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UniProtKB/Swiss-Prot entry P06762

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HMOX1_RAT
Primary accession number P06762
Secondary accession number Q5BK87
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 77)
Name and origin of the protein
Protein name Heme oxygenase 1
Synonyms HO-1
EC 1.14.99.3
HSP32
Gene name
Name: Hmox1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3032976 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller R.M., Taguchi H., Shibahara S.;
"Nucleotide sequence and organization of the rat heme oxygenase gene.";
J. Biol. Chem. 262:6795-6802(1987).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3865203 [NCBI, ExPASy, EBI, Israel, Japan]
Shibahara S., Mueller R., Taguchi H., Yoshida T.;
"Cloning and expression of cDNA for rat heme oxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 82:7865-7869(1985).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-267.
DOI=10.1016/S0014-5793(00)01353-3; PubMed=10760513 [NCBI, ExPASy, EBI, Israel, Japan]
Sugishima M., Omata Y., Kakuta Y., Sakamoto H., Noguchi M., Fukuyama K.;
"Crystal structure of rat heme oxygenase-1 in complex with heme.";
FEBS Lett. 471:61-66(2000).
Comments
  • FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
  • CATALYTIC ACTIVITY: Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.
  • SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum.
  • INDUCTION: Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin.
  • SIMILARITY: Belongs to the heme oxygenase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J02722; AAA41346.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC091164; AAH91164.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A92645; OHRTD.
RefSeq NP_036712.1; -.
UniGene Rn.3160
3D structure databases
PDB
1DVE; X-ray; 2.40 A; A=1-267.[ExPASy / RCSB / EBI]
1DVG; X-ray; 2.20 A; A/B=1-267.[ExPASy / RCSB / EBI]
1IRM; X-ray; 2.55 A; A/B/C=1-267.[ExPASy / RCSB / EBI]
1IVJ; X-ray; 1.90 A; A=1-267.[ExPASy / RCSB / EBI]
1IX3; X-ray; 2.00 A; A=1-267.[ExPASy / RCSB / EBI]
1IX4; X-ray; 1.80 A; A=1-267.[ExPASy / RCSB / EBI]
1J02; X-ray; 1.70 A; A=1-267.[ExPASy / RCSB / EBI]
1J2C; X-ray; 2.40 A; A=1-267.[ExPASy / RCSB / EBI]
1UBB; X-ray; 2.30 A; A=1-267.[ExPASy / RCSB / EBI]
1ULX; X-ray; 2.00 A; A=1-267.[ExPASy / RCSB / EBI]
1VGI; X-ray; 1.90 A; A=1-267.[ExPASy / RCSB / EBI]
2DY5; X-ray; 2.70 A; A=1-267.[ExPASy / RCSB / EBI]
2E7E; X-ray; 1.85 A; A=1-267.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DVE; -.
1DVG; -.
1IRM; -.
1IVJ; -.
1IX3; -.
1IX4; -.
1J02; -.
1J2C; -.
1UBB; -.
1ULX; -.
1VGI; -.
2DY5; -.
2E7E; -.
ModBase P06762.
PTM databases
PhosphoSite P06762; -.
Organism-specific databases
RGD 2806; Hmox1.
Gene expression databases
ArrayExpress P06762; -.
GermOnline ENSRNOG00000014117; Rattus norvegicus.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from UniProtKB).
GO:0005792; Cellular component: microsome (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0004392; Molecular function: heme oxygenase (decyclizing) activity (inferred from direct assay from UniProtKB).
GO:0008219; Biological process: cell death (inferred from direct assay from UniProtKB).
GO:0051090; Biological process: regulation of transcription factor activity (inferred from direct assay from UniProtKB).
GO:0043619; Biological process: regulation of transcription from RNA polymerase II promoter in response to oxidative stress (inferred from direct assay from UniProtKB).
GO:0042542; Biological process: response to hydrogen peroxide (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002051; Haem_Oase.
IPR016053; Haem_Oase-like.
IPR016084; Haem_Oase-like_multi-hlx.
Graphical view of domain structure.
Gene3D G3DSA:1.20.910.10; Haem_Oase-like_multi-hlx; 1.
PANTHER PTHR10720; Haem_Oase; 1.
Pfam PF01126; Heme_oxygenase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000343; Haem_Oase; 1.
PRINTS PR00088; HAEMOXYGNASE.
PROSITE PS00593; HEME_OXYGENASE; 1.
BLOCKS P06762.
ProtoNet P06762.
Genome annotation databases
Ensembl ENSRNOG00000014117; Rattus norvegicus. [Contig view]
GeneID 24451; -.
KEGG rno:24451; -.
NMPDR fig|10116.3.peg.14608; -.
Phylogenomic databases
HOVERGEN P06762; -.
Other
NextBio 603359; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   289  289     Heme oxygenase 1. PRO_0000209690
METAL   25    25        Iron (heme axial ligand). 
MOD_RES   229   229        Phosphoserine (By similarity). 
HELIX   13    29  17      
HELIX   32    38  7      
HELIX   44    68  25      
TURN   72    74  3      
HELIX   75    77  3      
TURN   80    83  4      
HELIX   86    97  12      
HELIX   101   104  4      
HELIX   109   124  16      
HELIX   126   128  3      
HELIX   129   140  12      
HELIX   143   155  13      
HELIX   165   167  3      
HELIX   175   186  12      
HELIX   193   222  30      
Sequence information
Length: 289 AA [This is the length of the unprocessed precursor] Molecular weight: 33006 Da [This is the MW of the unprocessed precursor] CRC64: EF7D2B98048AF44D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV MASLYHIYTA 

        70         80         90        100        110        120 
LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEAIPYTPA TQHYVKRLHE 

       130        140        150        160        170        180 
VGGTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ 

       190        200        210        220        230        240 
LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP 

       250        260        270        280 
ASLVQDTTSA ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM
P06762 in FASTA format

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