CATA2_CAEEL
ID CATA2_CAEEL Reviewed; 497 AA.
AC O61235; O18193; Q9XVZ4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Catalase-2;
DE EC=1.11.1.6 {ECO:0000269|PubMed:14996832};
GN Name=ctl-1 {ECO:0000312|WormBase:Y54G11A.6};
GN Synonyms=cat-2 {ECO:0000312|WormBase:Y54G11A.6};
GN ORFNames=Y54G11A.6 {ECO:0000312|WormBase:Y54G11A.6};
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 [GENOMIC DNA / MRNA].
RC STRAIN=Bristol N2;
RA Eckelt V.H.O.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=18077412; DOI=10.1073/pnas.0707393104;
RA Blaise B.J., Giacomotto J., Elena B., Dumas M.E., Toulhoat P., Segalat L.,
RA Emsley L.;
RT "Metabotyping of Caenorhabditis elegans reveals latent phenotypes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19808-19812(2007).
RN [7]
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 [8]
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: Catalase involved in the oxidative stress response serving to
CC protect cells from toxicity (Probable) (PubMed:25243607,
CC PubMed:28456303). For instance plays a role in defending against
CC oxidative damage induced by excessive copper stress (PubMed:25243607).
CC Not required for maintaining normal lifespan (PubMed:14996832).
CC {ECO:0000269|PubMed:14996832, ECO:0000269|PubMed:25243607,
CC ECO:0000269|PubMed:28456303, ECO:0000305|PubMed:18077412}.
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:14996832};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
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: No defects in lifespan or egg laying capacity
CC (PubMed:14996832). Abolishes ctl-1 enzymatic activity and reduces the
CC global levels of catalase activity to 75% of the total catalase
CC activity observed in wild-type animals (PubMed:14996832).
CC {ECO:0000269|PubMed:14996832}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC14537.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; U55384; AAC14537.1; ALT_SEQ; mRNA.
DR EMBL; Y14066; CAA74394.1; -; mRNA.
DR EMBL; Y14065; CAA74392.1; -; Genomic_DNA.
DR EMBL; BX284602; CAA22458.2; -; Genomic_DNA.
DR PIR; T37477; T37477.
DR PIR; T42443; T42443.
DR RefSeq; NP_496979.2; NM_064578.4.
DR AlphaFoldDB; O61235; -.
DR SMR; O61235; -.
DR BioGRID; 56780; 4.
DR STRING; 6239.Y54G11A.6; -.
DR PeroxiBase; 8429; CelKat01.
DR EPD; O61235; -.
DR PaxDb; O61235; -.
DR PeptideAtlas; O61235; -.
DR PRIDE; O61235; -.
DR EnsemblMetazoa; Y54G11A.6.1; Y54G11A.6.1; WBGene00000830.
DR GeneID; 259738; -.
DR KEGG; cel:CELE_Y54G11A.6; -.
DR UCSC; B0432.5a; c. elegans.
DR CTD; 259738; -.
DR WormBase; Y54G11A.6; CE30713; WBGene00000830; ctl-1.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; O61235; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR PhylomeDB; O61235; -.
DR PRO; PR:O61235; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000830; Expressed in larva and 3 other 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; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IMP: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:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR CDD; cd08156; catalase_clade_3; 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; 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; 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 Reference proteome.
FT CHAIN 1..497
FT /note="Catalase-2"
FT /id="PRO_0000084910"
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 385..386
FT /note="DG -> EV (in Ref. 1; CAA74394/CAA74392)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="GD -> EN (in Ref. 1; CAA74394/CAA74392)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Y -> S (in Ref. 1; CAA74394/CAA74392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 57305 MW; 26662FE6EF38CCE5 CRC64;
MPNDPSDNQL KTYKETYPKP QVITTSNGAP IYSKTAVLTA GRRGPMLMQD VVYMDEMAHF
DRERIPERVV HAKGAGAHGY FEVTHDITKY CKADMFNKVG KQTPLLVRFS TVAGESGSAD
TVRDPRGFSL KFYTEEGNWD LVGNNTPIFF IRDAIHFPNF IHALKRNPQT HMRDPNALFD
FWMNRPESIH QVMFLYSDRG IPDGFRFMNG YGAHTFKMVN KEGNPIYCKF HFKPAQGSKN
LDPTDAGKLA SSDPDYAIRD LFNAIESRNF PEWKMFIQVM TFEQAEKWEF NPFDVTKVWP
HGDYPLIEVG KMVLNRNVKN YFAEVEQAAF CPAHIVPGIE FSPDKMLQGR IFSYTDTHYH
RLGPNYIQLP VNCPYRSRAH TTQRDGAMAY ESQGDAPNYF PNSFRGYRTR DDVKESTFQT
TGDVDRYETG DDHNYEQPRQ FWEKVLKEEE RDRLVGNLAS DLGGCLEEIQ NGMVKEFTKV
HPDFGNALRH QLCQKKH
