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UniProtKB/Swiss-Prot entry O23044


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

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Entry information
Entry name PER3_ARATH
Primary accession number O23044
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 74)
Name and origin of the protein
Protein name Peroxidase 3 [Precursor]
Synonyms Atperox P3
EC 1.11.1.7
Rare cold-inducible protein
RCI3A
ATPRC
Gene name
Name: PER3
Synonyms: P3, RCI3
OrderedLocusNames: At1g05260
ORFNames: YUP8H12.13
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Etiolated seedling;
PubMed=12366797 [NCBI, ExPASy, EBI, Israel, Japan]
Llorente F., Lopez-Cobollo R.M., Catala R., Martinez-Zapater J.M., Salinas J.;
"A novel cold-inducible gene from Arabidopsis, RCI3, encodes a peroxidase that constitutes a component for stress tolerance.";
Plant J. 32:13-24(2002).
[2]
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).
[3]
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).
[4]
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.
[5]
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
U97684; AAB94661.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC000098; AAB71452.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT004817; AAO44083.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY084678; AAM61240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B86187; B86187.
RefSeq NP_172018.1; -.
UniGene At.23986
3D structure databases
HSSP O22443; 1FHF. [HSSP ENTRY / PDB]
ModBase O23044.
Protein family/group databases
PeroxiBase 79; AtPrx03.
Organism-specific databases
GeneFarm 1833; 61.
TAIR At1g05260; -.
Gene expression databases
ArrayExpress O23044; -.
GermOnline AT1G05260; Arabidopsis thaliana.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004601; Molecular function: peroxidase activity (inferred from electronic annotation from InterPro).
GO:0042744; Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0042538; Biological process: hyperosmotic salinity response (inferred from mutant phenotype from TAIR).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009409; Biological process: response to cold (inferred from expression pattern from TAIR).
GO:0009269; Biological process: response to desiccation (inferred from mutant phenotype from TAIR).
QuickGo view.
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).
Proteomics databases
PRIDE O23044; -.
Genome annotation databases
GeneID 837028; -.
GenomeReviews CT485782_GR; AT1G05260.
KEGG ath:AT1G05260; -.
Other
ProtoNet O23044.
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; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    24  24     Potential. 
CHAIN   25   326  302     Peroxidase 3. PRO_0000023669
ACT_SITE   66    66        Proton acceptor (By similarity). 
METAL   67    67        Calcium 1 (By similarity). 
METAL   70    70        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   72    72        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   76    76        Calcium 1 (By similarity). 
METAL   191   191        Iron (heme axial ligand) (By similarity). 
METAL   192   192        Calcium 2 (By similarity). 
METAL   244   244        Calcium 2 (By similarity). 
METAL   247   247        Calcium 2 (By similarity). 
METAL   252   252        Calcium 2 (By similarity). 
BINDING   161   161        Substrate; via carbonyl oxygen (By similarity). 
SITE   62    62  1     Transition state stabilizer (By similarity). 
MOD_RES   25    25        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   80    80        N-linked (GlcNAc...) (Potential). 
CARBOHYD   138   138        N-linked (GlcNAc...) (Potential). 
CARBOHYD   166   166        N-linked (GlcNAc...) (Potential). 
CARBOHYD   207   207        N-linked (GlcNAc...) (Potential). 
CARBOHYD   237   237        N-linked (GlcNAc...) (Potential). 
DISULFID   35   113        By similarity. 
DISULFID   68    73        By similarity. 
DISULFID   119   321        By similarity. 
DISULFID   198   231        By similarity. 
CONFLICT   18    18        I -> M (in Ref. 4; AAM61240). 
Sequence information
Length: 326 AA [This is the length of the unprocessed precursor] Molecular weight: 34906 Da [This is the MW of the unprocessed precursor] CRC64: 45D45362E5DD1B83 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNCLIAIALS VSFFLVGIVG PIQAQLQMNF YANSCPNAEK IVQDFVSNHV SNAPSLAAAL 

        70         80         90        100        110        120 
IRMHFHDCFV RGCDGSVLIN STSGNAERDA TPNLTVRGFG FIDAIKSVLE AQCPGIVSCA 

       130        140        150        160        170        180 
DIIALASRDA VVFTGGPNWS VPTGRRDGRI SNAAEALANI PPPTSNITNL QTLFANQGLD 

       190        200        210        220        230        240 
LKDLVLLSGA HTIGVSHCSS FTNRLYNFTG RGGQDPALDS EYAANLKSRK CPSLNDNKTI 

       250        260        270        280        290        300 
VEMDPGSRKT FDLSYYQLVL KRRGLFQSDS ALTTNPTTLS NINRILTGSV GSFFSEFAKS 

       310        320 
MEKMGRINVK TGSAGVVRRQ CSVANS 

O23044 in FASTA format

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View entry in raw text format (no links)
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