OAZ2_HUMAN
ID OAZ2_HUMAN Reviewed; 189 AA.
AC O95190;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ornithine decarboxylase antizyme 2;
DE Short=AZ2;
DE Short=ODC-Az 2;
GN Name=OAZ2;
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].
RX PubMed=9782076; DOI=10.1006/geno.1998.5434;
RA Ivanov I.P., Gesteland R.F., Atkins J.F.;
RT "A second mammalian antizyme: conservation of programmed ribosomal
RT frameshifting.";
RL Genomics 52:119-129(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10352227; DOI=10.1016/s0378-1119(99)00128-6;
RA Zhou J., Atkins J.F., Gesteland R.F.;
RT "Structure of human ornithine decarboxylase antizyme 2 gene.";
RL Gene 232:165-171(1999).
RN [3]
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). Involved in the translocation of
CC AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (By
CC similarity). {ECO:0000250|UniProtKB:O08608,
CC 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). {ECO:0000250|UniProtKB:P54368,
CC ECO:0000269|PubMed:17900240}.
CC -!- INTERACTION:
CC O95190; Q01850: CDR2; NbExp=3; IntAct=EBI-1051861, EBI-1181367;
CC O95190; Q4VX76: SYTL3; NbExp=3; IntAct=EBI-1051861, EBI-2840607;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Ser-32
CC and Asp-33. An autoregulatory mechanism enables modulation of
CC frameshifting according to the cellular concentration of polyamines.;
CC Name=1;
CC IsoId=O95190-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ODC antizyme family. {ECO:0000305}.
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DR EMBL; AF057297; AAD03265.1; -; mRNA.
DR CCDS; CCDS58372.1; -. [O95190-1]
DR RefSeq; NP_002528.1; NM_002537.3. [O95190-1]
DR AlphaFoldDB; O95190; -.
DR SMR; O95190; -.
DR BioGRID; 111001; 11.
DR IntAct; O95190; 5.
DR MINT; O95190; -.
DR STRING; 9606.ENSP00000463013; -.
DR iPTMnet; O95190; -.
DR PhosphoSitePlus; O95190; -.
DR BioMuta; OAZ2; -.
DR MassIVE; O95190; -.
DR PaxDb; O95190; -.
DR PeptideAtlas; O95190; -.
DR PRIDE; O95190; -.
DR Antibodypedia; 42839; 91 antibodies from 20 providers.
DR DNASU; 4947; -.
DR Ensembl; ENST00000326005.10; ENSP00000463013.1; ENSG00000180304.14. [O95190-1]
DR GeneID; 4947; -.
DR KEGG; hsa:4947; -.
DR UCSC; uc002ano.3; human. [O95190-1]
DR CTD; 4947; -.
DR DisGeNET; 4947; -.
DR GeneCards; OAZ2; -.
DR HGNC; HGNC:8096; OAZ2.
DR HPA; ENSG00000180304; Low tissue specificity.
DR MIM; 604152; gene.
DR neXtProt; NX_O95190; -.
DR OpenTargets; ENSG00000180304; -.
DR PharmGKB; PA31885; -.
DR VEuPathDB; HostDB:ENSG00000180304; -.
DR eggNOG; KOG4387; Eukaryota.
DR GeneTree; ENSGT00940000157725; -.
DR HOGENOM; CLU_085486_2_0_1; -.
DR InParanoid; O95190; -.
DR OMA; IVHFRYE; -.
DR OrthoDB; 1403675at2759; -.
DR PhylomeDB; O95190; -.
DR TreeFam; TF314741; -.
DR PathwayCommons; O95190; -.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR SignaLink; O95190; -.
DR BioGRID-ORCS; 4947; 18 hits in 1086 CRISPR screens.
DR ChiTaRS; OAZ2; human.
DR GeneWiki; OAZ2; -.
DR GenomeRNAi; 4947; -.
DR Pharos; O95190; Tbio.
DR PRO; PR:O95190; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O95190; protein.
DR Bgee; ENSG00000180304; Expressed in left testis and 208 other tissues.
DR ExpressionAtlas; O95190; baseline and differential.
DR Genevisible; O95190; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008073; F:ornithine decarboxylase inhibitor activity; IDA:UniProtKB.
DR GO; GO:1902268; P:negative regulation of polyamine transmembrane transport; IEA:Ensembl.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:ProtInc.
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; IPR029916; ODC-AZ_2.
DR InterPro; IPR002993; ODC_AZ.
DR InterPro; IPR038581; ODC_AZ_sf.
DR PANTHER; PTHR10279; PTHR10279; 1.
DR PANTHER; PTHR10279:SF6; PTHR10279:SF6; 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 Nucleus; Phosphoprotein; Polyamine biosynthesis; Reference proteome;
KW Ribosomal frameshifting.
FT CHAIN 1..189
FT /note="Ornithine decarboxylase antizyme 2"
FT /id="PRO_0000220857"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08608"
FT VARIANT 70
FT /note="P -> L (in dbSNP:rs3751534)"
FT /id="VAR_050420"
SQ SEQUENCE 189 AA; 21011 MW; 66390D87EB30CB8F CRC64;
MINTQDSSIL PLSNCPQLQC CRHIVPGPLW CSDAPHPLSK IPGGRGGGRD PSLSALIYKD
EKLTVTQDLP VNDGKPHIVH FQYEVTEVKV SSWDAVLSSQ SLFVEIPDGL LADGSKEGLL
ALLEFAEEKM KVNYVFICFR KGREDRAPLL KTFSFLGFEI VRPGHPCVPS RPDVMFMVYP
LDQNLSDED