Heme oxygenase 2 - Rattus norvegicus (Rat)

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P23711 (HMOX2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

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

Documents (1) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Heme oxygenase 2
Short name=HO-2
EC=1.14.99.3

Gene names

Name:

Hmox2

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	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
Catalytic activity	Heme + 3 AH₂ + 3 O₂ = biliverdin + Fe²⁺ + CO + 3 A + 3 H₂O.
Subcellular location	Microsome. Endoplasmic reticulum.
Tissue specificity	Widely distributed in body with a high concentration in the brain.
Induction	Heme oxygenase 2 activity is non-inducible.
Sequence similarities	Belongs to the heme oxygenase family. Contains 2 HRM (heme regulatory motif) repeats.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome
Domain	Repeat
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	heme oxidation Traceable author statement PubMed 12114211. Source: RGD response to hypoxia Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from direct assay PubMed 11950143. Source: RGD
Cellular_component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	heme oxygenase (decyclizing) activity Inferred from direct assay Ref.1. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CALM	P62157	3	EBI-2910092,EBI-397403	From a different organism.
Calm3	P62161	2	EBI-2910092,EBI-397530

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 315

314

Heme oxygenase 2

PRO_0000209694

Regions

Repeat

263 – 268

HRM 1

Repeat

280 – 285

HRM 2

Sites

Metal binding

Iron (heme axial ligand) By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Experimental info

Sequence conflict

142 – 146

QNEPE → EFRNK in AAA41347. Ref.4

Sequence conflict

230 – 232

MQI → TEF in AAA41347. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P23711 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 981AADE01DE1AFCF
Show »

FASTA

315

35,762

        10         20         30         40         50         60 
MSSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN 

        70         80         90        100        110        120 
IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKEALIK DMEYFFGENW 

       130        140        150        160        170        180 
EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG 

       190        200        210        220        230        240 
EGTQFYLFEH VDNAQQFKQF YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG 

       250        260        270        280        290        300 
SMLTKETLED GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA 

       310 
ASVALVAGLL AWYYM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, characterization, and expression in Escherichia coli of a cDNA encoding rat heme oxygenase-2." Rotenberg M.O., Maines M.D. J. Biol. Chem. 265:7501-7506(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"The structure, organization and differential expression of the gene encoding rat heme oxygenase-2." McCoubrey W.K. Jr., Maines M.D. Gene 139:155-161(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley. Tissue: Liver.
[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: Prostate.
[4]	"Evidence suggesting that the two forms of heme oxygenase are products of different genes." Cruse I., Maines M.D. J. Biol. Chem. 263:3348-3353(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-232, PARTIAL PROTEIN SEQUENCE. Tissue: Liver and Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05405 mRNA. Translation: AAA41340.1. U05013 Genomic DNA. Translation: AAA19130.1. BC062061 mRNA. Translation: AAH62061.1. M18918 mRNA. Translation: AAA41347.1.
IPI	IPI00213655.
PIR	A35199.
RefSeq	NP_001264002.1. NM_001277073.1. NP_077363.1. NM_024387.2.
UniGene	Rn.10241.
3D structure databases
ProteinModelPortal	P23711.
SMR	P23711. Positions 29-247.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23711. 2 interactions.
STRING	10116.ENSRNOP00000005031.
Proteomic databases
PaxDb	P23711.
PRIDE	P23711.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000005031; ENSRNOP00000005031; ENSRNOG00000003773.
GeneID	79239.
KEGG	rno:79239.
UCSC	RGD:67402. rat.
Organism-specific databases
CTD	3163.
RGD	67402. Hmox2.
Phylogenomic databases
eggNOG	COG5398.
GeneTree	ENSGT00390000017673.
HOGENOM	HOG000233221.
HOVERGEN	HBG005982.
InParanoid	P23711.
KO	K00510.
OMA	KQFYRAR.
OrthoDB	EOG4RNB8T.
Gene expression databases
Genevestigator	P23711.
GermOnline	ENSRNOG00000003773. 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	P23711.
ChEMBL	CHEMBL3348.
NextBio	614672.

Entry information

Entry name

HMOX2_RAT

Accession

Primary (citable) accession number: P23711

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 105 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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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