Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5R7E3 (HMOX1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 46. 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
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 1
Short name=HO-1
EC=1.14.99.3
Gene names
Name:HMOX1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
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 By similarity.

Catalytic activity

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

Subcellular location

Microsome By similarity. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein; Cytoplasmic side.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain1 – 288288Heme oxygenase 1
PRO_0000317707

Sites

Metal binding251Iron (heme axial ligand)
Binding site181Heme By similarity
Binding site1341Heme By similarity
Binding site1831Heme By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R7E3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 10400CCCCA98F7F3

FASTA28832,712
        10         20         30         40         50         60 
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTREGFKLV MASLYHIYVA 

        70         80         90        100        110        120 
LEEEIEHNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE 

       130        140        150        160        170        180 
VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALGLPSS GEGLAFFTFP NIASATKFKQ 

       190        200        210        220        230        240 
LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA 

       250        260        270        280 
SNKAQDSAPV ETPRGKTPLN THSQAPLLRW VLTLSFLVAT VAVGLYAM

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR860175 mRNA. Translation: CAH92317.1.
RefSeqNP_001126358.1. NM_001132886.1.
UniGenePab.18812.

3D structure databases

HSSPHSSP built from PDB template 1T5P based on UniProtKB P09601.
ProteinModelPortalQ5R7E3.
SMRQ5R7E3. Positions 1-223.
ModBaseSearch...

Proteomic databases

PRIDEQ5R7E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173339.
KEGGpon:100173339.

Organism-specific databases

CTD3162.

Phylogenomic databases

HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidQ5R7E3.
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. Heme_oxygenase. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHMOX1_PONAB
AccessionPrimary (citable) accession number: Q5R7E3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: April 3, 2013
This is version 46 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents