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Reviewed, UniProtKB/Swiss-Prot P43242 (HMOX2_RABIT)

Last modified June 16, 2009. Version 58. 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

Names and origin

Protein namesRecommended name:
    Heme oxygenase 2
      Short name=HO-2
    EC=1.14.99.3
Gene names
Name: HMOX2
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the heme oxygenase family.

Contains 2 HRM (heme regulatory motif) repeats.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Heme oxygenase 2
PRO_0000209693

Regions

Repeat260 – 2656HRM 1
Repeat277 – 2826HRM 2

Sites

Metal binding411Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P43242-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 2D33FF39FA1F5505

FASTA31235,373
        10         20         30         40         50         60 
MSAEVETSEG VDEPEEKNFG ENHIRMADLS ELLKEGTKEA HDRAENTKFV KDFLKGNIKK 

        70         80         90        100        110        120 
EIFKLATTAL YFTYSALEEE MDRNKDHPAF APLYFPMELH RKEALTKDME YFFGENWEEQ 

       130        140        150        160        170        180 
VQCSEAAQKY VERIHYIGQN EPELLVAHAY TRYMGDLSGG QVLKKVAQRA LKLPSTGEGT 

       190        200        210        220        230        240 
QFYLFENVDN AQQFKQFYRA RMNALDLNLK TKERIVEEAN KAFEYNMQIF SELDQAGSAP 

       250        260        270        280        290        300 
ASETVEDRIP VHDGKGDVRK CPYYAAGQVN GALEGSSCPF RAAMAVLRKP SLQLVLAAAV 

       310 
ALAAGLLAWY YM 

« Hide

References

[1]"Characterization of a cDNA-encoding rabbit brain heme oxygenase-2 and identification of a conserved domain among mammalian heme oxygenase isozymes: possible heme-binding site?"
Rotenberg M.O., Maines M.D.
Arch. Biochem. Biophys. 290:336-344(1991) [PubMed: 1929402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases

S61699 mRNA. Translation: AAB20093.1.
PIRS18387.
RefSeqNP_001076216.1.
UniGeneOcu.3307

3D structure databases

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

Genome annotation databases

EnsemblENSOCUG00000006018. Oryctolagus cuniculus. [Contig view]
GeneID100009523.

Phylogenomic databases

HOVERGENP43242.

Enzyme and pathway databases

BRENDA1.14.99.3. 255.

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...

Entry information

Entry nameHMOX2_RABIT
AccessionPrimary (citable) accession number: P43242
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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