Heme oxygenase 1 - Rattus norvegicus (Rat)

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P06762 (HMOX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. 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)

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.
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 Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
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: BHF-UCL 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 DNA binding 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 neuron apoptosis Inferred from mutant phenotype. Source: RGD negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: RGD negative regulation of smooth muscle cell proliferation Inferred from mutant phenotype. Source: RGD phospholipid metabolic process Traceable author statement. Source: RGD positive regulation of angiogenesis Inferred from mutant phenotype. 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: BHF-UCL response to estrogen stimulus Inferred from direct assay. Source: RGD response to hydrogen peroxide Inferred from direct assay. Source: BHF-UCL 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 Inferred from direct assay Ref.2. Source: BHF-UCL microsome Inferred from direct assay Ref.2. Source: BHF-UCL nucleolus Inferred from direct assay. Source: RGD
Molecular function	enzyme binding Inferred from physical interaction. Source: BHF-UCL heme binding Inferred from direct assay. Source: RGD heme oxygenase (decyclizing) activity Inferred from direct assay Ref.2. Source: BHF-UCL phospholipase D activity Inferred from direct assay. Source: RGD
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)

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

N6-acetyllysine By similarity

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: 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.

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	[»]

ProteinModelPortal

P06762.

SMR

P06762. Positions 7-222.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4996356.

STRING

P06762.

PTM databases

PhosphoSite

P06762.

Proteomic databases

PRIDE

P06762.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117.

GeneID

24451.

KEGG

rno:24451.

NMPDR

fig|10116.3.peg.14608.

UCSC

NM_012580. rat.

Organism-specific databases

CTD

3162.

RGD

2806. Hmox1.

Phylogenomic databases

eggNOG

roNOG15435.

GeneTree

ENSGT00390000017673.

HOVERGEN

HBG005982.

InParanoid

P06762.

OrthoDB

EOG4TF0KR.

PhylomeDB

P06762.

Gene expression databases

ArrayExpress

P06762.

Genevestigator

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.

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

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:	November 16, 2011
This is version 104 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