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P14791 (HMOX1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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

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

Subcellular location

Microsome. Endoplasmic reticulum.

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
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

Chain1 – 296296Heme oxygenase 1
PRO_0000209696

Sites

Metal binding281Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P14791 [UniParc].

Last modified March 1, 1992. Version 2.
Checksum: 22DAA9324494CC0E

FASTA29633,509
        10         20         30         40         50         60 
METSQPHNAE SMSQDLSELL KEATKEVHEQ AENTPFMKNF QKGQVSLHEF KLVTASLYFI 

        70         80         90        100        110        120 
YSALEEEIER NKDNPVYAPV YFPMELHRKA ALEKDLEYFY GSNWRAEIPC PEATQKYVER 

       130        140        150        160        170        180 
LHVVGKKHPE LLVAHAYTRY LGDLSGGQVL KKIAQKALQL PSTGEGLAFF TFDGVSNATK 

       190        200        210        220        230        240 
FKQLYRSRMN ALEMDHATKK RVLEEAKKAF LLNIQVFEAL QKLVSKSQEN GHAVQPKAEL 

       250        260        270        280        290 
RTRSVNKSHE NSPAAGKESE RTSRMQADML TTSPLVRWLL ALGFIATTVA VGLFAM 

« Hide

References

[1]"Cloning, sequencing and expression of cDNA for chick liver haem oxygenase. Comparison of avian and mammalian cDNAs and deduced proteins."
Evans C.O., Healey J.F., Greene Y., Bonkovsky H.L.
Biochem. J. 273:659-666(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification and characterization of heme oxygenase from chick liver. Comparison of the avian and mammalian enzymes."
Bonkovsky H.L., Healey J.F., Pohl J.
Eur. J. Biochem. 189:155-166(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56201 mRNA. Translation: CAA39661.1.
PIRS15123.
RefSeqNP_990675.1. NM_205344.1.
UniGeneGga.2039.

3D structure databases

ProteinModelPortalP14791.
SMRP14791. Positions 1-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000036970.

Proteomic databases

PaxDbP14791.
PRIDEP14791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396287.
KEGGgga:396287.

Organism-specific databases

CTD3162.

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidP14791.
KOK00510.
PhylomeDBP14791.

Enzyme and pathway databases

SABIO-RKP14791.

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...

Other

NextBio20816338.
PROP14791.

Entry information

Entry nameHMOX1_CHICK
AccessionPrimary (citable) accession number: P14791
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 90 of the entry and version 2 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