CATA3_ARATH
ID CATA3_ARATH Reviewed; 492 AA.
AC Q42547; Q93VY9; Q9LDS9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Catalase-3;
DE EC=1.11.1.6;
GN Name=CAT3; OrderedLocusNames=At1g20620; ORFNames=F2D10.40, F5M15.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8668130; DOI=10.1007/bf02172918;
RA Zhong H.H., McClung C.R.;
RT "The circadian clock gates expression of two Arabidopsis catalase genes to
RT distinct and opposite circadian phases.";
RL Mol. Gen. Genet. 251:196-203(1996).
RN [2]
RP SEQUENCE REVISION TO 457 AND 492.
RA Zhong H.H., McClung C.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9584109; DOI=10.1093/genetics/149.1.355;
RA Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R.;
RT "Intron loss and gain during evolution of the catalase gene family in
RT angiosperms.";
RL Genetics 149:355-365(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP INTERACTION WITH LSD1.
RX PubMed=23958864; DOI=10.1104/pp.113.225805;
RA Li Y., Chen L., Mu J., Zuo J.;
RT "LESION SIMULATING DISEASE1 interacts with catalases to regulate
RT hypersensitive cell death in Arabidopsis.";
RL Plant Physiol. 163:1059-1070(2013).
RN [13]
RP INTERACTION WITH NCA1, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=25700484; DOI=10.1105/tpc.114.135095;
RA Li J., Liu J., Wang G., Cha J.Y., Li G., Chen S., Li Z., Guo J., Zhang C.,
RA Yang Y., Kim W.Y., Yun D.J., Schumaker K.S., Chen Z., Guo Y.;
RT "A chaperone function of NO CATALASE ACTIVITY1 is required to maintain
RT catalase activity and for multiple stress responses in Arabidopsis.";
RL Plant Cell 27:908-925(2015).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homotetramer and heterotetramer (PubMed:25700484). At least
CC six or seven isozymes are produced from a mixture of 3 gene products.
CC Interacts with NCA1 (PubMed:25700484). Interacts with LSD1
CC (PubMed:23958864). {ECO:0000269|PubMed:23958864,
CC ECO:0000269|PubMed:25700484}.
CC -!- INTERACTION:
CC Q42547; C1KKL7; Xeno; NbExp=4; IntAct=EBI-1537181, EBI-9078764;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:25700484}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42547-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:16502469}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF80611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U43147; AAC49807.1; -; Genomic_DNA.
DR EMBL; AF021937; AAC17732.1; -; Genomic_DNA.
DR EMBL; AC027665; AAF79625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069251; AAF80611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29995.1; -; Genomic_DNA.
DR EMBL; AY058104; AAL24212.1; -; mRNA.
DR EMBL; AY056447; AAL08303.1; -; mRNA.
DR EMBL; AY087477; AAM65021.1; -; mRNA.
DR PIR; S71112; S71112.
DR RefSeq; NP_564120.1; NM_101913.4. [Q42547-1]
DR AlphaFoldDB; Q42547; -.
DR SMR; Q42547; -.
DR BioGRID; 23890; 12.
DR IntAct; Q42547; 4.
DR STRING; 3702.AT1G20620.1; -.
DR PeroxiBase; 5143; AtKat03.
DR iPTMnet; Q42547; -.
DR PaxDb; Q42547; -.
DR PRIDE; Q42547; -.
DR ProteomicsDB; 223911; -. [Q42547-1]
DR EnsemblPlants; AT1G20620.1; AT1G20620.1; AT1G20620. [Q42547-1]
DR GeneID; 838651; -.
DR Gramene; AT1G20620.1; AT1G20620.1; AT1G20620. [Q42547-1]
DR KEGG; ath:AT1G20620; -.
DR Araport; AT1G20620; -.
DR TAIR; locus:2034357; AT1G20620.
DR eggNOG; KOG0047; Eukaryota.
DR PhylomeDB; Q42547; -.
DR PRO; PR:Q42547; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42547; baseline and differential.
DR Genevisible; Q42547; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004096; F:catalase activity; ISS:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; IDA:TAIR.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0009970; P:cellular response to sulfate starvation; IEP:TAIR.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IGI:TAIR.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
FT CHAIN 1..492
FT /note="Catalase-3"
FT /id="PRO_0000084932"
FT ACT_SITE 65
FT /evidence="ECO:0000250"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 109
FT /note="E -> G (in Ref. 2; AAC49807 and 3; AAC17732)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="P -> R (in Ref. 2; AAC49807 and 3; AAC17732)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="A -> V (in Ref. 7; AAM65021)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="I -> T (in Ref. 2; AAC49807 and 3; AAC17732)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..473
FT /note="SQ -> LK (in Ref. 2; AAC49807 and 3; AAC17732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56695 MW; 7322B111CFEBF37E CRC64;
MDPYKYRPSS AYNAPFYTTN GGAPVSNNIS SLTIGERGPV LLEDYHLIEK VANFTRERIP
ERVVHARGIS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVVHER ASPETMRDIR
GFAVKFYTRE GNFDLVGNNT PVFFIRDGIQ FPDVVHALKP NPKTNIQEYW RILDYMSHLP
ESLLTWCWMF DDVGIPQDYR HMEGFGVHTY TLIAKSGKVL FVKFHWKPTC GIKNLTDEEA
KVVGGANHSH ATKDLHDAIA SGNYPEWKLF IQTMDPADED KFDFDPLDVT KIWPEDILPL
QPVGRLVLNR TIDNFFNETE QLAFNPGLVV PGIYYSDDKL LQCRIFAYGD TQRHRLGPNY
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEI NYYPSKFDPV RCAEKVPTPT NSYTGIRTKC
VIKKENNFKQ AGDRYRSWAP DRQDRFVKRW VEILSEPRLT HEIRGIWISY WSQADRSLGQ
KLASRLNVRP SI
