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UniProtKB/Swiss-Prot entry Q9LDN9


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

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Entry information
Entry name PER37_ARATH
Primary accession number Q9LDN9
Secondary accession number Q8L7B3
Integrated into Swiss-Prot on December 6, 2002
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Peroxidase 37 [Precursor]
Synonyms Atperox P37
EC 1.11.1.7
ATP38
Gene name
Name: PER37
Synonyms: P37
OrderedLocusNames: At4g08770
ORFNames: T32A17.80
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=Root;
PubMed=12473102 [NCBI, ExPASy, EBI, Israel, Japan]
Welinder K.G., Justesen A.F., Kjaersgaard I.V.H., Jensen R.B., Rasmussen S.K., Jespersen H.M., Duroux L.;
"Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana.";
Eur. J. Biochem. 269:6063-6081(2002).
[2]
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).
[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]
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
AF452387; AAL40851.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161512; CAB78002.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161813; CAB82113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY136364; AAM97030.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000180; AAN15499.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B85088; B85088.
RefSeq NP_192617.1; -.
UniGene At.4181
3D structure databases
HSSP P00433; 2ATJ. [HSSP ENTRY / PDB]
SMR Q9LDN9; 23-328.
ModBase Q9LDN9.
Protein family/group databases
PeroxiBase 203; AtPrx37.
Organism-specific databases
GeneFarm 1864; 61.
TAIR At4g08770; -.
Gene expression databases
ArrayExpress Q9LDN9; -.
GermOnline AT4G08770; 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).
BLOCKS Q9LDN9.
ProtoNet Q9LDN9.
Genome annotation databases
GeneID 826447; -.
GenomeReviews CT486007_GR; AT4G08770.
KEGG ath:AT4G08770; -.
NMPDR fig|3702.1.peg.18530; -.
Other
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 37. PRO_0000023703
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   208   208        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. 
CONFLICT   28    28        F -> L (in Ref. 3; AAM97030/AAN15499). 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 38203 Da [This is the MW of the unprocessed precursor] CRC64: 744A4B8B618E15EE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHSSLIKLGF LLLLIQVSLS HAQLSPSFYD KTCPQVFDIA TTTIVNALRS DPRIAASILR 

        70         80         90        100        110        120 
LHFHDCFVNG CDASILLDNT TSFRTEKDAF GNANSARGFD VIDKMKAAVE KACPKTVSCA 

       130        140        150        160        170        180 
DLLAIAAQES VVLAGGPSWR VPNGRRDSLR GFMDLANDNL PAPFFTLNQL KDRFKNVGLD 

       190        200        210        220        230        240 
RASDLVALSG GHTFGKNQCQ FIMDRLYNFS NTGLPDPTLD KSYLSTLRKQ CPRNGNQSVL 

       250        260        270        280        290        300 
VDFDLRTPTL FDNKYYVNLK ENKGLIQSDQ ELFSSPDASD TLPLVREYAD GQGKFFDAFA 

       310        320        330        340 
KAMIRMSSLS PLTGKQGEIR LNCRVVNSKS KIMDVVEDAL EFASSM 

Q9LDN9 in FASTA format

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