Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5E9F2 (HMOX1_BOVIN)

Last modified June 16, 2009. Version 30. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length289 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 By similarity.

Catalytic activity

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

Subcellular location

Microsome By similarity. Endoplasmic reticulum By similarity.

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 – 289289Heme oxygenase 1
PRO_0000209686

Sites

Metal binding261Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict281Q → E AA sequence Ref.3
Sequence conflict1001P → PH AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q5E9F2-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 8EAEA06BCCA4B96C

FASTA28932,940
        10         20         30         40         50         60 
MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL VMASLYHIYV 

        70         80         90        100        110        120 
ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP RWQEAIPYTQ ATKRYVQRLQ 

       130        140        150        160        170        180 
EVGRTEPELL VAHAYTRYLG DLSGGQVLKK IAQKALNLPS SGEGLAFFTF PNIASATKFK 

       190        200        210        220        230        240 
QLYRSRMNTL EMTPEVRQRV LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR 

       250        260        270        280 
AGSKVQDLAP TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Structural studies on bovine spleen heme oxygenase. Immunological and structural diversity among mammalian heme oxygenase enzymes."
Schacter B.A., Cripps V., Troxler R.F., Offner G.D.
Arch. Biochem. Biophys. 282:404-412(1990) [PubMed: 1700666] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND 200-205.
Tissue: Spleen.

Cross-references

Sequence databases

BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
IPIIPI00690186.
PIRS13265.
RefSeqNP_001014912.1.
UniGeneBt.4001

3D structure databases

SMRQ5E9F2. Positions 1-224.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000015582. Bos taurus. [Contig view]
GeneID513221.
KEGGbta:513221.

Phylogenomic databases

HOVERGENQ5E9F2.

Enzyme and pathway databases

BRENDA1.14.99.3. 251.

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_BOVIN
AccessionPrimary (citable) accession number: Q5E9F2
Secondary accession number(s): Q3ZCK7, Q7M338
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 15, 2005
Last modified: June 16, 2009
This is version 30 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