Reviewed, UniProtKB/Swiss-Prot P04040 (CATA_HUMAN)

Names and origin

Protein names

Recommended name:
    Catalase
    EC=1.11.1.6

Gene names

Name:

CAT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O.
Cofactor	Heme group. NADP.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Involvement in disease	Defects in CAT are the cause of acatalasia [MIM:115500]; also known as acatalasemia. This disease is characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	UV protection Inferred from mutant phenotype. Source: UniProtKB hydrogen peroxide catabolic process Inferred from direct assay. Source: UniProtKB negative regulation of apoptosis Inferred from mutant phenotype. Source: UniProtKB protein tetramerization Ref.12 Ref.13 Inferred from direct assay. Source: UniProtKB
Cellular component	peroxisomal membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NADP binding Ref.12 Inferred from direct assay. Source: UniProtKB catalase activity Inferred from direct assay. Source: UniProtKB heme binding Ref.12 Ref.13 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Ref.12 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 527

526

Catalase

Sites

Active site

75

1

Active site

148

1

Metal binding

358

1

Iron (heme axial ligand)

Amino acid modifications

Modified residue

422

1

Phosphoserine By similarity

Modified residue

517

1

Phosphoserine By similarity

Experimental info

Sequence conflict

54

1

D → N in AAK29181. Ref.3

Sequence conflict

239

1

D → G in AAK29181. Ref.3

Sequence conflict

274

1

Y → D in AAK29181. Ref.3

Sequence conflict

301

1

K → R in AAK29181. Ref.3

Sequence conflict

514

1

Q → R in AAK29181. Ref.3

Sequence conflict

520

1

A → V in AAK29181. Ref.3

Secondary structure

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527

Helix Strand Turn

Details...

Helix

7 – 10

4

Helix

11 – 17

7

Turn

18 – 21

4

Beta strand

38 – 40

3

Beta strand

42 – 45

4

Helix

55 – 64

10

Beta strand

77 – 87

11

Turn

92 – 94

3

Helix

98 – 100

3

Beta strand

106 – 114

9

Beta strand

116 – 118

3

Beta strand

124 – 128

5

Beta strand

131 – 138

8

Beta strand

141 – 151

11

Helix

158 – 160

3

Helix

161 – 168

8

Turn

172 – 174

3

Helix

179 – 188

10

Helix

190 – 192

3

Helix

193 – 199

7

Helix

202 – 204

3

Beta strand

205 – 209

5

Beta strand

220 – 223

4

Beta strand

229 – 238

10

Helix

247 – 256

10

Helix

260 – 270

11

Beta strand

276 – 284

9

Helix

286 – 291

6

Turn

305 – 307

3

Beta strand

311 – 320

10

Helix

325 – 328

4

Beta strand

343 – 345

3

Helix

349 – 365

17

Helix

370 – 372

3

Helix

374 – 376

3

Turn

397 – 400

4

Beta strand

404 – 406

3

Helix

416 – 418

3

Beta strand

424 – 431

8

Helix

441 – 449

9

Helix

453 – 467

15

Helix

472 – 485

14

Helix

487 – 500

14

Sequences

	Sequence		Length	Mass (Da)
	P04040-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 7BAA2394D124ED20	FASTA	527	59,756
	10 20 30 40 50 60 MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE 70 80 90 100 110 120 MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES 130 140 150 160 170 180 GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD 190 200 210 220 230 240 MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 250 260 270 280 290 300 GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT 310 320 330 340 350 360 KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD 370 380 390 400 410 420 THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE 430 440 450 460 470 480 HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK 490 500 510 520 NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the human catalase gene." Quan F., Korneluk R.G., Tropak M.B., Gravel R.A. Nucleic Acids Res. 14:5321-5335(1986) [PubMed: 3755525] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"cDNA sequence coding for human kidney catalase." Bell G.I., Najarian R.C., Mullenbach G.T., Hallewell R.A. Nucleic Acids Res. 14:5561-5562(1986) [PubMed: 3755526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Transduction of human catalase mediated by an HIV-1 TAT protein basic domain and arginine-rich peptides into mammalian cells." Jin L.H., Bahn J.H., Eum W.S., Kwon H.Y., Jang S.H., Han K.H., Kang T.C., Won M.H., Kang J.H., Cho S.W., Park J., Choi S.Y. Free Radic. Biol. Med. 31:1509-1519(2001) [PubMed: 11728823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	SeattleSNPs program for genomic applications Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum and Eye.
[7]	"Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress." Yoo J.-H., Erzurum S.C., Hay J.G., Lemarchand P., Crystal R.G. J. Clin. Invest. 93:297-302(1994) [PubMed: 8282800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-22.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19. Tissue: Platelet.
[9]	"Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA." Korneluk R.G., Quan F., Lewis W.H., Guise K.S., Willard H.F., Holmes M.T., Gravel R.A. J. Biol. Chem. 259:13819-13823(1984) [PubMed: 6548744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-527. Tissue: Fibroblast.
[10]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 445-456, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[11]	"Structure of human erythrocyte catalase." Ko T.P., Safo M.K., Musayev F.N., Di Salvo M.L., Wang C., Wu S.H., Abraham D.J. Acta Crystallogr. D 56:241-245(2000) [PubMed: 10666617] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[12]	"Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism." Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A. J. Mol. Biol. 296:295-309(2000) [PubMed: 10656833] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[13]	"Structure of tetragonal crystals of human erythrocyte catalase." Safo M.K., Musayev F.N., Wu S.H., Abraham D.J., Ko T.P. Acta Crystallogr. D 57:1-7(2001) [PubMed: 11134921] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Web resources

Wikipedia

Catalase entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04085 , X04086, X04087, X04088, X04089, X04090, X04091, X04092, X04093, X04094, X04095, X04096 Genomic DNA. Translation: CAA27721.1.
X04076 mRNA. Translation: CAA27717.1.
AY028632 mRNA. Translation: AAK29181.1.
AY545477 Genomic DNA. Translation: AAS37679.1.
AL035079 Genomic DNA. Translation: CAB45236.1.
BC110398 mRNA. Translation: AAI10399.1.
BC112217 mRNA. Translation: AAI12218.1.
BC112219 mRNA. Translation: AAI12220.1.
L13609 Unassigned DNA. Translation: AAA16651.1.
K02400 Genomic DNA. Translation: AAB59522.1.

PIR

CSHU. A23646.

RefSeq

NP_001743.1.

UniGene

Hs.502302

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DGB	X-ray	2.20	A/B/C/D	4-501	[»]
1DGF