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P32394 (HMOX1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 82. 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 1

Short name=HO-1
EC=1.14.99.3
Gene names
Name:HMOX1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Catalytic activity

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

Subcellular location

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

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
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

heme 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: 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

Chain1 – 288288Heme oxygenase 1
PRO_0000209689

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P32394 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60677 mRNA. Translation: CAA43092.1.
PIRS37687.
RefSeqNP_001004027.1. NM_001004027.1.
UniGeneSsc.115.

3D structure databases

ProteinModelPortalP32394.
SMRP32394. Positions 1-223.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID445512.
KEGGssc:445512.

Organism-specific databases

CTD3162.

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 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: October 16, 2013
This is version 82 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