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P43242 (HMOX2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 81. 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length312 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.

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
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme oxidation

Inferred from electronic annotation. Source: InterPro

response to hypoxia

Inferred from electronic annotation. Source: Compara

   Cellular_componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Compara

   Molecular_functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: 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 – 312311Heme oxygenase 2
PRO_0000209693

Regions

Repeat260 – 2656HRM 1
Repeat277 – 2826HRM 2

Sites

Metal binding411Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P43242 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S61699 mRNA. Translation: AAB20093.1.
PIRS18387.
RefSeqNP_001076216.1. NM_001082747.1.
UniGeneOcu.3307.

3D structure databases

ProteinModelPortalP43242.
SMRP43242. Positions 26-244.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000005212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009523.

Organism-specific databases

CTD3163.

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
HOVERGENHBG005982.
OrthoDBEOG4RNB8T.

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. Heme_oxygenase. 1 hit.
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: April 3, 2013
This is version 81 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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