OAZ_DROME
ID OAZ_DROME Reviewed; 254 AA.
AC P54361; O44436;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ornithine decarboxylase antizyme;
DE Short=ODC-Az;
DE AltName: Full=Protein gutfeeling;
GN Name=Oda; Synonyms=guf; ORFNames=CG16747;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=8878684; DOI=10.1093/genetics/144.1.183;
RA Salzberg A., Golden K., Bodmer R., Bellen H.J.;
RT "Gutfeeling, a Drosophila gene encoding an antizyme-like protein, is
RT required for late differentiation of neurons and muscles.";
RL Genetics 144:183-196(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9488472; DOI=10.1128/mcb.18.3.1553;
RA Ivanov I.P., Simin K., Letsou A., Atkins J.F., Gesteland R.F.;
RT "The Drosophila gene for antizyme requires ribosomal frameshifting for
RT expression and contains an intronic gene for snRNP Sm D3 on the opposite
RT strand.";
RL Mol. Cell. Biol. 18:1553-1561(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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 (By
CC similarity). Required for cellular differentiation in neuronal and
CC myogenic lineages during embryonic development (PubMed:8878684).
CC {ECO:0000250|UniProtKB:P54368, ECO:0000269|PubMed:8878684}.
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=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-61
CC and Asp-62. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=P54361-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Expressed in all stages of embryonic and larval
CC development as well as in pupae and adults.
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR EMBL; U29529; AAB49330.1; ALT_SEQ; mRNA.
DR EMBL; AF038597; AAC97538.1; -; mRNA.
DR EMBL; AE013599; AAF58569.2; -; Genomic_DNA.
DR PIR; S72228; S72228.
DR RefSeq; NP_725103.1; NM_165863.3. [P54361-1]
DR AlphaFoldDB; P54361; -.
DR SMR; P54361; -.
DR BioGRID; 62088; 53.
DR IntAct; P54361; 4.
DR STRING; 7227.FBpp0087122; -.
DR PaxDb; P54361; -.
DR PRIDE; P54361; -.
DR EnsemblMetazoa; FBtr0088013; FBpp0087121; FBgn0014184. [P54361-1]
DR GeneID; 36307; -.
DR KEGG; dme:Dmel_CG16747; -.
DR CTD; 36307; -.
DR FlyBase; FBgn0014184; Oda.
DR VEuPathDB; VectorBase:FBgn0014184; -.
DR eggNOG; KOG4387; Eukaryota.
DR InParanoid; P54361; -.
DR PhylomeDB; P54361; -.
DR Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC).
DR SignaLink; P54361; -.
DR BioGRID-ORCS; 36307; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Oda; fly.
DR GenomeRNAi; 36307; -.
DR PRO; PR:P54361; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0014184; Expressed in adult Malpighian tubule (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P54361; baseline and differential.
DR Genevisible; P54361; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; ISS:FlyBase.
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 Developmental protein; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..254
FT /note="Ornithine decarboxylase antizyme"
FT /id="PRO_0000220862"
SQ SEQUENCE 254 AA; 28283 MW; 22A73822A2C50D59 CRC64;
MPSNMNNKLD PVFSSGFVRR EFNDSGIADG KLRTISTSSC ATTMSSESYR ISLGVGPLWW
SDVPVHHRTD HDRASLLTGY SRKSSVDSAG GSLYEASSRA SSLSSSQSDC SDLESQPDIH
SLCSDDDCQE VLRQILQHDQ PVQITIKLHV TEDQYTNWNT ILNPVNNLLY VALPKDLPPA
GSKQTFISLL EFAEEKLEVD GIVMVMPKDQ PDRARLIEAF LFMGFEPLSR KAPQAPPAAI
NDNENYYFLY SIEE
