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Reviewed, UniProtKB/Swiss-Prot P32394 (HMOX1_PIG)

Last modified June 16, 2009. Version 57. 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 1
      Short name=HO-1
    EC=1.14.99.3
Gene names
Name: HMOX1
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length288 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.

Catalytic activity

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

Subcellular location

Microsome. Endoplasmic reticulum.

Induction

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   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 – 288288Heme oxygenase 1
PRO_0000209689

Sites

Metal binding251Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P32394-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 156D6175A308E0D2

FASTA28833,074
        10         20         30         40         50         60 
MEHSQPNSMP QDLSEALKEA TKEVHVQAEN AEFMKNFQKG EVTREGFKLV MASLYHIYDA 

        70         80         90        100        110        120 
LEEEIEHNKE NPVYTPLYFP EELHRRAALE QDMAFWYGPR WQEAIPYTQA TKRYVRRLQQ 

       130        140        150        160        170        180 
VGRFEPELLV AHAYTRYMGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NVANATKFKQ 

       190        200        210        220        230        240 
LYRSRMNTLE MTPEVKQRVL EEAKTAFLLN IQLFEEVQEL LTQDTKDQRP SQASDIRKRA 

       250        260        270        280 
GSRVQDSTPV TTPRGKPQLS VLSQVPLIRW VLTLSFLVAT VAMGLYAM 

« Hide

References

[1]"Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli."
Suzuki T., Sato M., Ishikawa K., Yoshida T.
Biochem. Int. 28:887-893(1992) [PubMed: 1288499] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

X60677 mRNA. Translation: CAA43092.1.
PIRS37687.
RefSeqNP_001004027.1.
UniGeneSsc.115

3D structure databases

HSSPHSSP built from PDB template 1NI6 based on UniProtKB P09601.
SMRP32394. Positions 1-223.
ModBaseSearch...

Genome annotation databases

GeneID445512.
KEGGssc:445512.

Phylogenomic databases

HOVERGENP32394.

Enzyme and pathway databases

BRENDA1.14.99.3. 249.

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 nameHMOX1_PIG
AccessionPrimary (citable) accession number: P32394
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 57 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