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Reviewed, UniProtKB/Swiss-Prot Q2PG53 (HMOX2_MACFA)

Last modified June 16, 2009. Version 17. 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
ORF Names: QbsB-11392
OrganismMacaca fascicularis (Crab eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length316 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 By similarity.

Catalytic activity

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

Subcellular location

Microsome. Endoplasmic reticulum By similarity.

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 – 316316Heme oxygenase 2
PRO_0000317708

Regions

Repeat264 – 2696HRM 1
Repeat281 – 2866HRM 2

Sites

Metal binding451Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2PG53-1 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 40A85866272B219E

FASTA31636,081
        10         20         30         40         50         60 
MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG 

        70         80         90        100        110        120 
NIKKELFKLA TTALYFTYSA LEEEMERNKD HPTFAPLYFP MELHRKEALT KDMEYFFGEN 

       130        140        150        160        170        180 
WEEQVQCPKA AKKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST 

       190        200        210        220        230        240 
GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA 

       250        260        270        280        290        300 
GSTLARETLE DGFPVHDGKG DMRKCPFYAG EQDKGALEGS SCPFRTAMAV LRKPSLQFIL 

       310 
AAGMALAAGL LAWYYM 

« Hide

References

[1]"Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA oligo-chips."
Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S., Hashimoto K.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain stem.

Cross-references

Sequence databases

AB220384 mRNA. Translation: BAE72917.1.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENQ2PG53.

Enzyme and pathway databases

BRENDA1.14.99.3. 3438.

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_MACFA
AccessionPrimary (citable) accession number: Q2PG53
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 7, 2006
Last modified: June 16, 2009
This is version 17 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