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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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.
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 Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC
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
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	39	1	N6-acetyllysine By similarity
	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: 3409220] [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: 8288554] [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: 15489334] [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: 18474359] [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: 18400743] [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.
STRING	P14901.
PTM databases
PhosphoSite	P14901.
Proteomic databases
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	roNOG15435.
HOGENOM	HBG431019.
HOVERGEN	HBG005982.
InParanoid	P14901.
OMA	AENTEFM.
PhylomeDB	P14901.
Gene expression databases
ArrayExpress	P14901.
Bgee	P14901.
CleanEx	MM_HMOX1.
Genevestigator	P14901.
GermOnline	ENSMUSG00000005413. Mus musculus.
Family and domain databases
InterPro	IPR002051. Haem_Oase. IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR018207. Haem_oxygenase_CS. [Graphical view]
Gene3D	G3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
KO	K00510.
PANTHER	PTHR10720. Haem_Oase. 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
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:	November 16, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program