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Protein

Ornithine decarboxylase antizyme 3

Gene

OAZ3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to ODC1 without promoting its degradation (PubMed:17900240). Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Polyamine biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine decarboxylase antizyme 3
Short name:
AZ3
Short name:
ODC-Az 3
Gene namesi
Name:OAZ3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8097. OAZ3.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31886.

Chemistry

DrugBankiDB00129. L-Ornithine.

Polymorphism and mutation databases

DMDMi13431750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Ornithine decarboxylase antizyme 3PRO_0000220859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei12 – 121PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9UMX2.
PRIDEiQ9UMX2.

PTM databases

PhosphoSiteiQ9UMX2.

Expressioni

Tissue specificityi

Testis specific.

Developmental stagei

Expression starts early in spermiogenesis and finishes in the late spermatid phase.

Gene expression databases

BgeeiQ9UMX2.
CleanExiHS_OAZ3.
ExpressionAtlasiQ9UMX2. baseline and differential.
GenevisibleiQ9UMX2. HS.

Organism-specific databases

HPAiHPA045808.

Interactioni

Subunit structurei

Interacts with GGN (By similarity). Interacts with AZIN2; the interaction stabilizes the complex by inhibiting AZIN2 ubiquitination and degradation and leads to increased ornithine decarboxylase (ODC) activity and decreased rate of ODC1 degradation.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AZIN1O149773EBI-10281601,EBI-1054824
AZIN2Q96A705EBI-10281601,EBI-10281609
BLZF1Q9H2G93EBI-10281601,EBI-2548012
C1orf94Q6P1W53EBI-10281601,EBI-946029
IKZF3Q9UKT93EBI-10281601,EBI-747204
L3MBTL3Q96JM73EBI-10281601,EBI-2686809
ODC1P119263EBI-10281601,EBI-1044287
RELQ048643EBI-10281601,EBI-307352

Protein-protein interaction databases

BioGridi119677. 30 interactions.
IntActiQ9UMX2. 8 interactions.
STRINGi9606.ENSP00000415904.

Structurei

3D structure databases

ProteinModelPortaliQ9UMX2.
SMRiQ9UMX2. Positions 99-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ODC antizyme family.Curated

Phylogenomic databases

eggNOGiKOG4387. Eukaryota.
ENOG4112791. LUCA.
GeneTreeiENSGT00390000009476.
HOGENOMiHOG000115254.
HOVERGENiHBG101008.
InParanoidiQ9UMX2.
KOiK16614.
OrthoDBiEOG7KM5W3.

Family and domain databases

InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR029913. ODC-AZ_3.
IPR002993. ODC_AZ.
[Graphical view]
PANTHERiPTHR10279. PTHR10279. 1 hit.
PTHR10279:SF9. PTHR10279:SF9. 1 hit.
PfamiPF02100. ODC_AZ. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS01337. ODC_AZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing and ribosomal frameshifting. AlignAdd to basket

Note: A ribosomal frameshift occurs between the codons for Ser-76 and Glu-77. An autoregulatory mechanism enables modulation of frameshifting according to the cellular concentration of polyamines.

Isoform 1 (identifier: Q9UMX2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPCKRCRPSV YSLSYIKRGK TRNYLYPIWS PYAYYLYCYK YRITLREKML
60 70 80 90 100
PRCYKSITYK EEEDLTLQPR SCLQCSESLV GLQEGKSTEQ GNHDQLKELY
110 120 130 140 150
SAGNLTVLAT DPLLHQDPVQ LDFHFRLTSQ TSAHWHGLLC DRRLFLDIPY
160 170 180 190 200
QALDQGNRES LTATLEYVEE KTNVDSVFVN FQNDRNDRGA LLRAFSYMGF
210 220 230
EVVRPDHPAL PPLDNVIFMV YPLERDVGHL PSEPP
Length:235
Mass (Da):27,413
Last modified:October 29, 2014 - v2
Checksum:iD9DA9CD9CAEED311
GO
Isoform 2 (identifier: Q9UMX2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.
     49-56: MLPRCYKS → MTVPWRPGKRR
     71-76: SCLQCS → PASSAP

Note: No experimental confirmation available.
Show »
Length:190
Mass (Da):21,650
Checksum:iD416886E1902962B
GO

Sequence cautioni

The sequence AAD51734.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAD51734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 2. VSP_056789Add
BLAST
Alternative sequencei49 – 568MLPRCYKS → MTVPWRPGKRR in isoform 2. 1 PublicationVSP_056790
Alternative sequencei71 – 766SCLQCS → PASSAP in isoform 2. 1 PublicationVSP_056791

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175296 mRNA. Translation: AAD51734.1. Sequence problems.
AL589765 Genomic DNA. No translation available.
BC073949 mRNA. Translation: AAH73949.1.
CCDSiCCDS58028.1. [Q9UMX2-2]
RefSeqiNP_001128411.1. NM_001134939.1.
NP_001288300.1. NM_001301371.1.
NP_057262.2. NM_016178.2. [Q9UMX2-1]
UniGeneiHs.713789.

Genome annotation databases

EnsembliENST00000627780; ENSP00000486158; ENSG00000143450. [Q9UMX2-2]
GeneIDi51686.
KEGGihsa:51686.
UCSCiuc010pdl.3. human. [Q9UMX2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF175296 mRNA. Translation: AAD51734.1. Sequence problems.
AL589765 Genomic DNA. No translation available.
BC073949 mRNA. Translation: AAH73949.1.
CCDSiCCDS58028.1. [Q9UMX2-2]
RefSeqiNP_001128411.1. NM_001134939.1.
NP_001288300.1. NM_001301371.1.
NP_057262.2. NM_016178.2. [Q9UMX2-1]
UniGeneiHs.713789.

3D structure databases

ProteinModelPortaliQ9UMX2.
SMRiQ9UMX2. Positions 99-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119677. 30 interactions.
IntActiQ9UMX2. 8 interactions.
STRINGi9606.ENSP00000415904.

Chemistry

DrugBankiDB00129. L-Ornithine.

PTM databases

PhosphoSiteiQ9UMX2.

Polymorphism and mutation databases

DMDMi13431750.

Proteomic databases

PaxDbiQ9UMX2.
PRIDEiQ9UMX2.

Protocols and materials databases

DNASUi51686.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000627780; ENSP00000486158; ENSG00000143450. [Q9UMX2-2]
GeneIDi51686.
KEGGihsa:51686.
UCSCiuc010pdl.3. human. [Q9UMX2-1]

Organism-specific databases

CTDi51686.
GeneCardsiOAZ3.
HGNCiHGNC:8097. OAZ3.
HPAiHPA045808.
MIMi605138. gene.
neXtProtiNX_Q9UMX2.
PharmGKBiPA31886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4387. Eukaryota.
ENOG4112791. LUCA.
GeneTreeiENSGT00390000009476.
HOGENOMiHOG000115254.
HOVERGENiHBG101008.
InParanoidiQ9UMX2.
KOiK16614.
OrthoDBiEOG7KM5W3.

Enzyme and pathway databases

ReactomeiR-HSA-350562. Regulation of ornithine decarboxylase (ODC).

Miscellaneous databases

GenomeRNAii51686.
NextBioi55690.
PROiQ9UMX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UMX2.
CleanExiHS_OAZ3.
ExpressionAtlasiQ9UMX2. baseline and differential.
GenevisibleiQ9UMX2. HS.

Family and domain databases

InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR029913. ODC-AZ_3.
IPR002993. ODC_AZ.
[Graphical view]
PANTHERiPTHR10279. PTHR10279. 1 hit.
PTHR10279:SF9. PTHR10279:SF9. 1 hit.
PfamiPF02100. ODC_AZ. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS01337. ODC_AZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Discovery of a spermatogenesis stage-specific ornithine decarboxylase antizyme: antizyme 3."
    Ivanov I.P., Rohrwasser A., Terreros D.A., Gesteland R.F., Atkins J.F.
    Proc. Natl. Acad. Sci. U.S.A. 97:4808-4813(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mammary gland.
  4. "Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase."
    Kanerva K., Makitie L.T., Pelander A., Heiskala M., Andersson L.C.
    Biochem. J. 409:187-192(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AZIN2.

Entry informationi

Entry nameiOAZ3_HUMAN
AccessioniPrimary (citable) accession number: Q9UMX2
Secondary accession number(s): E7EUE7, Q6GMR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 29, 2014
Last modified: April 13, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.