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Reviewed, UniProtKB/Swiss-Prot P23711 (HMOX2_RAT)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Heme oxygenase 2
      Short name=HO-2
    EC=1.14.99.3
Gene names
Name: Hmox2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.

Catalytic activity

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

Subcellular location

Microsome. Endoplasmic reticulum.

Tissue specificity

Widely distributed in body with a high concentration in the brain.

Induction

Heme oxygenase 2 activity is non-inducible.

Sequence similarities

Belongs to the heme oxygenase family.

Contains 2 HRM (heme regulatory motif) repeats.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   DomainRepeat
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processheme oxidation

Traceable author statement. Source: RGD

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to oxidative stress

Inferred from direct assay. Source: RGD

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme oxygenase (decyclizing) activity Ref.1

Inferred from direct assay. Source: RGD

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Heme oxygenase 2
PRO_0000209694

Regions

Repeat263 – 2686HRM 1
Repeat280 – 2856HRM 2

Sites

Metal binding441Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict142 – 1465QNEPE → EFRNK in AAA41347. Ref.4
Sequence conflict230 – 2323MQI → TEF in AAA41347. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
P23711-1 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 981AADE01DE1AFCF

FASTA31535,762
        10         20         30         40         50         60 
MSSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN 

        70         80         90        100        110        120 
IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKEALIK DMEYFFGENW 

       130        140        150        160        170        180 
EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG 

       190        200        210        220        230        240 
EGTQFYLFEH VDNAQQFKQF YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG 

       250        260        270        280        290        300 
SMLTKETLED GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA 

       310 
ASVALVAGLL AWYYM

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References

« Hide 'large scale' references
[1]"Isolation, characterization, and expression in Escherichia coli of a cDNA encoding rat heme oxygenase-2."
Rotenberg M.O., Maines M.D.
J. Biol. Chem. 265:7501-7506(1990) [PubMed: 2185251] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"The structure, organization and differential expression of the gene encoding rat heme oxygenase-2."
McCoubrey W.K. Jr., Maines M.D.
Gene 139:155-161(1994) [PubMed: 8112599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[4]"Evidence suggesting that the two forms of heme oxygenase are products of different genes."
Cruse I., Maines M.D.
J. Biol. Chem. 263:3348-3353(1988) [PubMed: 3343248] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-232, PARTIAL PROTEIN SEQUENCE.
Tissue: Liver and Testis.

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Cross-references

Sequence databases

J05405 mRNA. Translation: AAA41340.1.
U05013 Genomic DNA. Translation: AAA19130.1.
BC062061 mRNA. Translation: AAH62061.1.
M18918 mRNA. Translation: AAA41347.1.
IPIIPI00213655.
PIRA35199.
RefSeqNP_077363.1.
UniGeneRn.10241

3D structure databases

HSSPHSSP built from PDB template 1DVG based on UniProtKB P06762.
ModBaseSearch...

Proteomic databases

PRIDEP23711.

Genome annotation databases

EnsemblENSRNOG00000003773. Rattus norvegicus. [Contig view]
GeneID79239.
KEGGrno:79239.

Organism-specific databases

RGD67402. Hmox2.

Phylogenomic databases

HOVERGENP23711.
OMAP23711. REGTKKS.

Enzyme and pathway databases

BRENDA1.14.99.3. 248.

Gene expression databases

ArrayExpressP23711.
GermOnlineENSRNOG00000003773. Rattus norvegicus.

Family and domain databases

InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
Gene3DG3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
PANTHERPTHR10720. Haem_Oase. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio614672.

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Entry information

Entry nameHMOX2_RAT
AccessionPrimary (citable) accession number: P23711
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents