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P06762 (HMOX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme oxygenase 1

Short name=HO-1
EC=1.14.99.3
Alternative name(s):
HSP32
Gene names
Name:Hmox1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Catalytic activity

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Subcellular location

Microsome. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein; Cytoplasmic side.

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.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay PubMed 12593860. Source: RGD

cell death

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

cellular response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient

Inferred from expression pattern PubMed 15531134. Source: RGD

erythrocyte homeostasis

Inferred from electronic annotation. Source: Ensembl

heme catabolic process

Inferred from direct assay PubMed 15226268. Source: RGD

heme oxidation

Traceable author statement PubMed 12114196. Source: RGD

intracellular signal transduction

Inferred from direct assay PubMed 12225959. Source: RGD

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from direct assay PubMed 11854317. Source: RGD

iron ion homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA binding

Inferred from direct assay PubMed 17234154. Source: RGD

negative regulation of cell proliferation

Inferred from direct assay PubMed 16319139. Source: RGD

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell cytokine production

Inferred from direct assay PubMed 17234154. Source: RGD

negative regulation of mast cell degranulation

Inferred from direct assay PubMed 17234154. Source: RGD

negative regulation of muscle cell apoptotic process

Inferred from direct assay PubMed 12396617. Source: RGD

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 19177228. Source: RGD

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17234154. Source: RGD

negative regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 19885007. Source: RGD

phospholipid metabolic process

Traceable author statement PubMed 12511545. Source: RGD

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 20925964. Source: RGD

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from direct assay PubMed 12215473. Source: RGD

regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

response to estrogen

Inferred from direct assay PubMed 15734876. Source: RGD

response to hydrogen peroxide

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

response to hypoxia

Inferred from expression pattern PubMed 14970910. Source: RGD

response to nicotine

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from direct assay PubMed 17020887. Source: RGD

small GTPase mediated signal transduction

Inferred from direct assay PubMed 12511545. Source: RGD

wound healing involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from direct assay PubMed 15226268. Source: RGD

cytosol

Inferred from direct assay PubMed 14766239. Source: RGD

endoplasmic reticulum

Inferred from direct assay Ref.2. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay PubMed 14766239. Source: RGD

nucleus

Inferred from direct assay PubMed 17430897. Source: BHF-UCL

plasma membrane

Traceable author statement PubMed 12511545. Source: RGD

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 15516695. Source: BHF-UCL

heme binding

Inferred from direct assay PubMed 12044160. Source: RGD

heme oxygenase (decyclizing) activity

Inferred from direct assay Ref.2. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity

Inferred from direct assay PubMed 12114196. Source: RGD

phospholipase D activity

Inferred from direct assay PubMed 12511545. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Heme oxygenase 1
PRO_0000209690

Sites

Metal binding251Iron (heme axial ligand)
Binding site181Heme By similarity
Binding site1341Heme By similarity
Binding site1831Heme By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity

Secondary structure

.............................. 289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06762 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: EF7D2B98048AF44D

FASTA28933,006
        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 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and organization of the rat heme oxygenase gene."
Mueller R.M., Taguchi H., Shibahara S.
J. Biol. Chem. 262:6795-6802(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Cloning and expression of cDNA for rat heme oxygenase."
Shibahara S., Mueller R., Taguchi H., Yoshida T.
Proc. Natl. Acad. Sci. U.S.A. 82:7865-7869(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[4]"Crystal structure of rat heme oxygenase-1 in complex with heme."
Sugishima M., Omata Y., Kakuta Y., Sakamoto H., Noguchi M., Fukuyama K.
FEBS Lett. 471:61-66(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-267.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02722 Genomic DNA. Translation: AAA41346.1.
BC091164 mRNA. Translation: AAH91164.1.
PIROHRTD. A92645.
RefSeqNP_036712.1. NM_012580.2.
UniGeneRn.3160.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DVEX-ray2.40A1-267[»]
1DVGX-ray2.20A/B1-267[»]
1IRMX-ray2.55A/B/C1-267[»]
1IVJX-ray1.90A1-267[»]
1IX3X-ray2.00A1-267[»]
1IX4X-ray1.80A1-267[»]
1J02X-ray1.70A1-267[»]
1J2CX-ray2.40A1-267[»]
1UBBX-ray2.30A1-267[»]
1ULXX-ray2.00A1-267[»]
1VGIX-ray1.90A1-267[»]
2DY5X-ray2.70A1-267[»]
2E7EX-ray1.85A1-267[»]
2ZVUX-ray2.20A1-267[»]
3I9TX-ray2.15A1-261[»]
3I9UX-ray2.25A1-261[»]
3WKTX-ray4.30C/D1-267[»]
4G7LX-ray1.80A1-267[»]
4G7PX-ray1.90A1-267[»]
4G7TX-ray1.90A1-267[»]
4G7UX-ray1.90A1-267[»]
4G8PX-ray1.90A1-267[»]
4G8UX-ray2.10A1-267[»]
4G8WX-ray2.40A1-267[»]
4G98X-ray2.30A1-267[»]
4G99X-ray2.30A1-267[»]
ProteinModelPortalP06762.
SMRP06762. Positions 7-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246615. 1 interaction.
MINTMINT-4996356.
STRING10116.ENSRNOP00000019192.

Chemistry

BindingDBP06762.
ChEMBLCHEMBL5035.

PTM databases

PhosphoSiteP06762.

Proteomic databases

PaxDbP06762.
PRIDEP06762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117.
GeneID24451.
KEGGrno:24451.
UCSCRGD:2806. rat.

Organism-specific databases

CTD3162.
RGD2806. Hmox1.

Phylogenomic databases

eggNOGCOG5398.
GeneTreeENSGT00390000017673.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidP06762.
KOK00510.
OMAYAPLYFP.
OrthoDBEOG7JQBNR.
PhylomeDBP06762.
TreeFamTF314786.

Enzyme and pathway databases

SABIO-RKP06762.

Gene expression databases

GenevestigatorP06762.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06762.
NextBio603359.
PROP06762.

Entry information

Entry nameHMOX1_RAT
AccessionPrimary (citable) accession number: P06762
Secondary accession number(s): Q5BK87
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references