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UniProtKB/Swiss-Prot entry Q9LDA4


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

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Entry information
Entry name PER38_ARATH
Primary accession number Q9LDA4
Secondary accession numbers None
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 67)
Name and origin of the protein
Protein name Peroxidase 38 [Precursor]
Synonyms Atperox P38
EC 1.11.1.7
Gene name
Name: PER38
Synonyms: P38
OrderedLocusNames: At4g08780
ORFNames: T32A17.90
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[2]
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
AL161512; CAB78003.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161813; CAB82114.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C85088; C85088.
RefSeq NP_192618.1; -.
UniGene At.54214
3D structure databases
HSSP P00433; 2ATJ. [HSSP ENTRY / PDB]
SMR Q9LDA4; 23-327.
ModBase Q9LDA4.
Protein family/group databases
PeroxiBase 204; AtPrx38.
Organism-specific databases
GeneFarm 1867; 61.
TAIR At4g08780; -.
Gene expression databases
ArrayExpress Q9LDA4; -.
GermOnline AT4G08780; Arabidopsis thaliana.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005773; Cellular component: vacuole (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:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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 Q9LDA4; -.
Genome annotation databases
GeneID 826448; -.
GenomeReviews CT486007_GR; AT4G08780.
KEGG ath:AT4G08780; -.
NMPDR fig|3702.1.peg.18531; -.
Other
ProtoNet Q9LDA4.
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; Vacuole.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    22  22     Potential. 
CHAIN   23   346  324     Peroxidase 38. PRO_0000023704
ACT_SITE   64    64        Proton acceptor (By similarity). 
METAL   65    65        Calcium 1 (By similarity). 
METAL   68    68        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   70    70        Calcium 1; via carbonyl oxygen (By similarity). 
METAL   72    72        Calcium 1 (By similarity). 
METAL   74    74        Calcium 1 (By similarity). 
METAL   192   192        Iron (heme axial ligand) (By similarity). 
METAL   193   193        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   60    60  1     Transition state stabilizer (By similarity). 
MOD_RES   23    23        Pyrrolidone carboxylic acid (By similarity). 
CARBOHYD   79    79        N-linked (GlcNAc...) (Potential). 
CARBOHYD   236   236        N-linked (GlcNAc...) (Potential). 
DISULFID   33   113        By similarity. 
DISULFID   66    71        By similarity. 
DISULFID   119   323        By similarity. 
DISULFID   199   231        By similarity. 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 38086 Da [This is the MW of the unprocessed precursor] CRC64: D5CD5762D9C03392 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHSSLIKLGF LLLLLQVSLS HAQLSPSFYD KTCPQVFDIV TNTIVNALRS DPRIAASILR 

        70         80         90        100        110        120 
LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAIE KACPRTVSCA 

       130        140        150        160        170        180 
DMLAIAAKES IVLAGGPSWM VPNGRRDSLR GFMDLANDNL PGPSSTLKQL KDRFKNVGLD 

       190        200        210        220        230        240 
RSSDLVALSG GHTFGKSQCQ FIMDRLYNFG ETGLPDPTLD KSYLATLRKQ CPRNGNQSVL 

       250        260        270        280        290        300 
VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDAAD TLPLVRAYAD GQGTFFDAFV 

       310        320        330        340 
KAIIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVDDAL EFASFM 

Q9LDA4 in FASTA format

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