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UniProtKB/Swiss-Prot entry Q42547


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

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Entry information
Entry name CATA3_ARATH
Primary accession number Q42547
Secondary accession numbers Q93VY9 Q9LDS9
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 11, 2002 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 68)
Name and origin of the protein
Protein name Catalase-3
Synonym EC 1.11.1.6
Gene name
Name: CAT3
OrderedLocusNames: At1g20620
ORFNames: F2D10.40, F5M15.5
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 [GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1007/s004380050157; PubMed=8668130 [NCBI, ExPASy, EBI, Israel, Japan]
Zhong H.H., McClung C.R.;
"The circadian clock gates expression of two Arabidopsis catalase genes to distinct and opposite circadian phases.";
Mol. Gen. Genet. 251:196-203(1996).
[2]
SEQUENCE REVISION TO 457 AND 492.
Zhong H.H., McClung C.R.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9584109 [NCBI, ExPASy, EBI, Israel, Japan]
Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R.;
"Intron loss and gain during evolution of the catalase gene family in angiosperms.";
Genetics 149:355-365(1998).
[4]
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).
[5]
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).
[6]
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.
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
U43147; AAC49807.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF021937; AAC17732.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC069251; AAF80611.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC027665; AAF79625.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY058104; AAL24212.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY056447; AAL08303.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY087477; AAM65021.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S71112; S71112.
RefSeq NP_564120.1; -.
UniGene At.24821
3D structure databases
HSSP P46206; 1M7S. [HSSP ENTRY / PDB]
ModBase Q42547.
Protein-protein interaction databases
IntAct Q42547; -.
Protein family/group databases
PeroxiBase 5143; AtKat03.
Organism-specific databases
TAIR At1g20620; -.
Gene expression databases
ArrayExpress Q42547; -.
Family and domain databases
InterPro IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; FALSE_NEG.
BLOCKS Q42547.
Proteomic databases
ProMEX Q42547; -.
Genome annotation databases
GeneID 838651; -.
GenomeReviews CT485782_GR; AT1G20620.
NMPDR fig|3702.1.peg.2410; -.
Other
ProtoNet Q42547.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   492  492     Catalase-3. PRO_0000084932
ACT_SITE   65    65        By similarity. 
ACT_SITE   138   138        By similarity. 
METAL   348   348        Iron (heme axial ligand) (By similarity). 
CONFLICT   109   109        E -> G (in Ref. 1, 2 and 3). 
CONFLICT   162   162        P -> R (in Ref. 1, 2 and 3). 
CONFLICT   260   260        A -> V (in Ref. 6; AAM65021). 
CONFLICT   468   468        I -> T (in Ref. 1, 2 and 3). 
CONFLICT   472   473        SQ -> LK (in Ref. 1, 2 and 3). 
Sequence information
Length: 492 AA [This is the length of the unprocessed precursor] Molecular weight: 56695 Da [This is the MW of the unprocessed precursor] CRC64: 7322B111CFEBF37E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPYKYRPSS AYNAPFYTTN GGAPVSNNIS SLTIGERGPV LLEDYHLIEK VANFTRERIP 

        70         80         90        100        110        120 
ERVVHARGIS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVVHER ASPETMRDIR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNT PVFFIRDGIQ FPDVVHALKP NPKTNIQEYW RILDYMSHLP 

       190        200        210        220        230        240 
ESLLTWCWMF DDVGIPQDYR HMEGFGVHTY TLIAKSGKVL FVKFHWKPTC GIKNLTDEEA 

       250        260        270        280        290        300 
KVVGGANHSH ATKDLHDAIA SGNYPEWKLF IQTMDPADED KFDFDPLDVT KIWPEDILPL 

       310        320        330        340        350        360 
QPVGRLVLNR TIDNFFNETE QLAFNPGLVV PGIYYSDDKL LQCRIFAYGD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEI NYYPSKFDPV RCAEKVPTPT NSYTGIRTKC 

       430        440        450        460        470        480 
VIKKENNFKQ AGDRYRSWAP DRQDRFVKRW VEILSEPRLT HEIRGIWISY WSQADRSLGQ 

       490 
KLASRLNVRP SI 

Q42547 in FASTA format

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