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Reviewed, UniProtKB/Swiss-Prot P14791 (HMOX1_CHICK)

Last modified June 16, 2009. Version 61. 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
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

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.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
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 – 296296Heme oxygenase 1
PRO_0000209696

Sites

Metal binding281Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P14791-1 [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: 1996964] [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: 2158889] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

X56201 mRNA. Translation: CAA39661.1.
IPIIPI00580654.
PIRS15123.
RefSeqNP_990675.1.
UniGeneGga.2039

3D structure databases

HSSPHSSP built from PDB template 1N45 based on UniProtKB P09601.
SMRP14791. Positions 4-225.
ModBaseSearch...

Proteomic databases

PRIDEP14791.

Genome annotation databases

EnsemblENSGALG00000012550. Gallus gallus. [Contig view]
GeneID396287.
KEGGgga:396287.

Phylogenomic databases

HOVERGENP14791.

Enzyme and pathway databases

BRENDA1.14.99.3. 4.

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_CHICK
AccessionPrimary (citable) accession number: P14791
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 1, 1992
Last modified: June 16, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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