Reviewed, UniProtKB/Swiss-Prot Q96518 (PER16_ARATH)

Names and origin

Protein names

Recommended name:
    Peroxidase 16
      Short name=Atperox P16
    EC=1.11.1.7
Alternative name(s):
    ATP22a

Gene names

Name:	PER16
Synonyms:	P16
Ordered Locus Names:	At2g18980
ORF Names:	F19F24.18

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	323 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	Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. Binds 2 calcium ions per subunit By similarity.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in the whole plant, but preferentially in roots and leaves. Ref.5
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Complete proteome
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	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro peroxidase activity 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
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 323	300	Peroxidase 16		PRO_0000023682
Sites
	Active site	65	1	Proton acceptor By similarity
	Metal binding	66	1	Calcium 1 By similarity
	Metal binding	69	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	71	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	73	1	Calcium 1 By similarity
	Metal binding	75	1	Calcium 1 By similarity
	Metal binding	191	1	Iron (heme axial ligand) By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	243	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 2 By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Binding site	161	1	Substrate; via carbonyl oxygen By similarity
	Site	61	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	24	1	Pyrrolidone carboxylic acid By similarity
	Disulfide bond	34 ↔ 113		By similarity
	Disulfide bond	67 ↔ 72		By similarity
	Disulfide bond	119 ↔ 319		By similarity
	Disulfide bond	198 ↔ 230		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96518-1 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: 43880AD393482989	FASTA	323	35,832
	10 20 30 40 50 60 MKNQSSFSIV ALLLIFFSSS VFAQLQTNFY RKSCPNVETI VRNAVRQKFQ QTFVTAPATL 70 80 90 100 110 120 RLFFHDCFVR GCDASILLAS PSEKDHPDDK SLAGDGFDTV AKAKQALDRD PNCRNKVSCA 130 140 150 160 170 180 DILALATRDV VVLTGGPNYP VELGRRDGRL STVASVQHSL PQPSFKLDQL NTMFARHGLS 190 200 210 220 230 240 QTDMIALSGA HTIGFAHCGK FSKRIYNFSP KRPIDPTLNI RYALQLRQMC PIRVDLRIAI 250 260 270 280 290 300 NMDPTSPNTF DNAYFKNLQK GMGLFTSDQV LFSDERSRST VNSFASSEAT FRQAFISAIT 310 320 KLGRVGVKTG NAGEIRRDCS RVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases." Welinder K.G., Jespersen H.M., Kjaersgaard I.V.H., Justesen A.F., Oestergaard L., Abelskov A.K., Jensen R.B., Hansen L.N., Rasmussen S.K. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-323. Strain: cv. Columbia.
[4]	"Computational analyses and annotations of the Arabidopsis peroxidase gene family." Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G. FEBS Lett. 433:98-102(1998) [PubMed: 9738941] [Abstract] Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[5]	"Toward elucidating the global gene expression patterns of developing Arabidopsis: parallel analysis of 8300 genes by a high-density oligonucleotide probe array." Zhu T., Budworth P., Han B., Brown D., Chang H.-S., Zou G., Wang X. Plant Physiol. Biochem. 39:221-242(2001) Cited for: TISSUE SPECIFICITY. Strain: cv. Columbia.
[6]	"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana." Tognolli M., Penel C., Greppin H., Simon P. Gene 288:129-138(2002) [PubMed: 12034502] [Abstract] Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC003673 Genomic DNA. Translation: AAC09031.1. BT003082 mRNA. Translation: AAO23647.1. Y08781 mRNA. Translation: CAA70034.1.
IPI	IPI00527019.
PIR	T01626.
RefSeq	NP_179488.1.
UniGene	At.86
3D structure databases
HSSP	HSSP built from PDB template 1PA2 based on UniProtKB Q42578.
ModBase	Search...
Protein family/group databases
PeroxiBase	97. AtPrx16.
Proteomic databases
PRIDE	Q96518.
Genome annotation databases
GeneID	816415.
GenomeReviews	Gene locus AT2G18980 in contig CT485783_GR.
KEGG	ath:AT2G18980.
NMPDR	fig|3702.1.peg.8895.
Organism-specific databases
GeneFarm	1840. 61.
TAIR	At2g18980.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q96518.
GermOnline	AT2G18980. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002016. Haem_peroxidase_pln/fun/bac. IPR000823. Peroxidase_pln. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 1 hit. [Graphical view]
PRINTS	PR00458. PEROXIDASE. PR00461. PLPEROXIDASE.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PER16_ARATH

Accession

Primary (citable) accession number: Q96518

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)