Skip Header

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

Q5E9F2 (HMOX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 59. 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
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length289 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 By similarity.

Catalytic activity

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

Subcellular location

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

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cadmium ion

Inferred from electronic annotation. Source: Compara

cellular response to hypoxia

Inferred from electronic annotation. Source: Compara

erythrocyte homeostasis

Inferred from electronic annotation. Source: Compara

heme oxidation

Inferred from electronic annotation. Source: InterPro

iron ion homeostasis

Inferred from electronic annotation. Source: Compara

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Compara

positive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from electronic annotation. Source: Compara

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Compara

protein homooligomerization

Inferred from electronic annotation. Source: Compara

response to nicotine

Inferred from electronic annotation. Source: Compara

response to oxidative stress

Inferred from electronic annotation. Source: Compara

signal transduction

Inferred from electronic annotation. Source: GOC

wound healing involved in inflammatory response

Inferred from electronic annotation. Source: Compara

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: Compara

   Molecular_functionheme oxygenase (decyclizing) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from electronic annotation. Source: Compara

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
Binding site191Heme By similarity
Binding site1351Heme By similarity
Binding site1841Heme By similarity

Experimental info

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

Sequences

Sequence LengthMass (Da)Tools
Q5E9F2 [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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ		BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
IPIIPI00690186.
PIRS13265.
RefSeqNP_001014912.1. NM_001014912.1.
UniGeneBt.4001.

3D structure databases

ProteinModelPortalQ5E9F2.
SMRQ5E9F2. Positions 1-224.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000020701.

Proteomic databases

PRIDEQ5E9F2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneID513221.
KEGGbta:513221.

Organism-specific databases

CTD3162.

Phylogenomic databases

eggNOGCOG5398.
GeneTreeENSGT00390000017673.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidQ5E9F2.
KOK00510.
OMAYAPLYFP.
OrthoDBEOG4TF0KR.

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. Heme_oxygenase. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL1255146.
NextBio20870758.

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: April 3, 2013
This is version 59 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents