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UniProtKB/Swiss-Prot entry Q96520


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PER12_ARATH
Primary accession number Q96520
Secondary accession number Q43734
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name Peroxidase 12 [Precursor]
Synonyms Atperox P12
EC 1.11.1.7
PRXR6
ATP4a
Gene name
Name: PER12
Synonyms: P12
OrderedLocusNames: At1g71695
ORFNames: F26A9.5, F14O23.6
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Capelli N., Tognolli M., Flach J., Overney S., Penel C., Greppin H., Simon P.;
"Eleven cDNA clones from Arabidopsis thaliana encoding isoperoxidases.";
(er) Plant Gene Register PGR96-066.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
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.;
"From expressed sequence tags to structure, function, evolution and expression of 28 ER-targeted Arabidopsis peroxidases.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
CHARACTERIZATION.
STRAIN=cv. Columbia;
DOI=10.1016/S0014-5793(98)00849-7; PubMed=9738941 [NCBI, ExPASy, EBI, Israel, Japan]
Oestergaard L., Pedersen A.G., Jespersen H.M., Brunak S., Welinder K.G.;
"Computational analyses and annotations of the Arabidopsis peroxidase gene family.";
FEBS Lett. 433:98-102(1998).
[7]
DEVELOPMENTAL STAGE.
STRAIN=cv. Columbia;
DOI=10.1104/pp.124.4.1570; PubMed=11115875 [NCBI, ExPASy, EBI, Israel, Japan]
Girke T., Todd J., Ruuska S., White J., Benning C., Ohlrogge J.;
"Microarray analysis of developing Arabidopsis seeds.";
Plant Physiol. 124:1570-1581(2000).
[8]
CHARACTERIZATION.
STRAIN=cv. Columbia;
Dunand C., Tognolli M., Overney S., von Tobel L., de Meyer M., Simon P., Penel C.;
"Identification and characterization of Ca(2+)-pectate binding peroxidases in Arabidopsis thaliana.";
J. Plant Physiol. 159:1165-1171(2002).
[9]
INDUCTION.
STRAIN=cv. Columbia;
DOI=10.1073/pnas.97.21.11655; PubMed=11027363 [NCBI, ExPASy, EBI, Israel, Japan]
Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T., Somerville S.C., Manners J.M.;
"Coordinated plant defense responses in Arabidopsis revealed by microarray analysis.";
Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
[10]
GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
STRAIN=cv. Columbia;
DOI=10.1016/S0378-1119(02)00465-1; PubMed=12034502 [NCBI, ExPASy, EBI, Israel, Japan]
Tognolli M., Penel C., Greppin H., Simon P.;
"Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana.";
Gene 288:129-138(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X98318; CAA66962.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X98773; CAA67309.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC016163; AAG51834.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012654; AAF43221.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF334732; AAG50110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000715; AAN31858.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087964; AAM65511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A96739; A96739.
RefSeq NP_177313.1; -.
UniGene At.94
3D structure databases
HSSP Q39034; 1QGJ. [HSSP ENTRY / PDB]
ModBase Q96520.
Protein family/group databases
PeroxiBase 93; AtPrx12.
Organism-specific databases
GeneFarm 1474; 61.
TAIR At1g71695; -.
Gene expression databases
ArrayExpress Q96520; -.
GermOnline AT1G71695; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002016; Haem_peroxidase_pln/fun/bac.
IPR000823; Peroxidase_pln.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00458; PEROXIDASE.
PR00461; PLPEROXIDASE.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q96520.
Genome annotation databases
GeneID 843498; -.
GenomeReviews CT485782_GR; AT1G71695.
KEGG ath:AT1G71695; -.
NMPDR fig|3702.1.peg.6650; -.
Other
ProtoNet Q96520.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Complete proteome; Glycoprotein; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    31  31     Potential. 
CHAIN   32   358  327     Peroxidase 12. PRO_0000023678
ACT_SITE   84    84        Proton acceptor (By similarity). 
METAL   85    85        Calcium 1 (By similarity). 
METAL   88    88        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   90    90        Calcium 1 (via carbonyl oxygen) (By similarity). 
METAL   92    92        Calcium 1 (By similarity). 
METAL   94    94        Calcium 1 (By similarity). 
METAL   213   213        Iron (heme axial ligand) (By similarity). 
METAL   214   214        Calcium 2 (By similarity). 
METAL   259   259        Calcium 2 (By similarity). 
METAL   262   262        Calcium 2 (By similarity). 
METAL   267   267        Calcium 2 (By similarity). 
BINDING   183   183        Substrate; via carbonyl oxygen (By similarity). 
SITE   80    80  1     Transition state stabilizer (By similarity). 
CARBOHYD   188   188        N-linked (GlcNAc...) (Potential). 
CARBOHYD   202   202        N-linked (GlcNAc...) (Potential). 
CARBOHYD   251   251        N-linked (GlcNAc...) (Potential). 
CARBOHYD   334   334        N-linked (GlcNAc...) (Potential). 
DISULFID   53   134        By similarity. 
DISULFID   86    91        By similarity. 
DISULFID   140   335        By similarity. 
DISULFID   220   247        By similarity. 
CONFLICT   257   257        V -> G (in Ref. 1; CAA66962). 
Sequence information
Length: 358 AA [This is the length of the unprocessed precursor] Molecular weight: 39559 Da [This is the MW of the unprocessed precursor] CRC64: B8F18C56CFCB4CB2 [This is a checksum on the sequence]
        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 

Q96520 in FASTA format

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