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P23711 (HMOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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

Protein attributes

Sequence length315 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALMP621573EBI-2910092,EBI-397403From a different organism.
Calm1P621612EBI-2910092,EBI-397530

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 315314Heme oxygenase 2
PRO_0000209694

Regions

Repeat263 – 2686HRM 1
Repeat280 – 2856HRM 2

Sites

Metal binding441Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
P23711 [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

« Hide

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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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. NM_024387.1.
UniGeneRn.10241.

3D structure databases

ProteinModelPortalP23711.
SMRP23711. Positions 29-247.
ModBaseSearch...

Protein-protein interaction databases

IntActP23711. 2 interactions.
STRINGP23711.

Proteomic databases

PRIDEP23711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005031; ENSRNOP00000005031; ENSRNOG00000003773.
GeneID79239.
KEGGrno:79239.
UCSCNM_024387. rat.

Organism-specific databases

CTD3163.
RGD67402. Hmox2.

Phylogenomic databases

eggNOGroNOG10441.
GeneTreeENSGT00390000017673.
HOVERGENHBG005982.
InParanoidP23711.
OMAREGTKKS.
OrthoDBEOG4RNB8T.
PhylomeDBP23711.

Gene expression databases

ArrayExpressP23711.
GenevestigatorP23711.
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.
KOK00510.
PANTHERPTHR10720. Haem_Oase. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. Heme_oxygenase. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614672.

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: December 14, 2011
This is version 95 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

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