Heme oxygenase 1 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P06762 (HMOX1_RAT)

Last modified June 16, 2009. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Heme oxygenase 1
      Short name=HO-1
    EC=1.14.99.3
Alternative name(s):
    HSP32

Gene names

Name:

Hmox1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Sequence similarities	Belongs to the heme oxygenase family.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in induction of apoptosis Inferred from direct assay. Source: RGD angiogenesis Inferred from direct assay. Source: RGD cell death Inferred from direct assay. Source: UniProtKB cellular response to nutrient Inferred from expression pattern. Source: RGD heme catabolic process Inferred from direct assay. Source: RGD heme oxidation Traceable author statement. Source: RGD negative regulation of cell proliferation Inferred from direct assay. Source: RGD negative regulation of mast cell cytokine production Inferred from direct assay. Source: RGD negative regulation of mast cell degranulation Inferred from direct assay. Source: RGD negative regulation of transcription factor activity Inferred from direct assay. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Traceable author statement. Source: RGD positive regulation of anti-apoptosis Inferred from direct assay. Source: RGD regulation of blood pressure Inferred from direct assay. Source: RGD regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from direct assay. Source: UniProtKB response to estrogen stimulus Inferred from direct assay. Source: RGD response to hydrogen peroxide Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from expression pattern. Source: RGD small GTPase mediated signal transduction Inferred from direct assay. Source: RGD
Cellular component	caveola Inferred from direct assay. Source: RGD cytosol Inferred from direct assay. Source: RGD endoplasmic reticulum Ref.2 Inferred from direct assay. Source: UniProtKB microsome Ref.2 Inferred from direct assay. Source: UniProtKB nucleolus Inferred from direct assay. Source: RGD
Molecular function	enzyme binding Inferred from physical interaction. Source: UniProtKB heme binding Inferred from direct assay. Source: RGD heme oxygenase (decyclizing) activity Ref.2 Inferred from direct assay. Source: UniProtKB phospholipase D activity Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 289

289

Heme oxygenase 1

PRO_0000209690

Sites

Metal binding

Iron (heme axial ligand)

Amino acid modifications

Modified residue

229

Phosphoserine By similarity

Secondary structure

289

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P06762-1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: EF7D2B98048AF44D
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FASTA

289

33,006

        10         20         30         40         50         60 
MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV MASLYHIYTA 

        70         80         90        100        110        120 
LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEAIPYTPA TQHYVKRLHE 

       130        140        150        160        170        180 
VGGTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ 

       190        200        210        220        230        240 
LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP 

       250        260        270        280 
ASLVQDTTSA ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and organization of the rat heme oxygenase gene." Mueller R.M., Taguchi H., Shibahara S. J. Biol. Chem. 262:6795-6802(1987) [PubMed: 3032976] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and expression of cDNA for rat heme oxygenase." Shibahara S., Mueller R., Taguchi H., Yoshida T. Proc. Natl. Acad. Sci. U.S.A. 82:7865-7869(1985) [PubMed: 3865203] [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]. Tissue: Thymus.
[4]	"Crystal structure of rat heme oxygenase-1 in complex with heme." Sugishima M., Omata Y., Kakuta Y., Sakamoto H., Noguchi M., Fukuyama K. FEBS Lett. 471:61-66(2000) [PubMed: 10760513] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-267.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J02722 Genomic DNA. Translation: AAA41346.1.
BC091164 mRNA. Translation: AAH91164.1.

IPI

IPI00206626.

PIR

OHRTD. A92645.

RefSeq

NP_036712.1.

UniGene

Rn.3160

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DVE	X-ray	2.40	A	1-267	[»]
1DVG	X-ray	2.20	A/B	1-267	[»]
1IRM	X-ray	2.55	A/B/C	1-267	[»]
1IVJ	X-ray	1.90	A	1-267	[»]
1IX3	X-ray	2.00	A	1-267	[»]
1IX4	X-ray	1.80	A	1-267	[»]
1J02	X-ray	1.70	A	1-267	[»]
1J2C	X-ray	2.40	A	1-267	[»]
1UBB	X-ray	2.30	A	1-267	[»]
1ULX	X-ray	2.00	A	1-267	[»]
1VGI	X-ray	1.90	A	1-267	[»]
2DY5	X-ray	2.70	A	1-267	[»]
2E7E	X-ray	1.85	A	1-267	[»]
2ZVU	X-ray	2.20	A	1-267	[»]

ModBase

Search...

PTM databases

PhosphoSite

P06762.

Proteomic databases

PRIDE

P06762.

Genome annotation databases

Ensembl

ENSRNOG00000014117. Rattus norvegicus. [Contig view]

GeneID

24451.

KEGG

rno:24451.

NMPDR

fig|10116.3.peg.14608.

Organism-specific databases

RGD

2806. Hmox1.

Phylogenomic databases

HOVERGEN

P06762.

Enzyme and pathway databases

BRENDA

1.14.99.3. 248.

Gene expression databases

ArrayExpress

P06762.

GermOnline

ENSRNOG00000014117. Rattus norvegicus.

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.

PANTHER

PTHR10720. Haem_Oase. 1 hit.

Pfam

PF01126. Heme_oxygenase. 1 hit.
[Graphical view]

PIRSF

PIRSF000343. Haem_Oase. 1 hit.

PRINTS

PR00088. HAEMOXYGNASE.

PROSITE

PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

603359.

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Entry information

Entry name

HMOX1_RAT

Accession

Primary (citable) accession number: P06762
Secondary accession number(s): Q5BK87

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families