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Q2PG53 (HMOX2_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 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 further processed into a mature form.
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

Protoheme + 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
   PTMAcetylation
Gene Ontology (GO)
   Biological_processheme oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 316315Heme oxygenase 2
PRO_0000317708

Regions

Repeat264 – 2696HRM 1
Repeat281 – 2866HRM 2

Sites

Metal binding451Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2PG53 [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

EMBL
GenBank
DDBJ
AB220384 mRNA. Translation: BAE72917.1.
RefSeqNP_001270155.1. NM_001283226.1.
UniGeneMfa.8715.

3D structure databases

ProteinModelPortalQ2PG53.
SMRQ2PG53. Positions 30-248.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ2PG53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102143766.
KEGGmcf:102143766.

Organism-specific databases

CTD3163.

Phylogenomic databases

HOVERGENHBG005982.
KOK00510.

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...

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: April 16, 2014
This is version 36 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