CATA_PIG
ID CATA_PIG Reviewed; 527 AA.
AC O62839; Q9TR38; Q9TR39;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=CAT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace; TISSUE=Liver;
RX PubMed=9475954; DOI=10.1023/a:1021865603981;
RA Lin Z.-H., Wang Y.-F., Sarai A., Yasue H.;
RT "Swine catalase deduced from cDNA and localization of the catalase gene on
RT swine chromosome 2p16-p15.";
RL Biochem. Genet. 35:297-302(1997).
RN [2]
RP PROTEIN SEQUENCE OF 20-38 AND 321-349.
RC TISSUE=Submandibular gland;
RX PubMed=7592879; DOI=10.1074/jbc.270.44.26577;
RA Thurin J., Blaszczyk-Thurin M.;
RT "Porcine submaxillary gland GDP-L-fucose: beta-D-galactoside alpha-2-L-
RT fucosyltransferase is likely a counterpart of the human Secretor gene-
RT encoded blood group transferase.";
RL J. Biol. Chem. 270:26577-26580(1995).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Promotes growth of cells.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25301.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D89812; BAA25301.1; ALT_FRAME; mRNA.
DR RefSeq; NP_999466.2; NM_214301.2.
DR STRING; 9823.ENSSSCP00000014135; -.
DR PeroxiBase; 5272; SscKat01.
DR PaxDb; O62839; -.
DR PeptideAtlas; O62839; -.
DR PRIDE; O62839; -.
DR GeneID; 397568; -.
DR KEGG; ssc:397568; -.
DR CTD; 847; -.
DR eggNOG; KOG0047; Eukaryota.
DR InParanoid; O62839; -.
DR OrthoDB; 507937at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; IBA:GO_Central.
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:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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 Acetylation; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Mitogen; NADP; Oxidoreductase; Peroxidase; Peroxisome;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT CHAIN 2..527
FT /note="Catalase"
FT /id="PRO_0000084903"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 358
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 221
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P24270"
FT MOD_RES 511
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04040"
SQ SEQUENCE 527 AA; 59883 MW; 20BC72D91893FFE9 CRC64;
MADNRDPASD QMKHWKEQRA AQKPDILTTG SGNPIGDKLN ILTAGPRGPL LVQDVVFTDE
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRFSKAKVF EHVGKRTPIA VRFSTVAGES
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNEKGEAV YCKFHYKTDQ
GIKNLSVEDA ARLPQEDPDY GIRDLFNAIA TGNYPSWTFY IQVMTFQEAE AFPFNPFDLT
KVWPHSEYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM LQGRLFGYPD
THRHRLGANY LQIPVNCPFR ARVANYQRDG PMCFQDNQGG APNYYPNSFS APEQTHSALE
HCTRYSGDVQ RFNSANEDNV TQVRTFYLNV LNEEERKRLC ENIAGHLKDA QLFIQKKAVK
NFSDVHPDYG ARIQALLDKY NAEXPENAVH TYVQAGSHLA AREKANL
