Reviewed, UniProtKB/Swiss-Prot P54368 (OAZ1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ornithine decarboxylase antizyme
      Short name=ODC-Az

Gene names

Name:	OAZ1
Synonyms:	OAZ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Binds to, and destabilizes, ornithine decarboxylase which is then degraded. Also inhibits cellular uptake of polyamines by inactivating the polyamine uptake transporter.
Sequence similarities	Belongs to the ODC antizyme family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism Ribosomal frameshifting
Gene Ontology (GO)
Biological process	polyamine biosynthetic process Traceable author statement. Source: ProtInc
Cellular component	centrosome Inferred from direct assay. Source: HPA intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA
Molecular function	ornithine decarboxylase inhibitor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by ribosomal frameshifting. [Select]

Notes: A ribosomal frameshift occurs between the codons for Ser-68 and Asp-69. An autoregulatory mechanism enables modulation of frameshifting according to the cellular concentration of polyamines.

Isoform 1 (identifier: P54368-1)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 228	227	Ornithine decarboxylase antizyme		PRO_0000220849
Natural variations
	Natural variant	32	1	R → L		VAR_022215
	Natural variant	44	1	G → D		VAR_022216
	Natural variant	50	1	S → F		VAR_022217
	Natural variant	53	1	S → F		VAR_022218
	Natural variant	147	1	A → V		VAR_022219
Experimental info
	Sequence conflict	69	1	D → C in BAA13497. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DA43B74DF030BD9D	FASTA	228	25,406
	10 20 30 40 50 60 MVKSSLQRIL NSHCFAREKE GDKPSATIHA SRTMPLLSLH SRGGSSSESS RVSLHCCSNP 70 80 90 100 110 120 GPGPRWCSDA PHPPLKIPGG RGNSQRDHNL SANLFYSDDR LNVTEELTSN DKTRILNVQS 130 140 150 160 170 180 RLTDAKRINW RTVLSGGSLY IEIPGGALPE GSKDSFAVLL EFAEEQLRAD HVFICFHKNR 190 200 210 220 EDRAALLRTF SFLGFEIVRP GHPLVPKRPD ACFMAYTFER ESSGEEEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme." Tewari D.S., Qian Y., Thornton R.D., Pieringer J., Taub R., Mochan E., Tewari M. Biochim. Biophys. Acta 1209:293-295(1994) [PubMed: 7811704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[2]	"Molecular cloning of human antizyme from brain library." Hideyama T., Nisiyama M., Hayashi S. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Molecular cloning of human antizyme cDNA." Yang D., Takii T., Hayashi H., Itoh S., Hayashi M., Onozaki K. Biochem. Mol. Biol. Int. 38:957-964(1996) [PubMed: 9132164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphoma.
[4]	"Characterization of the human antizyme gene." Hayashi T., Matsufuji S., Hayashi S. Gene 203:131-139(1997) [PubMed: 9426243] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-32; ASP-44; PHE-50; PHE-53 AND VAL-147.
[6]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U09202 mRNA. Translation: AAA82155.1. Sequence problems. U09202 mRNA. Translation: AAA82154.1. Sequence problems. D87914 mRNA. Translation: BAA13497.1. D78361 mRNA. Translation: BAA11373.1. D78361 mRNA. Translation: BAA11374.1. Different initiation. D89870 Genomic DNA. Translation: BAA23101.1. AY865622 Genomic DNA. Translation: AAW56074.1. AC004152 Genomic DNA. Translation: AAC02802.1. AC004152 Genomic DNA. Translation: AAC02803.1.
PIR	I38591.
RefSeq	NP_004143.1.
UniGene	Hs.446427
3D structure databases
SMR	P54368. Positions 94-219.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54368.
PTM databases
PhosphoSite	P54368.
Polymorphism databases
NIEHS-SNPs	Search...
Genome annotation databases
Ensembl	ENSG00000104904. Homo sapiens. [Contig view]
GeneID	4946.
KEGG	hsa:4946.
Organism-specific databases
HGNC	HGNC:8095. OAZ1.
HPA	HPA009291.
MIM	601579. gene.
PharmGKB	PA31884.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P54368.
HOVERGEN	P54368.
Gene expression databases
ArrayExpress	P54368.
CleanEx	HS_OAZ1.
GermOnline	ENSG00000104904. Homo sapiens.
Family and domain databases
InterPro	IPR002993. ODC_AZ. [Graphical view]
PANTHER	PTHR10279. ODC_AZ. 1 hit.
Pfam	PF02100. ODC_AZ. 1 hit. [Graphical view]
ProDom	PD007483. ODC_AZ. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS01337. ODC_AZ. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00129. L-Ornithine.
LinkHub	P54368.
NextBio	19053.
SOURCE	Search...

Entry information

Entry name

OAZ1_HUMAN

Accession

Primary (citable) accession number: P54368
Secondary accession number(s): O43382 , Q14989, Q92595, Q9UPL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 57 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)