Reviewed, UniProtKB/Swiss-Prot Q10N21 (APX1_ORYSJ)

Names and origin

Protein names

Recommended name:
    L-ascorbate peroxidase 1, cytosolic
      Short name=APXa
    EC=1.11.1.11
Alternative name(s):
    OsAPx01

Gene names

Name:	APX1
Ordered Locus Names:	Os03g0285700, LOC_Os03g17690
ORF Names:	OSJNBa0013D02.10, OsJ_009999

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

General annotation (Comments)

Function	Plays a key role in hydrogen peroxide removal.
Catalytic activity	L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group By similarity. Binds 1 potassium or calcium ion per subunit By similarity.
Enzyme regulation	Inhibited by p-chloromercuriphenylsulfonic acid (CMPSA).
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in roots, aerial vegetative parts and reproductive organs.
Induction	By stress and hormones. By infection with rice blast fungus (M.grisea). Circadian-regulation. Expression is higher during the light phase than during the dark phase.
Sequence similarities	Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=4 mM for ascorbate KM=0.3 mM for H(2)O(2) Vmax=15 mM/min/mg enzyme with ascorbate as substrate Vmax=1 mM/min/mg enzyme with H(2)O(2) as substrate pH dependence: Optimum pH is 6-7.

Ontologies

Keywords
Biological process	Hydrogen peroxide Stress response
Cellular component	Cytoplasm
Ligand	Calcium Heme Iron Metal-binding Potassium
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-ascorbate peroxidase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 250	249	L-ascorbate peroxidase 1, cytosolic		PRO_0000055593
Sites
	Active site	42	1	Proton acceptor By similarity
	Metal binding	163	1	Iron (heme axial ligand) By similarity
	Metal binding	164	1	Potassium or calcium By similarity
	Metal binding	180	1	Potassium or calcium By similarity
	Metal binding	182	1	Potassium or calcium By similarity
	Metal binding	187	1	Potassium or calcium By similarity
	Site	38	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q10N21-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 637D70B191CC92E9	FASTA	250	27,156
	10 20 30 40 50 60 MAKNYPVVSA EYQEAVEKAR QKLRALIAEK SCAPLMLRLA WHSAGTFDVS SKTGGPFGTM 70 80 90 100 110 120 KTPAELSHAA NAGLDIAVRM LEPIKEEIPT ISYADFYQLA GVVAVEVSGG PAVPFHPGRE 130 140 150 160 170 180 DKPAPPPEGR LPDATKGSDH LRQVFGAQMG LSDQDIVALS GGHTLGRCHK ERSGFEGPWT 190 200 210 220 230 240 RNPLQFDNSY FTELLSGDKE GLLQLPSDKA LLSDPAFRPL VEKYAADEKA FFEDYKEAHL 250 KLSELGFADA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of cytosolic ascorbate peroxidase cDNA from rice." Morita S., Kaminaka H., Yokoi H., Masumura T., Tanaka K. (er) Plant Gene Register PGR97-012 Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Nipponbare. Tissue: Seedling.
[2]	"Sequence, annotation, and analysis of synteny between rice chromosome 3 and diverged grass species." The rice chromosome 3 sequencing consortium Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S. , Johri S., Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H.-I., Rambo T., Currie J., Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., Jin W., Lee H.R., Jiang J., Jackson S. Genome Res. 15:1284-1291(2005) [PubMed: 16109971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"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.
[4]	"Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana." The rice annotation project (RAP) Genome Res. 17:175-183(2007) [PubMed: 17210932] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[5]	"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.
[6]	"Proteome analysis of differentially displayed proteins as a tool for investigating ozone stress in rice (Oryza sativa L.) seedlings." Agrawal G.K., Rakwal R., Yonekura M., Kubo A., Saji H. Proteomics 2:947-959(2002) [PubMed: 12203890] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11, INDUCTION. Strain: cv. Nipponbare. Tissue: Leaf.
[7]	"Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003." Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K. Nucleic Acids Res. 32:D388-D392(2004) [PubMed: 14681440] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 25-34 AND 107-116, SUBCELLULAR LOCATION. Strain: cv. Nipponbare. Tissue: Anther, Callus, Panicle, Root, Sheath and Stem.
[8]	"Heat shock-mediated APX gene expression and protection against chilling injury in rice seedlings." Sato Y., Murakami T., Funatsuki H., Matsuba S., Saruyama H., Tanida M. J. Exp. Bot. 52:145-151(2001) [PubMed: 11181723] [Abstract] Cited for: INDUCTION.
[9]	"Importance of ascorbate peroxidases OsAPX1 and OsAPX2 in the rice pathogen response pathways and growth and reproduction revealed by their transcriptional profiling." Agrawal G.K., Jwa N.-S., Iwahashi H., Rakwal R. Gene 322:93-103(2003) [PubMed: 14644501] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[10]	"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.
[11]	"Purification and characterization of two ascorbate peroxidases of rice (Oryza sativa L.) expressed in Escherichia coli." Lu Z., Takano T., Liu S. Biotechnol. Lett. 27:63-67(2005) [PubMed: 15685422] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D45423 mRNA. Translation: BAA08264.1. AC134232 Genomic DNA. Translation: AAO17000.1. DP000009 Genomic DNA. Translation: ABF95353.1. AP008209 Genomic DNA. Translation: BAF11683.1. CM000140 Genomic DNA. Translation: EAZ26516.1.
PIR	T03595.
RefSeq	NP_001049769.1.
UniGene	Os.12723
3D structure databases
HSSP	HSSP built from PDB template 1OAF based on UniProtKB Q43758.
SMR	Q10N21. Positions 2-250.
ModBase	Search...
Protein family/group databases
PeroxiBase	1865. OsAPx01.
Genome annotation databases
GeneID	4332474.
KEGG	osa:4332474.
Organism-specific databases
Gramene	P93404.
Family and domain databases
InterPro	IPR002207. Asc_perxdse. IPR002016. Haem_peroxidase_pln/fun/bac. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00459. ASPEROXIDASE. PR00458. PEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APX1_ORYSJ

Accession

Primary (citable) accession number: Q10N21
Secondary accession number(s): P93404, Q84QS3, Q8GZZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	August 22, 2006
Last modified:	November 25, 2008
This is version 24 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)