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   16-JUN-2009, entry version 72.
DE   RecName: Full=Catalase-2;
DE            EC=1.11.1.6;
GN   Name=ctl-1; Synonyms=cat-2; ORFNames=Y54G11A.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Bristol N2;
RX   MEDLINE=99266878; PubMed=10335847; DOI=10.1038/20208;
RA   Taub J., Lau J.F., Ma C., Hahn J.H., Hoque R., Rothblatt J.,
RA   Chalfie M.;
RT   "A cytosolic catalase is needed to extend adult lifespan in C. elegans
RT   daf-C and clk-1 mutants.";
RL   Nature 399:162-166(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide. Responsible for the increase in catalase activity
CC       detected in dauer larvae. May act as a general scavenger of
CC       hydrogen peroxide in the cytosol, or it may protect cells from the
CC       effects of an unknown, dauer-specific metabolic process.
CC       Expression may be directly regulated by daf-16.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: With abundant food, the amount of ctl-1
CC       decreases slightly as worms mature.
CC   -!- INDUCTION: Overcrowding and depletion of food.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U55384; AAC14537.1; -; mRNA.
DR   EMBL; Y14066; CAA74394.1; -; mRNA.
DR   EMBL; Y14065; CAA74392.1; -; Genomic_DNA.
DR   EMBL; AL034488; CAA22458.2; -; Genomic_DNA.
DR   PIR; T37477; T37477.
DR   PIR; T42443; T42443.
DR   RefSeq; NP_496979.2; -.
DR   UniGene; Cel.34211; -.
DR   UniGene; Cel.34268; -.
DR   HSSP; P04040; 1F4J.
DR   Ensembl; Y54G11A.6; Caenorhabditis elegans.
DR   GeneID; 259738; -.
DR   KEGG; cel:Y54G11A.6; -.
DR   NMPDR; fig|6239.3.peg.8173; -.
DR   WormBase; WBGene00000830; ctl-1.
DR   WormPep; Y54G11A.6; CE30713.
DR   OMA; O61235; NENEQLA.
DR   BRENDA; 1.11.1.6; 672.
DR   NextBio; 952568; -.
DR   ArrayExpress; O61235; -.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0004096; F:catalase activity; IMP:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008340; P:determination of adult life span; IMP:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN         1    497       Catalase-2.
FT                                /FTId=PRO_0000084910.
FT   ACT_SITE     71     71       By similarity.
FT   ACT_SITE    144    144       By similarity.
FT   METAL       354    354       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     91     91       C -> G (in Ref. 1; AAC14537).
FT   CONFLICT     97     97       N -> H (in Ref. 1; AAC14537).
FT   CONFLICT    190    190       Missing (in Ref. 1; AAC14537).
FT   CONFLICT    237    237       G -> P (in Ref. 1; AAC14537).
FT   CONFLICT    270    270       F -> L (in Ref. 1; AAC14537).
FT   CONFLICT    282    282       F -> I (in Ref. 1; AAC14537).
FT   CONFLICT    310    310       G -> A (in Ref. 1; AAC14537).
FT   CONFLICT    313    313       V -> L (in Ref. 1; AAC14537).
FT   CONFLICT    385    386       DG -> EV (in Ref. 2; CAA74394/CAA74392).
FT   CONFLICT    394    395       GD -> EN (in Ref. 2; CAA74394/CAA74392).
FT   CONFLICT    399    399       Y -> S (in Ref. 2; CAA74394/CAA74392).
FT   CONFLICT    425    428       DRYE -> GSLW (in Ref. 1; AAC14537).
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
//