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O97492

- CATA_CANFA

UniProt

O97492 - CATA_CANFA

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Protein

Catalase

Gene

CAT

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - 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

  1. catalase activity Source: UniProtKB-EC
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
  2. positive regulation of cell division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_174045. Detoxification of Reactive Oxygen Species.
REACT_250585. Purine catabolism.

Protein family/group databases

PeroxiBasei5319. CfaKat01.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:CAT
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 18

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Defects in CAT are the cause of acatalasia; also known as acatalasemia. This disease is characterized by absence of catalase activity.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 527526CatalasePRO_0000084899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei221 – 2211N6-succinyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei449 – 4491N6-acetyllysine; alternateBy similarity
Modified residuei449 – 4491N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO97492.
PRIDEiO97492.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000010324.

Structurei

3D structure databases

ProteinModelPortaliO97492.
SMRiO97492. Positions 4-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiO97492.
KOiK03781.
OMAiNASQFIQ.
OrthoDBiEOG7V7660.
TreeFamiTF300540.

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.

O97492-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADSRDPASD QMKLWKEQRA AQKPDVLTTG GGNPIGDKLN VMTAGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF
110 120 130 140 150
EHIGKRTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDAIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNAAGEAV YCKFHYKTDQ GIKNLSVEDA
260 270 280 290 300
ARLSHEDPDY GLRDLFNAIA TGNYPSWTFY IQVMTFSQAE TFPFNPFDLT
310 320 330 340 350
KIWPHQDYPL IPVGKLVLNR NPVNYFAEVE QMAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LQIPVNCPFR ARVANYQRDG PMCMLDNQGG
410 420 430 440 450
APNYYPNSFS APEQQRCVLE HSSQCSPDVQ RFNSANEDNV TQVRTFYLKV
460 470 480 490 500
LGEEERKRLC ENIAGHLKDA QLFIQKKAVK NFSDVHPDYG ARIQALLDKY
510 520
NAEKPKNAIH TFMQHGSHLA AREKANL
Length:527
Mass (Da):59,797
Last modified:January 23, 2007 - v3
Checksum:iCC0BC7F88FE2C2AC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti327 – 3271A → T in acatalasemia; heat-labile. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012918 mRNA. Translation: BAA36420.1.
AB038231 mRNA. Translation: BAB20764.1.
RefSeqiNP_001002984.1. NM_001002984.1.
UniGeneiCfa.188.

Genome annotation databases

EnsembliENSCAFT00000011146; ENSCAFP00000010324; ENSCAFG00000006941.
GeneIDi403474.
KEGGicfa:403474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012918 mRNA. Translation: BAA36420.1 .
AB038231 mRNA. Translation: BAB20764.1 .
RefSeqi NP_001002984.1. NM_001002984.1.
UniGenei Cfa.188.

3D structure databases

ProteinModelPortali O97492.
SMRi O97492. Positions 4-501.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000010324.

Protein family/group databases

PeroxiBasei 5319. CfaKat01.

Proteomic databases

PaxDbi O97492.
PRIDEi O97492.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000011146 ; ENSCAFP00000010324 ; ENSCAFG00000006941 .
GeneIDi 403474.
KEGGi cfa:403474.

Organism-specific databases

CTDi 847.

Phylogenomic databases

eggNOGi COG0753.
GeneTreei ENSGT00390000018100.
HOGENOMi HOG000087852.
HOVERGENi HBG003986.
InParanoidi O97492.
KOi K03781.
OMAi NASQFIQ.
OrthoDBi EOG7V7660.
TreeFami TF300540.

Enzyme and pathway databases

Reactomei REACT_174045. Detoxification of Reactive Oxygen Species.
REACT_250585. Purine catabolism.

Miscellaneous databases

NextBioi 20816990.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "cDNA and deduced amino acid sequences of dog catalase."
    Nakamura K., Watanabe M., Ikeda T.
    DNA Seq. 9:347-352(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Beagle.
    Tissue: Liver.
  2. "cDNA cloning of mutant catalase in acatalasemic beagle dog: single nucleotide substitution leading to thermal-instability and enhanced proteolysis of mutant enzyme."
    Nakamura K., Watanabe M., Takanaka K., Sasaki Y., Ikeda T.
    Int. J. Biochem. Cell Biol. 32:1183-1193(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ACATALASEMIA THR-327.
    Strain: Beagle.

Entry informationi

Entry nameiCATA_CANFA
AccessioniPrimary (citable) accession number: O97492
Secondary accession number(s): Q9GKY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3