Peroxidase 12 precursor - Arabidopsis thaliana (Mouse-ear cress)

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Reviewed, UniProtKB/Swiss-Prot Q96520 (PER12_ARATH)

Last modified June 16, 2009. Version 92. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Peroxidase 12
      Short name=Atperox P12
    EC=1.11.1.7
Alternative name(s):
    PRXR6
    ATP4a

Gene names

Name:	PER12
Synonyms:	P12
Ordered Locus Names:	At1g71695
ORF Names:	F26A9.5, F14O23.6

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

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Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Exhibits a Ca²⁺-pectate binding affinity which could be interpreted in vivo as a specificity to interact with the pectic structure of the cell wall.
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 Probable. Vacuole Probable. Note: Carboxy-terminal extension appears to target the protein to vacuoles.
Tissue specificity	Expressed in roots and leaves.
Developmental stage	Expressed in the first stage of developing seeds. Ref.7
Induction	Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule. Ref.9
Miscellaneous	There are 73 peroxidase genes in A.thaliana.
Sequence similarities	Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.

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Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Secreted Vacuole
Domain	Signal
Ligand	Calcium Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
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 membrane Inferred from direct assay. Source: TAIR plant-type cell wall Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

Potential

Chain

32 – 358

327

Peroxidase 12

PRO_0000023678

Sites

Active site

Proton acceptor By similarity

Metal binding

Calcium 1 By similarity

Metal binding

Calcium 1; via carbonyl oxygen By similarity

Metal binding

Calcium 1; via carbonyl oxygen By similarity

Metal binding

Calcium 1 By similarity

Metal binding

Calcium 1 By similarity

Metal binding

213

Iron (heme axial ligand) By similarity

Metal binding

214

Calcium 2 By similarity

Metal binding

259

Calcium 2 By similarity

Metal binding

262

Calcium 2 By similarity

Metal binding

267

Calcium 2 By similarity

Binding site

183

Substrate; via carbonyl oxygen By similarity

Site

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

188

N-linked (GlcNAc...) Potential

Glycosylation

202

N-linked (GlcNAc...) Potential

Glycosylation

251

N-linked (GlcNAc...) Potential

Glycosylation

334

N-linked (GlcNAc...) Potential

Disulfide bond

53 ↔ 134

By similarity

Disulfide bond

86 ↔ 91

By similarity

Disulfide bond

140 ↔ 335

By similarity

Disulfide bond

220 ↔ 247

By similarity

Experimental info

Sequence conflict

257

V → G in CAA66962. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q96520-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: B8F18C56CFCB4CB2
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FASTA

358

39,559

        10         20         30         40         50         60 
MTKAYSTRVL TFLILISLMA VTLNLFPTVE AKKRSRDAPI VKGLSWNFYQ KACPKVENII 

        70         80         90        100        110        120 
RKELKKVFKR DIGLAAAILR IHFHDCFVQG CEASVLLAGS ASGPGEQSSI PNLTLRQQAF 

       130        140        150        160        170        180 
VVINNLRALV QKKCGQVVSC SDILALAARD SVVLSGGPDY AVPLGRRDSL AFASQETTLN 

       190        200        210        220        230        240 
NLPPPFFNAS QLIADFANRN LNITDLVALS GGHTIGIAHC PSFTDRLYPN QDPTMNQFFA 

       250        260        270        280        290        300 
NSLKRTCPTA NSSNTQVNDI RSPDVFDNKY YVDLMNRQGL FTSDQDLFVD KRTRGIVESF 

       310        320        330        340        350 
AIDQQLFFDY FTVAMIKMGQ MSVLTGTQGE IRSNCSARNT QSFMSVLEEG IEEAISMI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases." Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P. Plant Gene Register PGR96-066 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"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 (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"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.
[7]	"Microarray analysis of developing Arabidopsis seeds." Girke T., Todd J., Ruuska S., White J., Benning C., Ohlrogge J. Plant Physiol. 124:1570-1581(2000) [PubMed: 11115875] [Abstract] Cited for: DEVELOPMENTAL STAGE. Strain: cv. Columbia.
[8]	"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana." Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C. J. Plant Physiol. 159:1165-1171(2002) Cited for: CHARACTERIZATION. Strain: cv. Columbia.
[9]	"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis." Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M. Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000) [PubMed: 11027363] [Abstract] Cited for: INDUCTION. Strain: cv. Columbia.
[10]	"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.

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Cross-references

Sequence databases
	X98318 mRNA. Translation: CAA66962.1. X98773 mRNA. Translation: CAA67309.1. AC016163 Genomic DNA. Translation: AAG51834.1. AC012654 Genomic DNA. Translation: AAF43221.1. AF334732 mRNA. Translation: AAG50110.1. BT000715 mRNA. Translation: AAN31858.1. AY087964 mRNA. Translation: AAM65511.1.
IPI	IPI00538176.
PIR	A96739.
RefSeq	NP_177313.1.
UniGene	At.67041 At.94
3D structure databases
HSSP	HSSP built from PDB template 1QGJ based on UniProtKB Q39034.
ModBase	Search...
Protein family/group databases
PeroxiBase	93. AtPrx12.
Proteomic databases
PRIDE	Q96520.
Genome annotation databases
GeneID	843498.
GenomeReviews	Gene locus AT1G71695 in contig CT485782_GR.
KEGG	ath:AT1G71695.
NMPDR	fig\|3702.1.peg.6650.
Organism-specific databases
GeneFarm	1474. 61.
TAIR	At1g71695.
Phylogenomic databases
OMA	Q96520. NLVNREG.
Enzyme and pathway databases
BRENDA	1.11.1.7. 302.
Gene expression databases
ArrayExpress	Q96520.
GermOnline	AT1G71695. 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...

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Entry information

Entry name

PER12_ARATH

Accession

Primary (citable) accession number: Q96520
Secondary accession number(s): Q43734

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents