OAZ3_HUMAN
ID OAZ3_HUMAN Reviewed; 235 AA.
AC Q9UMX2; E7EUE7; Q6GMR0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Ornithine decarboxylase antizyme 3;
DE Short=AZ3;
DE Short=ODC-Az 3;
GN Name=OAZ3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH AZIN2.
RX PubMed=17900240; DOI=10.1042/bj20071004;
RA Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.;
RT "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor
RT but not an arginine decarboxylase.";
RL Biochem. J. 409:187-192(2008).
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:17900240). Stabilizes AZIN2 by interfering with
CC its ubiquitination. Involved in the translocation of AZNI2 from ER-
CC Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a
CC key role in spermatogenesis by regulating the intracellular
CC concentration of polyamines in haploid germ cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9R109, ECO:0000269|PubMed:17900240}.
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:17900240). Interacts with GGN (By similarity).
CC {ECO:0000250|UniProtKB:P54368, ECO:0000250|UniProtKB:Q9R109,
CC ECO:0000269|PubMed:17900240}.
CC -!- INTERACTION:
CC Q9UMX2; O14977: AZIN1; NbExp=5; IntAct=EBI-10281601, EBI-1054824;
CC Q9UMX2; Q96A70: AZIN2; NbExp=5; IntAct=EBI-10281601, EBI-10281609;
CC Q9UMX2; Q9H2G9: BLZF1; NbExp=4; IntAct=EBI-10281601, EBI-2548012;
CC Q9UMX2; Q6P1W5: C1orf94; NbExp=4; IntAct=EBI-10281601, EBI-946029;
CC Q9UMX2; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-10281601, EBI-747204;
CC Q9UMX2; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-10281601, EBI-2686809;
CC Q9UMX2; P11926: ODC1; NbExp=5; IntAct=EBI-10281601, EBI-1044287;
CC Q9UMX2; Q04864: REL; NbExp=3; IntAct=EBI-10281601, EBI-307352;
CC Q9UMX2-2; O14977: AZIN1; NbExp=3; IntAct=EBI-12049527, EBI-1054824;
CC Q9UMX2-2; Q96A70: AZIN2; NbExp=3; IntAct=EBI-12049527, EBI-10281609;
CC Q9UMX2-2; P11926: ODC1; NbExp=3; IntAct=EBI-12049527, EBI-1044287;
CC Q9UMX2-2; P01189: POMC; NbExp=3; IntAct=EBI-12049527, EBI-12219503;
CC Q9UMX2-2; P78424: POU6F2; NbExp=3; IntAct=EBI-12049527, EBI-12029004;
CC Q9UMX2-2; Q04864-2: REL; NbExp=3; IntAct=EBI-12049527, EBI-10829018;
CC Q9UMX2-2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-12049527, EBI-11139477;
CC Q9UMX2-2; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-12049527, EBI-12287587;
CC Q9UMX2-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-12049527, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Ribosomal frameshifting; Named isoforms=2;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-76
CC and Glu-77. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=Q9UMX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMX2-2; Sequence=VSP_056789, VSP_056790, VSP_056791;
CC -!- TISSUE SPECIFICITY: Testis specific.
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=AAD51734.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD51734.1; 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; AF175296; AAD51734.1; ALT_SEQ; mRNA.
DR EMBL; AL589765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC073949; AAH73949.1; -; mRNA.
DR CCDS; CCDS58028.1; -. [Q9UMX2-2]
DR CCDS; CCDS81378.1; -. [Q9UMX2-1]
DR RefSeq; NP_001128411.1; NM_001134939.1.
DR RefSeq; NP_001288300.1; NM_001301371.1.
DR RefSeq; NP_057262.2; NM_016178.2. [Q9UMX2-1]
DR AlphaFoldDB; Q9UMX2; -.
DR SMR; Q9UMX2; -.
DR BioGRID; 119677; 40.
DR IntAct; Q9UMX2; 34.
DR STRING; 9606.ENSP00000313922; -.
DR iPTMnet; Q9UMX2; -.
DR PhosphoSitePlus; Q9UMX2; -.
DR BioMuta; OAZ3; -.
DR DMDM; 13431750; -.
DR MassIVE; Q9UMX2; -.
DR PaxDb; Q9UMX2; -.
DR PeptideAtlas; Q9UMX2; -.
DR PRIDE; Q9UMX2; -.
DR ProteomicsDB; 85220; -. [Q9UMX2-1]
DR Antibodypedia; 34072; 90 antibodies from 20 providers.
DR DNASU; 51686; -.
DR Ensembl; ENST00000400999.7; ENSP00000383784.3; ENSG00000143450.19. [Q9UMX2-1]
DR GeneID; 51686; -.
DR KEGG; hsa:51686; -.
DR UCSC; uc010pdl.3; human. [Q9UMX2-1]
DR CTD; 51686; -.
DR DisGeNET; 51686; -.
DR GeneCards; OAZ3; -.
DR HGNC; HGNC:8097; OAZ3.
DR HPA; ENSG00000143450; Tissue enriched (testis).
DR MIM; 605138; gene.
DR neXtProt; NX_Q9UMX2; -.
DR OpenTargets; ENSG00000143450; -.
DR PharmGKB; PA31886; -.
DR VEuPathDB; HostDB:ENSG00000143450; -.
DR eggNOG; KOG4387; Eukaryota.
DR GeneTree; ENSGT00940000161581; -.
DR HOGENOM; CLU_085486_0_0_1; -.
DR InParanoid; Q9UMX2; -.
DR OrthoDB; 1403675at2759; -.
DR PathwayCommons; Q9UMX2; -.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR SignaLink; Q9UMX2; -.
DR BioGRID-ORCS; 51686; 10 hits in 1078 CRISPR screens.
DR GenomeRNAi; 51686; -.
DR Pharos; Q9UMX2; Tbio.
DR PRO; PR:Q9UMX2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UMX2; protein.
DR Bgee; ENSG00000143450; Expressed in sperm and 110 other tissues.
DR ExpressionAtlas; Q9UMX2; baseline and differential.
DR Genevisible; Q9UMX2; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:UniProtKB.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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; Cytoplasm; Nucleus; Phosphoprotein;
KW Polyamine biosynthesis; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..235
FT /note="Ornithine decarboxylase antizyme 3"
FT /id="PRO_0000220859"
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"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /id="VSP_056789"
FT VAR_SEQ 49..56
FT /note="MLPRCYKS -> MTVPWRPGKRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056790"
FT VAR_SEQ 71..76
FT /note="SCLQCS -> PASSAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056791"
SQ SEQUENCE 235 AA; 27413 MW; D9DA9CD9CAEED311 CRC64;
MPCKRCRPSV YSLSYIKRGK TRNYLYPIWS PYAYYLYCYK YRITLREKML PRCYKSITYK
EEEDLTLQPR SCLQCSESLV GLQEGKSTEQ GNHDQLKELY SAGNLTVLAT DPLLHQDPVQ
LDFHFRLTSQ TSAHWHGLLC DRRLFLDIPY QALDQGNRES LTATLEYVEE KTNVDSVFVN
FQNDRNDRGA LLRAFSYMGF EVVRPDHPAL PPLDNVIFMV YPLERDVGHL PSEPP
