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Q96520 (PER12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxidase 12
Short name=Atperox P12
EC=1.11.1.7
Alternative name(s):
ATP4a
PRXR6
Gene names
Name:PER12
Synonyms:P12
Ordered Locus Names:At1g71695
ORF Names:F26A9.5, F14O23.6
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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

2 phenolic donor + H2O2 = 2 phenoxyl radical of the 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.8

Induction

Induced either by incompatible fungal pathogen attack, or by methyl jasmonate, a plant defense-related signaling molecule. Ref.10

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 processHydrogen peroxide
   Cellular componentSecreted
Vacuole
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular 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

plasmodesma

Inferred from direct assay. Source: TAIR

vacuole

Inferred from direct assay. Source: TAIR

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 358327Peroxidase 12
PRO_0000023678

Sites

Active site841Proton acceptor By similarity
Metal binding851Calcium 1 By similarity
Metal binding881Calcium 1; via carbonyl oxygen By similarity
Metal binding901Calcium 1; via carbonyl oxygen By similarity
Metal binding921Calcium 1 By similarity
Metal binding941Calcium 1 By similarity
Metal binding2131Iron (heme axial ligand) By similarity
Metal binding2141Calcium 2 By similarity
Metal binding2591Calcium 2 By similarity
Metal binding2621Calcium 2 By similarity
Metal binding2671Calcium 2 By similarity
Binding site1831Substrate; via carbonyl oxygen By similarity
Site801Transition state stabilizer By similarity

Amino acid modifications

Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 134 By similarity
Disulfide bond86 ↔ 91 By similarity
Disulfide bond140 ↔ 335 By similarity
Disulfide bond220 ↔ 247 By similarity

Experimental info

Sequence conflict2571V → G in CAA66962. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96520 [UniParc].

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

FASTA35839,559
        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

« Hide

References

« Hide '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. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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. expand/collapse author list , 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.
[6]"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].
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X98318 mRNA. Translation: CAA66962.1.
X98773 mRNA. Translation: CAA67309.1.
AC012654 Genomic DNA. Translation: AAF43221.1.
AC016163 Genomic DNA. Translation: AAG51834.1.
CP002684 Genomic DNA. Translation: AEE35217.1.
AF334732 mRNA. Translation: AAG50110.1.
BT000715 mRNA. Translation: AAN31858.1.
AY087964 mRNA. Translation: AAM65511.1.
IPIIPI00538176.
PIRA96739.
RefSeqNP_177313.1. NM_105826.3.
UniGeneAt.67041.
At.94.

3D structure databases

ProteinModelPortalQ96520.
SMRQ96520. Positions 38-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96520.

Protein family/group databases

PeroxiBase93. AtPrx12.

Proteomic databases

PRIDEQ96520.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G71695.1; AT1G71695.1; AT1G71695.
GeneID843498.
GenomeReviewsGene locus AT1G71695 in contig CT485782_GR.
KEGGath:AT1G71695.
NMPDRfig|3702.1.peg.6650.

Organism-specific databases

GeneFarm1474. 61.
TAIRAt1g71695.

Phylogenomic databases

GeneTreeEPGT00050000003680.
HOGENOMHBG597790.
InParanoidQ96520.
OMANCSARNT.
PhylomeDBQ96520.
ProtClustDBCLSN2679267.

Gene expression databases

ArrayExpressQ96520.
GenevestigatorQ96520.
GermOnlineAT1G71695. Arabidopsis thaliana.

Family and domain databases

InterProIPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR000823. Peroxidase_pln.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
KOK00430.
PfamPF00141. peroxidase. 1 hit.
[Graphical view]
PRINTSPR00458. PEROXIDASE.
PR00461. PLPEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePER12_ARATH
AccessionPrimary (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: December 14, 2011
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents