Q0JEQ2 (APX3_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable L-ascorbate peroxidase 3
EC=1.11.1.11

Alternative name(s):
OsAPx03

Gene names

Name:	APX3
Ordered Locus Names:	Os04g0223300, LOC_Os04g14680
ORF Names:	OSJNBb0072N21.2, OsJ_013310

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	291 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Plays a key role in hydrogen peroxide removal By similarity.
Catalytic activity	2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group By similarity. Binds 1 potassium or calcium ion per subunit By similarity.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Caution	According to Ref.5, it may be peroxisomal. There is however no experimental evidence to prove this.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 291	291	Probable L-ascorbate peroxidase 3		PRO_0000055595
Regions
	Transmembrane	263 – 283	21	Helical; Potential
Sites
	Active site	41	1	Proton acceptor By similarity
	Metal binding	161	1	Iron (heme axial ligand) By similarity
	Metal binding	162	1	Potassium or calcium By similarity
	Metal binding	178	1	Potassium or calcium By similarity
	Metal binding	185	1	Potassium or calcium By similarity
	Site	37	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0JEQ2 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 53CCEA0D39781236	FASTA	291	32,048
	10 20 30 40 50 60 MSAAPVVDAE YMAEVERARR DLRALIASKS CAPIMLRLAW HDAGTYDKAT KTGGPNGSIR 70 80 90 100 110 120 FPQEYSHAAN AGIKIAIDLL EPMKQKHPKI TYADLYQLAG VVAVEVTGGP TIDYVPGRRD 130 140 150 160 170 180 SSDSPEEGRL PDAKKGAAHL REVFYRMGLS DKDIVALSGG HTLGKARPER SGFDGAWTKD 190 200 210 220 230 240 PLKFDNSYFI ELLKENSEGL LKLPTDKALV EDPTFRRYVE LYAKDEDAFF RDYAESHKKL 250 260 270 280 290 SELGFTPPRS AFIYKSCQKP KSLLMQTAAG VAVAAAVVAW AYLCESNKRL G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of rice chromosome 4." Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., Zhang L. , Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., Li J., Hong G., Xue Y., Han B. Nature 420:316-320(2002) [PubMed: 12447439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[2]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed: 16100779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"The rice annotation project database (RAP-DB): 2008 update." The rice annotation project (RAP) Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed: 18089549] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[4]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[5]	"Analysis of the molecular evolutionary history of the ascorbate peroxidase gene family: inferences from the rice genome." Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M. J. Mol. Evol. 59:761-770(2004) [PubMed: 15599508] [Abstract] Cited for: NOMENCLATURE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL606634 Genomic DNA. Translation: CAD39836.2. AP008210 Genomic DNA. Translation: BAF14185.1. CM000141 Genomic DNA. Translation: EAZ29827.1.
RefSeq	NP_001052271.1. NM_001058806.1.
UniGene	Os.4987.
3D structure databases
ProteinModelPortal	Q0JEQ2.
SMR	Q0JEQ2. Positions 5-245.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0JEQ2.
Protein family/group databases
PeroxiBase	1867. OsAPx03.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os04g14680.1; LOC_Os04g14680.1; LOC_Os04g14680.
GeneID	4335202.
KEGG	osa:4335202.
Organism-specific databases
Gramene	Q6TY83.
Phylogenomic databases
GeneTree	EPGT00070000028978.
HOGENOM	HBG597790.
OMA	AYLCESN.
PhylomeDB	Q0JEQ2.
ProtClustDB	PLN02608.
Family and domain databases
InterPro	IPR002207. Asc_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
KO	K00434.
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX3_ORYSJ

Accession

Primary (citable) accession number: Q0JEQ2
Secondary accession number(s): Q6TY83, Q7XWZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 3, 2006
Last modified:	November 16, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program