ID CATA1_CAEEL Reviewed; 500 AA.
AC Q27487; O18192; Q9XVZ5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Peroxisomal catalase 1;
DE EC=1.11.1.6 {ECO:0000269|PubMed:10691967, ECO:0000269|PubMed:14996832};
DE AltName: Full=Catalase-2 {ECO:0000303|PubMed:10691967};
GN Name=ctl-2 {ECO:0000312|WormBase:Y54G11A.5};
GN Synonyms=cat {ECO:0000312|WormBase:Y54G11A.5},
GN cat-1 {ECO:0000312|WormBase:Y54G11A.5};
GN ORFNames=Y54G11A.5 {ECO:0000312|WormBase:Y54G11A.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Henkle-Duehrsen K.J.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RA Eckelt V.H.O.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP RETRACTED PAPER.
RC STRAIN=Bristol N2;
RX PubMed=10335847; DOI=10.1038/20208;
RA Taub J., Lau J.F., Ma C., Hahn J.H., Hoque R., Rothblatt J., Chalfie M.;
RT "A cytosolic catalase is needed to extend adult lifespan in C. elegans daf-
RT C and clk-1 mutants.";
RL Nature 399:162-166(1999).
RN [5]
RP RETRACTION NOTICE OF PUBMED:10335847.
RX PubMed=12610632; DOI=10.1038/nature01425;
RA Taub J., Lau J.F., Ma C., Hahn J.H., Hoque R., Rothblatt J., Chalfie M.;
RL Nature 421:764-764(2003).
RN [6]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10691967; DOI=10.1046/j.1432-1327.2000.01091.x;
RA Togo S.H., Maebuchi M., Yokota S., Bun-Ya M., Kawahara A., Kamiryo T.;
RT "Immunological detection of alkaline-diaminobenzidine-negative peroxisomes
RT of the nematode Caenorhabditis elegans. Purification and unique pH optima
RT of peroxisomal catalase.";
RL Eur. J. Biochem. 267:1307-1312(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14996832; DOI=10.1074/jbc.m400207200;
RA Petriv O.I., Rachubinski R.A.;
RT "Lack of peroxisomal catalase causes a progeric phenotype in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 279:19996-20001(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17483415; DOI=10.1534/genetics.107.072587;
RA Chavez V., Mohri-Shiomi A., Maadani A., Vega L.A., Garsin D.A.;
RT "Oxidative stress enzymes are required for DAF-16-mediated immunity due to
RT generation of reactive oxygen species by Caenorhabditis elegans.";
RL Genetics 176:1567-1577(2007).
RN [9]
RP FUNCTION, AND INDUCTION BY COPPER.
RX PubMed=25243607; DOI=10.1371/journal.pone.0107685;
RA Song S., Zhang X., Wu H., Han Y., Zhang J., Ma E., Guo Y.;
RT "Molecular basis for antioxidant enzymes in mediating copper detoxification
RT in the nematode Caenorhabditis elegans.";
RL PLoS ONE 9:E107685-E107685(2014).
RN [10]
RP FUNCTION, AND INDUCTION BY PESTICIDES.
RX PubMed=28456303; DOI=10.1016/j.pestbp.2017.02.005;
RA Han Y., Song S., Wu H., Zhang J., Ma E.;
RT "Antioxidant enzymes and their role in phoxim and carbaryl stress in
RT Caenorhabditis elegans.";
RL Pestic. Biochem. Physiol. 138:43-50(2017).
CC -!- FUNCTION: Peroxisomal catalase involved in the oxidative stress
CC response serving to protect cells from toxicity (PubMed:25243607,
CC PubMed:28456303). Plays a role in maintaining normal lifespan
CC (PubMed:14996832). Plays a role in regulating the response to pathogens
CC such as E.faecalis (PubMed:17483415). {ECO:0000269|PubMed:14996832,
CC ECO:0000269|PubMed:17483415, ECO:0000269|PubMed:25243607,
CC ECO:0000269|PubMed:28456303}.
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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10013,
CC ECO:0000269|PubMed:10691967, ECO:0000269|PubMed:14996832};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:10691967};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10691967}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10691967}.
CC -!- INDUCTION: Up-regulated in response to Cu(2+) (PubMed:25243607). Up-
CC regulated in response to phoxim (an organophosphorus insecticide) and
CC carbaryl (a carbamate insecticide) (PubMed:28456303).
CC {ECO:0000269|PubMed:25243607, ECO:0000269|PubMed:28456303}.
CC -!- DISRUPTION PHENOTYPE: Shortened lifespan and reduced egg laying
CC capacity (PubMed:14996832). Abolishes ctl-2 enzymatic activity and
CC reduces the global levels of catalase activity to 20% of the total
CC catalase activity observed in wild-type animals (PubMed:14996832).
CC Increased size and clustering of peroxisomes (PubMed:14996832).
CC Increased sensitivity to pathogens (PubMed:17483415). Reduced survival
CC and resistance to E.faecalis in a daf-2 RNAi mutant background
CC (PubMed:17483415). {ECO:0000269|PubMed:14996832,
CC ECO:0000269|PubMed:17483415}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- CAUTION: Was originally reported to play a role in determining adult
CC lifespan. However, the paper was later retracted due to errors in the
CC data. {ECO:0000305|PubMed:10335847, ECO:0000305|PubMed:12610632}.
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DR EMBL; X82175; CAA57665.1; -; mRNA.
DR EMBL; Y14065; CAA74393.1; -; Genomic_DNA.
DR EMBL; BX284602; CAA22451.1; -; Genomic_DNA.
DR PIR; T27177; T27177.
DR RefSeq; NP_001022473.1; NM_001027302.5.
DR AlphaFoldDB; Q27487; -.
DR SMR; Q27487; -.
DR BioGRID; 40366; 59.
DR STRING; 6239.Y54G11A.5.2; -.
DR EPD; Q27487; -.
DR PaxDb; 6239-Y54G11A-5-1; -.
DR PeptideAtlas; Q27487; -.
DR EnsemblMetazoa; Y54G11A.5.1; Y54G11A.5.1; WBGene00000831.
DR GeneID; 175085; -.
DR KEGG; cel:CELE_Y54G11A.5; -.
DR UCSC; Y54G11A.5.1; c. elegans.
DR AGR; WB:WBGene00000831; -.
DR WormBase; Y54G11A.5; CE22476; WBGene00000831; ctl-2.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; Q27487; -.
DR OMA; KFRWNVF; -.
DR OrthoDB; 3198922at2759; -.
DR PhylomeDB; Q27487; -.
DR PRO; PR:Q27487; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000831; Expressed in larva and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:WormBase.
DR GO; GO:0004096; F:catalase activity; IDA:WormBase.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IDA:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IMP:WormBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08156; catalase_clade_3; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
DR InterPro; IPR024708; Catalase_AS.
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; CATALASE; 1.
DR PANTHER; PTHR11465:SF25; PEROXISOMAL CATALASE 1; 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; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Peroxisome; Reference proteome.
FT CHAIN 1..500
FT /note="Peroxisomal catalase 1"
FT /id="PRO_0000084909"
FT MOTIF 498..500
FT /note="Microbody targeting signal"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 354
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 325..327
FT /note="Missing (in Ref. 2; CAA74393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 57467 MW; B9A705148C059034 CRC64;
MPNDPSDNQL KTYKETYPKP QVITTSNGAP IYSKTAVLTA GRRGPMLMQD VVYMDEMAHF
DRERIPERVV HAKGAGAHGY FEVTHDISKY CKADIFNKVG KQTPLLIRFS TVGGESGSAD
TARDPRGFAI KFYTEEGNWD LVGNNTPIFF IRDPIHFPNF IHTQKRNPQT HLKDPNMIFD
FWLHRPEALH QVMFLFSDRG LPDGYRHMNG YGSHTFKMVN KDGKAIYVKF HFKPTQGVKN
LTVEKAGQLA SSDPDYSIRD LFNAIEKGDF PVWKMFIQVM TFEQAEKWEF NPFDVTKVWP
HGDYPLIEVG KMVLNRNPRN YFAEVEQSAF CPAHIVPGIE FSPDKMLQGR IFSYTDTHFH
RLGPNYIQLP VNCPYRSRAH NTQRDGAMAY DNQQHAPNFF PNSFNYGKTR PDVKDTTFPA
TGDVDRYESG DDNNYDQPRQ FWEKVLDTGA RERMCQNFAG PLGECHDFII KGMIDHFSKV
HPDFGARVKA LIQKQARSHI
//
