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Entry version 114 (10 Apr 2019)
Sequence version 1 (22 Aug 2006)
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Protein

Catalase isozyme C

Gene

CATC

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Responsible for the redox homeostasis in leaves. Prevents nitric oxide (NO) accumulation and subsequent NO-mediated leaf cell death as well as the S-nitrosylation of specific proteins (e.g. glyceraldehyde 3-phosphate dehydrogenase and thioredoxin) by degrading H2O2 (PubMed:22106097, PubMed:23331502). Involved in photorespiration. Promotes drought stress tolerance and recovery (Ref. 13). Involved in NO-mediated enhanced tolerance to zinc oxide nanoparticles (ZnO NPs)-induced phytotoxicity (PubMed:25958266). Participates to melatonin-mediated detoxification (PubMed:25912474).1 Publication4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

hemeBy similarity

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly inhibited by beta-mercaptoethanol, sodium azide and potassium cyanide. Slightly repressed by 3-amino-1,2,4-triazole (3-AT). Activity is repressed proportionally to increased concentration of NaCl, KCl, LiCl and MgCl2.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.5 min(-1) with H2O2 as substrate (at pH 7.5) (PubMed:21979082). kcat is 28 sec(-1) with H2O2 as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:26900141).2 Publications
  1. KM=43 mM for H2O2 (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. KM=40 mM for H2O2 (at pH 7.5)1 Publication
  1. Vmax=251 mmol/min/mg enzyme (at pH 7.4 and 30 degrees Celsius)1 Publication
  2. Vmax=0.03 µmol/min/g enzyme (at pH 7.5)1 Publication

pH dependencei

Optimum pH is 7.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei62HemeBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei65PROSITE-ProRule annotation1
Binding sitei102HemeBy similarity1
Active sitei138By similarity1
Binding sitei151HemeBy similarity1
Binding sitei344HemeBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi348Iron (heme axial ligand)By similarity1
Binding sitei355HemeBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • catalase activity Source: UniProtKB
  • heme binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide, Stress response
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-OSA-3299685 Detoxification of Reactive Oxygen Species
R-OSA-6798695 Neutrophil degranulation

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
5144 OsKat03

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Catalase isozyme C1 Publication (EC:1.11.1.6PROSITE-ProRule annotation2 Publications)
Short name:
CAT-C1 Publication
Short name:
OsCatC1 Publication
Alternative name(s):
Protein NITRIC OXIDE EXCESS 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CATC1 Publication
Synonyms:CAT11 Publication, NOE11 Publication
Ordered Locus Names:LOC_Os03g03910Imported, Os03g0131200Imported
ORF Names:OsJ_09293Imported, OSNPB_030131200Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOryza sativa subsp. japonica (Rice)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri39947 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryzaOryza sativa
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000059680 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Glyoxysome, Membrane, Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impaired catalase activity in leaves. Accumulation of hydrogen peroxide (H2O2) in leaves, which consequently promotes nitric oxide (NO) production via the activation of nitrate reductase, thus leading to subsequent NO-mediated leaf cell death, as well as increased S-nitrosylation of specific proteins including glyceraldehyde 3-phosphate dehydrogenase and thioredoxin (PubMed:22106097, PubMed:23331502). Leaf bleaching and cell death; these phenotypes are reversed by melatonin treatment (PubMed:25912474). Increased tolerance to zinc oxide nanoparticles (ZnO NPs) (PubMed:25958266).1 Publication3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi210Y → D: Phosphorylation mimic exhibits higher catalase activity. Impaired STRK1-mediated phosphorylation. 1 Publication1
Mutagenesisi210Y → F: Non-phosphorylation mimic exhibits loss of catalase activity. Impaired STRK1-mediated phosphorylation. 1 Publication1
Mutagenesisi360Y → D or F: Normal STRK1-mediated phosphorylation and subsequent catalase activity enhancement. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004456261 – 492Catalase isozyme CAdd BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei210Phosphotyrosine; by STRK11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki325 ↔ 3483-(S-cysteinyl)-tyrosine (Cys-Tyr)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by STRK1-mediated phosphorylation at Tyr-210 upon salt and oxidative stress.1 Publication

Keywords - PTMi

Phosphoprotein, Thioether bond

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in mature leaves (PubMed:21979082, PubMed:21398647, PubMed:22106097, PubMed:23331502, PubMed:26900141, PubMed:28969789, PubMed:29464319). Mainly expressed in leaf blades, stems, panicles, leaf sheaths, and culms, but barely in roots (PubMed:22106097, PubMed:23331502, PubMed:29464319).7 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Abundance in leaves follows a light-dependent rhythm with an oscillating expression pattern peaking early in the light period (PubMed:21398647, PubMed:23331502). Inhibited by water stress and abscisic acid (ABA) in a concentration-dependent manner (PubMed:21398647, PubMed:23331502). Enhanced by ABA biosynthesis inhibitors nordihydroguaiaretic acid and tungstate under water stress (PubMed:21398647). Slightly affected by high salinity and hydrogen peroxide (H2O2) treatments (PubMed:23331502). Accumulates upon infection by the bacterial blight agent X.oryzae pv. Oryzae (Xoo) strain PXO99 (PubMed:27185545). Repressed by cadmium (Cd) (PubMed:28969789).4 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (By similarity). Interacts with GLO1 and GLO4; these interactions are disturbed by alpha-hydroxy-2-pyridinemethanesulfonic acid (HPMS) and salicylic acid (SA) (PubMed:26900141). Interacts with STRK1 at the plasma membrane (PubMed:29581216).By similarity2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
4530.OS03T0131200-01

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q10S82

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi484 – 492Peroxisome targeting signal1 Publication9

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0047 Eukaryota
COG0753 LUCA

KEGG Orthology (KO)

More...
KOi
K03781

Identification of Orthologs from Complete Genome Data

More...
OMAi
KLAQFNR

Database of Orthologous Groups

More...
OrthoDBi
507937at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.180.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018028 Catalase
IPR024708 Catalase_AS
IPR024711 Catalase_clade1/3
IPR011614 Catalase_core
IPR037060 Catalase_core_sf
IPR002226 Catalase_haem_BS
IPR010582 Catalase_immune_responsive
IPR020835 Catalase_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11465 PTHR11465, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00199 Catalase, 1 hit
PF06628 Catalase-rel, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF038928 Catalase_clade1-3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00067 CATALASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01060 Catalase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56634 SSF56634, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00437 CATALASE_1, 1 hit
PS00438 CATALASE_2, 1 hit
PS51402 CATALASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q10S82-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPYKHRPSS SFNGPLWSTN SGAPVWNNNN SLTVGSRGPI LLEDYHLVEK
60 70 80 90 100
LANFDRERIP ERVVHARGAS AKGFFEVTHD ITHLTCADFL RAPGVQTPVI
110 120 130 140 150
VRFSTVIHER GSPETLRDPR GFAIKFYTRE GNWDLVGNNF PVFFIRDGMK
160 170 180 190 200
FPDMVHSLKP NPKSHVQENW RILDFFSHHP ESLHMFTFLF DDIGIPADYR
210 220 230 240 250
HMDGSGVNTY TLVNRAGKSH YVKFHWKPTC GVKSLLDDEA VTVGGTNHSH
260 270 280 290 300
ATQDLYDSIA AGNFPEWKLF IQTIDPDHED RFDFDPLDVT KTWPEDIVPL
310 320 330 340 350
QPVGRMVLNR NIDNFFSENE QLAFCPGIIV PGIYYSDDKL LQTRIFSYSD
360 370 380 390 400
TQRHRLGPNY LLLPPNAPKC AHHNNHYDGF MNFMHRDEEV DYFPSRYDPA
410 420 430 440 450
KHAPRYPIPS ATLTGRREKV VIAKENNFKQ PGERYRSWDP ARQDRFIKRW
460 470 480 490
IDALSDPRLT HEIRSIWLSY WSQADRSLGQ KLASRLSAKP SM
Length:492
Mass (Da):56,764
Last modified:August 22, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4443434F3485C8AA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti121G → V in BAA34205 (Ref. 1) Curated1
Sequence conflicti121G → V in AAQ19030 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D86611 Genomic DNA Translation: BAA34205.1
AY339372 mRNA Translation: AAQ19030.1
DP000009 Genomic DNA Translation: ABF93810.1
AP008209 Genomic DNA Translation: BAF10775.1
AP014959 Genomic DNA Translation: BAS82138.1
CM000140 Genomic DNA Translation: EEE58275.1
AK062174 mRNA Translation: BAG88238.1
AK066378 mRNA Translation: BAG89941.1

NCBI Reference Sequences

More...
RefSeqi
XP_015629749.1, XM_015774263.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Os.7986

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
Os03t0131200-01; Os03t0131200-01; Os03g0131200
Os03t0131200-02; Os03t0131200-02; Os03g0131200

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4331509

Gramene; a comparative resource for plants

More...
Gramenei
Os03t0131200-01; Os03t0131200-01; Os03g0131200
Os03t0131200-02; Os03t0131200-02; Os03g0131200

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
osa:4331509

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86611 Genomic DNA Translation: BAA34205.1
AY339372 mRNA Translation: AAQ19030.1
DP000009 Genomic DNA Translation: ABF93810.1
AP008209 Genomic DNA Translation: BAF10775.1
AP014959 Genomic DNA Translation: BAS82138.1
CM000140 Genomic DNA Translation: EEE58275.1
AK062174 mRNA Translation: BAG88238.1
AK066378 mRNA Translation: BAG89941.1
RefSeqiXP_015629749.1, XM_015774263.1
UniGeneiOs.7986

3D structure databases

SMRiQ10S82
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4530.OS03T0131200-01

Protein family/group databases

PeroxiBasei5144 OsKat03

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiOs03t0131200-01; Os03t0131200-01; Os03g0131200
Os03t0131200-02; Os03t0131200-02; Os03g0131200
GeneIDi4331509
GrameneiOs03t0131200-01; Os03t0131200-01; Os03g0131200
Os03t0131200-02; Os03t0131200-02; Os03g0131200
KEGGiosa:4331509

Phylogenomic databases

eggNOGiKOG0047 Eukaryota
COG0753 LUCA
KOiK03781
OMAiKLAQFNR
OrthoDBi507937at2759

Enzyme and pathway databases

ReactomeiR-OSA-3299685 Detoxification of Reactive Oxygen Species
R-OSA-6798695 Neutrophil degranulation

Family and domain databases

Gene3Di2.40.180.10, 1 hit
InterProiView protein in InterPro
IPR018028 Catalase
IPR024708 Catalase_AS
IPR024711 Catalase_clade1/3
IPR011614 Catalase_core
IPR037060 Catalase_core_sf
IPR002226 Catalase_haem_BS
IPR010582 Catalase_immune_responsive
IPR020835 Catalase_sf
PANTHERiPTHR11465 PTHR11465, 1 hit
PfamiView protein in Pfam
PF00199 Catalase, 1 hit
PF06628 Catalase-rel, 1 hit
PIRSFiPIRSF038928 Catalase_clade1-3, 1 hit
PRINTSiPR00067 CATALASE
SMARTiView protein in SMART
SM01060 Catalase, 1 hit
SUPFAMiSSF56634 SSF56634, 1 hit
PROSITEiView protein in PROSITE
PS00437 CATALASE_1, 1 hit
PS00438 CATALASE_2, 1 hit
PS51402 CATALASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCATA3_ORYSJ
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q10S82
Secondary accession number(s): Q7XAD9, Q9ZRI9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2018
Last sequence update: August 22, 2006
Last modified: April 10, 2019
This is version 114 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
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