Heme oxygenase 1 - Rattus norvegicus (Rat)

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P06762 (HMOX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from direct assay PubMed 12593860. Source: RGD cellular response to cadmium ion Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to nutrient Inferred from expression pattern PubMed 15531134. Source: RGD erythrocyte homeostasis Inferred from electronic annotation. Source: Compara heme catabolic process Inferred from direct assay PubMed 15226268. Source: RGD heme oxidation Traceable author statement PubMed 12114196. Source: RGD intrinsic apoptotic signaling pathway in response to DNA damage Inferred from direct assay PubMed 11854317. Source: RGD iron ion homeostasis Inferred from electronic annotation. Source: Compara negative regulation of DNA binding Inferred from direct assay PubMed 17234154. Source: RGD negative regulation of mast cell cytokine production Inferred from direct assay PubMed 17234154. Source: RGD negative regulation of mast cell degranulation Inferred from direct assay PubMed 17234154. Source: RGD negative regulation of muscle cell apoptotic process Inferred from direct assay PubMed 12396617. Source: RGD negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 19177228. Source: RGD negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 17234154. Source: RGD negative regulation of smooth muscle cell proliferation Inferred from mutant phenotype PubMed 19885007. Source: RGD phospholipid metabolic process Traceable author statement PubMed 12511545. Source: RGD positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from mutant phenotype PubMed 20925964. Source: RGD 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 direct assay PubMed 12215473. Source: RGD regulation of transcription from RNA polymerase II promoter in response to oxidative stress Inferred from direct assay PubMed 17430897. Source: BHF-UCL response to estrogen stimulus Inferred from direct assay PubMed 15734876. Source: RGD response to hydrogen peroxide Inferred from direct assay PubMed 17430897. Source: BHF-UCL response to hypoxia Inferred from expression pattern PubMed 14970910. Source: RGD response to nicotine Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from direct assay PubMed 12511545. Source: RGD wound healing involved in inflammatory response Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from direct assay PubMed 15226268. Source: RGD cytosol Inferred from direct assay PubMed 14766239. Source: RGD endoplasmic reticulum Inferred from direct assay Ref.2. Source: BHF-UCL endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay PubMed 14766239. Source: RGD
Molecular_function	heme binding Inferred from direct assay PubMed 12044160. Source: RGD heme oxygenase (decyclizing) activity Inferred from direct assay Ref.2. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase D activity Inferred from direct assay PubMed 12511545. Source: RGD 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_0000209690

Sites

Metal binding

Iron (heme axial ligand)

Binding site

Heme By similarity

Binding site

134

Heme By similarity

Binding site

183

Heme By similarity

Amino acid modifications

Modified residue

229

Phosphoserine By similarity

Secondary structure

289

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06762 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: EF7D2B98048AF44D
Show »

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

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] [Europe PMC] [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] [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]. 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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-267.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

IPI

IPI00206626.

PIR

OHRTD. A92645.

RefSeq

NP_036712.1. NM_012580.2.

UniGene

Rn.3160.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3I9T	X-ray	2.15	A	1-261	[»]
3I9U	X-ray	2.25	A	1-261	[»]
4G7L	X-ray	1.80	A	1-267	[»]
4G7P	X-ray	1.90	A	1-267	[»]
4G7T	X-ray	1.90	A	1-267	[»]
4G7U	X-ray	1.90	A	1-267	[»]
4G8P	X-ray	1.90	A	1-267	[»]
4G8U	X-ray	2.10	A	1-267	[»]
4G8W	X-ray	2.40	A	1-267	[»]
4G98	X-ray	2.30	A	1-267	[»]
4G99	X-ray	2.30	A	1-267	[»]

ProteinModelPortal

P06762.

SMR

P06762. Positions 7-222.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4996356.

STRING

10116.ENSRNOP00000019192.

PTM databases

PhosphoSite

P06762.

Proteomic databases

PaxDb

P06762.

PRIDE

P06762.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117.

GeneID

24451.

KEGG

rno:24451.

UCSC

RGD:2806. rat.

Organism-specific databases

CTD

3162.

RGD

2806. Hmox1.

Phylogenomic databases

eggNOG

COG5398.

GeneTree

ENSGT00390000017673.

HOGENOM

HOG000233221.

HOVERGEN

HBG005982.

InParanoid

P06762.

K00510.

OrthoDB

EOG4TF0KR.

Gene expression databases

ArrayExpress

P06762.

Genevestigator

P06762.

GermOnline

ENSRNOG00000014117. Rattus norvegicus.

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

BindingDB

P06762.

ChEMBL

CHEMBL5035.

EvolutionaryTrace

P06762.

NextBio

603359.

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:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents