P14901 (HMOX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heme oxygenase 1
Short name=HO-1
EC=1.14.99.3

Alternative name(s):
P32 protein

Gene names

Name:

Hmox1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. It is also induced in macrophages, liver and the lungs upon infection with M.tuberculosis (at protein level). Data is conflicting as to whether macrophage induction is independent of the nitric oxide (NO) signaling pathway (Ref.5), or dependent on NO (Ref.4). Ref.4 Ref.5
Sequence similarities	Belongs to the heme oxygenase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara cellular response to cadmium ion Inferred from direct assay PubMed 16183037. Source: MGI cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to nutrient Inferred from electronic annotation. Source: Compara erythrocyte homeostasis Inferred from electronic annotation. Source: Compara heme catabolic process Inferred from electronic annotation. Source: Compara heme metabolic process Inferred from direct assay PubMed 16183037. Source: MGI heme oxidation Inferred from electronic annotation. Source: InterPro intrinsic apoptotic signaling pathway in response to DNA damage Inferred from electronic annotation. Source: Compara iron ion homeostasis Inferred from electronic annotation. Source: Compara negative regulation of DNA binding Inferred from electronic annotation. Source: Compara negative regulation of mast cell cytokine production Inferred from electronic annotation. Source: Compara negative regulation of mast cell degranulation Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis 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 regulation of blood pressure Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to nicotine Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: Compara wound healing involved in inflammatory response Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 17430897. Source: BHF-UCL
Molecular_function	heme binding Inferred from electronic annotation. Source: Compara heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase D activity Inferred from electronic annotation. Source: Compara signal transducer activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 289	289	Heme oxygenase 1		PRO_0000209688
Sites
	Metal binding	25	1	Iron (heme axial ligand) By similarity
	Binding site	18	1	Heme By similarity
	Binding site	134	1	Heme By similarity
	Binding site	183	1	Heme By similarity
Amino acid modifications
	Modified residue	229	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P14901 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 19DB0DCCD574044B	FASTA	289	32,929
	10 20 30 40 50 60 MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV MASLYHIYTA 70 80 90 100 110 120 LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEIIPCTPA TQHYVKRLHE 130 140 150 160 170 180 VGRTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ 190 200 210 220 230 240 LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP 250 260 270 280 ASLVQDTAPA ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of a complementary DNA clone for a Mr 32,000 protein which is induced with tumor promoters in BALB/c 3T3 cells." Kageyama H., Hiwasa T., Tokunaga K., Sakiyama S. Cancer Res. 48:4795-4798(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Fibroblast.
[2]	"Isolation and characterization of the mouse heme oxygenase-1 gene. Distal 5' sequences are required for induction by heme or heavy metals." Alam J., Cai J., Smith A. J. Biol. Chem. 269:1001-1009(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[4]	"Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection." Shiloh M.U., Manzanillo P., Cox J.S. Cell Host Microbe 3:323-330(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY M.TUBERCULOSIS.
[5]	"Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon." Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I., Agarwal A., Steyn A.J. J. Biol. Chem. 283:18032-18039(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION IN MACROPHAGES AND LUNGS BY M.TUBERCULOSIS. Strain: C3Heb/FeJ and C57BL/6 X FVB. Tissue: Lung and Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M33203 mRNA. Translation: AAA39872.1. X13356 mRNA. Translation: CAA31732.1. X56824 , X56825, X56826, X56827 Genomic DNA. Translation: CAA40159.1. BC010757 mRNA. Translation: AAH10757.1.
IPI	IPI00131577.
PIR	I48409.
RefSeq	NP_034572.1. NM_010442.2.
UniGene	Mm.276389.
3D structure databases
ProteinModelPortal	P14901.
SMR	P14901. Positions 30-225.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14901. 1 interaction.
PTM databases
PhosphoSite	P14901.
Proteomic databases
PaxDb	P14901.
PRIDE	P14901.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413.
GeneID	15368.
KEGG	mmu:15368.
Organism-specific databases
CTD	3162.
MGI	MGI:96163. Hmox1.
Phylogenomic databases
eggNOG	COG5398.
HOGENOM	HOG000233221.
HOVERGEN	HBG005982.
InParanoid	P14901.
KO	K00510.
OMA	YAPLYFP.
Gene expression databases
ArrayExpress	P14901.
Bgee	P14901.
CleanEx	MM_HMOX1.
Genevestigator	P14901.
GermOnline	ENSMUSG00000005413. Mus musculus.
Family and domain databases
Gene3D	1.20.910.10. 1 hit.
InterPro	IPR002051. Haem_Oase. IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR018207. Haem_oxygenase_CS. [Graphical view]
PANTHER	PTHR10720. PTHR10720. 1 hit.
Pfam	PF01126. Heme_oxygenase. 1 hit. [Graphical view]
PIRSF	PIRSF000343. Haem_Oase. 1 hit.
PRINTS	PR00088. HAEMOXYGNASE.
SUPFAM	SSF48613. Heme_oxygenase. 1 hit.
PROSITE	PS00593. HEME_OXYGENASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4434.
NextBio	287998.
SOURCE	Search...

Entry information

Entry name

HMOX1_MOUSE

Accession

Primary (citable) accession number: P14901

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program