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Protein

Catalase

Gene

CAT

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751PROSITE-ProRule annotation
Active sitei148 – 1481PROSITE-ProRule annotation
Metal bindingi358 – 3581Iron (heme axial ligand)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Protein family/group databases

PeroxiBasei5272. SscKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:CAT
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 527526CatalasePRO_0000084903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei221 – 2211N6-succinyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei417 – 4171PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei511 – 5111PhosphothreonineBy similarity
Modified residuei517 – 5171PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO62839.
PRIDEiO62839.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000014135.

Structurei

3D structure databases

ProteinModelPortaliO62839.
SMRiO62839. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiO62839.
KOiK03781.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O62839-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNRDPASD QMKHWKEQRA AQKPDILTTG SGNPIGDKLN ILTAGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRFSKAKVF
110 120 130 140 150
EHVGKRTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNEKGEAV YCKFHYKTDQ GIKNLSVEDA
260 270 280 290 300
ARLPQEDPDY GIRDLFNAIA TGNYPSWTFY IQVMTFQEAE AFPFNPFDLT
310 320 330 340 350
KVWPHSEYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFGYPD THRHRLGANY LQIPVNCPFR ARVANYQRDG PMCFQDNQGG
410 420 430 440 450
APNYYPNSFS APEQTHSALE HCTRYSGDVQ RFNSANEDNV TQVRTFYLNV
460 470 480 490 500
LNEEERKRLC ENIAGHLKDA QLFIQKKAVK NFSDVHPDYG ARIQALLDKY
510 520
NAEXPENAVH TYVQAGSHLA AREKANL
Length:527
Mass (Da):59,883
Last modified:January 23, 2007 - v4
Checksum:i20BC72D91893FFE9
GO

Sequence cautioni

The sequence BAA25301.1 differs from that shown. Reason: Frameshift at position 504. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89812 mRNA. Translation: BAA25301.1. Frameshift.
RefSeqiNP_999466.2. NM_214301.2.
UniGeneiSsc.1018.

Genome annotation databases

GeneIDi397568.
KEGGissc:397568.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89812 mRNA. Translation: BAA25301.1. Frameshift.
RefSeqiNP_999466.2. NM_214301.2.
UniGeneiSsc.1018.

3D structure databases

ProteinModelPortaliO62839.
SMRiO62839. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000014135.

Protein family/group databases

PeroxiBasei5272. SscKat01.

Proteomic databases

PaxDbiO62839.
PRIDEiO62839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397568.
KEGGissc:397568.

Organism-specific databases

CTDi847.

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiO62839.
KOiK03781.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Swine catalase deduced from cDNA and localization of the catalase gene on swine chromosome 2p16-p15."
    Lin Z.-H., Wang Y.-F., Sarai A., Yasue H.
    Biochem. Genet. 35:297-302(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Landrace.
    Tissue: Liver.
  2. "Porcine submaxillary gland GDP-L-fucose: beta-D-galactoside alpha-2-L-fucosyltransferase is likely a counterpart of the human Secretor gene-encoded blood group transferase."
    Thurin J., Blaszczyk-Thurin M.
    J. Biol. Chem. 270:26577-26580(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-38 AND 321-349.
    Tissue: Submandibular gland.

Entry informationi

Entry nameiCATA_PIG
AccessioniPrimary (citable) accession number: O62839
Secondary accession number(s): Q9TR38, Q9TR39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 104 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.