
CC Name=2 {ECO:0000305}; Synonyms=p12 {ECO:0000303|PubMed:21712390};
CC IsoId=A1BPI0-2; Sequence=VSP_056786;
CC -!- TISSUE SPECIFICITY: Testis-specific. Isoform 2 is expressed in outer
CC dense fibers, fibrous sheath and the connecting piece of sperm
CC (PubMed:21712390). {ECO:0000269|PubMed:17040916,
CC ECO:0000269|PubMed:21712390}.
CC -!- MISCELLANEOUS: PubMed:17040916 reports an event of trans-splicing that
CC creates a hybrid 14-kDa protein whose N-terminal 105 amino acids are
CC encoded by the rat Oaz3 gene, located on chromosome 2 and its C-
CC terminal 33 amino acids by a novel gene located on chromosome 4. The
CC nuclear pre-mRNA of Oaz3 gene has 5 adenosine residues whereas the
CC nuclear trans-spliced RNA has 6 adenosine residues suggesting that an
CC unknown nuclear process adds 1 adenosine affecting the reading frame.
CC Moreover the hybrid 14-kDa protein is the result of ribosomal
CC frameshift. The hybrid 14-KDa protein is present in the outer dense
CC fibers and the fibrous sheath and expressed in lung. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by ribosomal frameshifting
CC occurring between the codons for Ser-86 and Glu-87. An autoregulatory
CC mechanism enables modulation of frameshifting according to the cellular
CC concentration of polyamines.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing. This form
CC is not the result of ribosomal frameshift. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ODC antizyme family.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF59049.1; 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; DQ431008; ABF59049.1; ALT_SEQ; mRNA.
DR EMBL; AABR06019264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001094488.1; NM_001101018.1. [A1BPI0-1]
DR AlphaFoldDB; A1BPI0; -.
DR SMR; A1BPI0; -.
DR STRING; 10116.ENSRNOP00000028303; -.
DR iPTMnet; A1BPI0; -.
DR PhosphoSitePlus; A1BPI0; -.
DR PaxDb; A1BPI0; -.
DR GeneID; 689588; -.
DR KEGG; rno:689588; -.
DR UCSC; RGD:1599278; rat.
DR CTD; 51686; -.
DR RGD; 1599278; Oaz3.
DR eggNOG; KOG4387; Eukaryota.
DR OrthoDB; 1403675at2759; -.
DR PhylomeDB; A1BPI0; -.
DR TreeFam; TF314741; -.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR PRO; PR:A1BPI0; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0036126; C:sperm flagellum; IDA:RGD.
DR GO; GO:0071532; F:ankyrin repeat binding; IDA:RGD.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; ISO:RGD.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; ISO:RGD.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:RGD.
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 Alternative splicing; Cell projection; Cilium; Cytoplasm; Flagellum;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..243
FT /note="Ornithine decarboxylase antizyme 3"
FT /id="PRO_0000430516"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 87..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:21712390"
FT /id="VSP_056786"
SQ SEQUENCE 243 AA; 28185 MW; A40CF67D37FCBA2F CRC64;
MPCTRSRPSL YSLSYIKRGK TRNCLYPFWS PYAYYLYCYK YRITLREKML PCCYRSITYK
EQEDLTLRPH CCLPCSCLPY SCLPCSESLE GLQVGRSTAQ EKDHSQLKEL YSAGNLTVLS
ADPLLHQDPV QLDFHFRLTP HSSAHWHGLL CDHQLFLDIP FQALEQGNRE SLTATLEYVE
EKTNVDSVFV NFQSNHKDRG ALLRAFSYMG FEVVRPDHPA LPPWDNVIFM VYPLERDLGQ
PGQ
