UniProtKB - P06762 (HMOX1_RAT)
Protein
Heme oxygenase 1
Gene
Hmox1
Organism
Rattus norvegicus (Rat)
Status
Functioni
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Catalytic activityi
- heme b + 3 O2 + 3 reduced [NADPH—hemoprotein reductase] = biliverdin IXα + CO + Fe2+ + H+ + 3 H2O + 3 oxidized [NADPH—hemoprotein reductase]By similarityEC:1.14.14.18By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 18 | HemeBy similarity | 1 | |
Metal bindingi | 25 | Iron (heme axial ligand) | 1 | |
Binding sitei | 134 | HemeBy similarity | 1 | |
Binding sitei | 183 | HemeBy similarity | 1 |
GO - Molecular functioni
- enzyme binding Source: BHF-UCL
- heme binding Source: RGD
- heme oxygenase (decyclizing) activity Source: BHF-UCL
- identical protein binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- phospholipase D activity Source: RGD
- protein homodimerization activity Source: RGD
- structural molecule activity Source: RGD
GO - Biological processi
- angiogenesis Source: RGD
- cell death Source: BHF-UCL
- cellular iron ion homeostasis Source: RGD
- cellular response to arsenic-containing substance Source: RGD
- cellular response to cadmium ion Source: RGD
- cellular response to cisplatin Source: RGD
- cellular response to heat Source: RGD
- cellular response to hypoxia Source: RGD
- cellular response to nutrient Source: RGD
- erythrocyte homeostasis Source: RGD
- heme catabolic process Source: RGD
- heme metabolic process Source: RGD
- heme oxidation Source: RGD
- intracellular signal transduction Source: RGD
- intrinsic apoptotic signaling pathway in response to DNA damage Source: RGD
- iron ion homeostasis Source: RGD
- liver regeneration Source: RGD
- negative regulation of cell population proliferation Source: RGD
- negative regulation of DNA binding Source: RGD
- negative regulation of DNA-binding transcription factor activity Source: RGD
- negative regulation of epithelial cell apoptotic process Source: RGD
- negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: RGD
- negative regulation of macroautophagy Source: RGD
- negative regulation of mast cell cytokine production Source: RGD
- negative regulation of mast cell degranulation Source: RGD
- negative regulation of muscle cell apoptotic process Source: RGD
- negative regulation of neuron apoptotic process Source: RGD
- negative regulation of smooth muscle cell proliferation Source: RGD
- negative regulation of vascular associated smooth muscle cell proliferation Source: RGD
- phospholipid metabolic process Source: RGD
- positive regulation of angiogenesis Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: RGD
- positive regulation of cell migration involved in sprouting angiogenesis Source: RGD
- positive regulation of macroautophagy Source: RGD
- positive regulation of smooth muscle cell proliferation Source: RGD
- regulation of blood pressure Source: RGD
- regulation of DNA-binding transcription factor activity Source: BHF-UCL
- regulation of transcription from RNA polymerase II promoter in response to iron Source: RGD
- regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
- response to drug Source: RGD
- response to estrogen Source: RGD
- response to hydrogen peroxide Source: BHF-UCL
- response to hypoxia Source: RGD
- response to nicotine Source: RGD
- response to oxidative stress Source: RGD
- small GTPase mediated signal transduction Source: RGD
- wound healing involved in inflammatory response Source: RGD
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Apoptosis |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.14.99.3, 5301 |
Reactomei | R-RNO-189483, Heme degradation R-RNO-917937, Iron uptake and transport R-RNO-9609523, Insertion of tail-anchored proteins into the endoplasmic reticulum membrane |
SABIO-RKi | P06762 |
Names & Taxonomyi
Protein namesi | Recommended name: Heme oxygenase 1 (EC:1.14.14.18By similarity)Short name: HO-1 Alternative name(s): HSP32 |
Gene namesi | Name:Hmox1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2806, Hmox1 |
Subcellular locationi
Endoplasmic reticulum
Cytosol
- cytosol Source: RGD
Endoplasmic reticulum
- endoplasmic reticulum Source: BHF-UCL
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Nucleus
Plasma Membrane
- caveola Source: RGD
- plasma membrane Source: RGD
Other locations
- perinuclear region of cytoplasm Source: RGD
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane, MicrosomePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000209690 | 1 – 289 | Heme oxygenase 1Add BLAST | 289 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 229 | PhosphoserineBy similarity | 1 | |
Modified residuei | 242 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P06762 |
PaxDbi | P06762 |
PRIDEi | P06762 |
PTM databases
iPTMneti | P06762 |
PhosphoSitePlusi | P06762 |
Expressioni
Inductioni
Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin.
Gene expression databases
Bgeei | ENSRNOG00000014117, Expressed in spleen and 21 other tissues |
Genevisiblei | P06762, RN |
Interactioni
GO - Molecular functioni
- enzyme binding Source: BHF-UCL
- identical protein binding Source: RGD
- protein homodimerization activity Source: RGD
Protein-protein interaction databases
BioGRIDi | 246615, 1 interactor |
MINTi | P06762 |
STRINGi | 10116.ENSRNOP00000019192 |
Chemistry databases
BindingDBi | P06762 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | P06762 |
SMRi | P06762 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06762 |
Family & Domainsi
Sequence similaritiesi
Belongs to the heme oxygenase family.Curated
Phylogenomic databases
eggNOGi | KOG4480, Eukaryota |
GeneTreei | ENSGT00390000017673 |
HOGENOMi | CLU_057050_0_1_1 |
InParanoidi | P06762 |
OMAi | KKSHTMA |
OrthoDBi | 1424194at2759 |
PhylomeDBi | P06762 |
TreeFami | TF314786 |
Family and domain databases
Gene3Di | 1.20.910.10, 1 hit |
InterProi | View protein in InterPro IPR002051, Haem_Oase IPR016053, Haem_Oase-like IPR016084, Haem_Oase-like_multi-hlx IPR018207, Haem_oxygenase_CS |
PANTHERi | PTHR10720, PTHR10720, 1 hit |
Pfami | View protein in Pfam PF01126, Heme_oxygenase, 1 hit |
PIRSFi | PIRSF000343, Haem_Oase, 1 hit |
PRINTSi | PR00088, HAEMOXYGNASE |
SUPFAMi | SSF48613, SSF48613, 1 hit |
PROSITEi | View protein in PROSITE PS00593, HEME_OXYGENASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P06762-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV
60 70 80 90 100
MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH
110 120 130 140 150
WQEAIPYTPA TQHYVKRLHE VGGTHPELLV AHAYTRYLGD LSGGQVLKKI
160 170 180 190 200
AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ LYRARMNTLE MTPEVKHRVT
210 220 230 240 250
EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP ASLVQDTTSA
260 270 280
ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02722 Genomic DNA Translation: AAA41346.1 BC091164 mRNA Translation: AAH91164.1 |
PIRi | A92645, OHRTD |
RefSeqi | NP_036712.1, NM_012580.2 |
Genome annotation databases
Ensembli | ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117 |
GeneIDi | 24451 |
KEGGi | rno:24451 |
UCSCi | RGD:2806, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02722 Genomic DNA Translation: AAA41346.1 BC091164 mRNA Translation: AAH91164.1 |
PIRi | A92645, OHRTD |
RefSeqi | NP_036712.1, NM_012580.2 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
3WKT | X-ray | 4.30 | C/D | 1-267 | [»] | |
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 | [»] | |
4MEC | X-ray | 3.20 | A/B/C/D/E/F/G | 1-232 | [»] | |
6J7A | X-ray | 3.27 | A/B | 1-238 | [»] | |
BMRBi | P06762 | |||||
SMRi | P06762 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 246615, 1 interactor |
MINTi | P06762 |
STRINGi | 10116.ENSRNOP00000019192 |
Chemistry databases
BindingDBi | P06762 |
ChEMBLi | CHEMBL5035 |
GuidetoPHARMACOLOGYi | 1441 |
PTM databases
iPTMneti | P06762 |
PhosphoSitePlusi | P06762 |
Proteomic databases
jPOSTi | P06762 |
PaxDbi | P06762 |
PRIDEi | P06762 |
Genome annotation databases
Ensembli | ENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117 |
GeneIDi | 24451 |
KEGGi | rno:24451 |
UCSCi | RGD:2806, rat |
Organism-specific databases
CTDi | 3162 |
RGDi | 2806, Hmox1 |
Phylogenomic databases
eggNOGi | KOG4480, Eukaryota |
GeneTreei | ENSGT00390000017673 |
HOGENOMi | CLU_057050_0_1_1 |
InParanoidi | P06762 |
OMAi | KKSHTMA |
OrthoDBi | 1424194at2759 |
PhylomeDBi | P06762 |
TreeFami | TF314786 |
Enzyme and pathway databases
BRENDAi | 1.14.99.3, 5301 |
Reactomei | R-RNO-189483, Heme degradation R-RNO-917937, Iron uptake and transport R-RNO-9609523, Insertion of tail-anchored proteins into the endoplasmic reticulum membrane |
SABIO-RKi | P06762 |
Miscellaneous databases
EvolutionaryTracei | P06762 |
PROi | PR:P06762 |
Gene expression databases
Bgeei | ENSRNOG00000014117, Expressed in spleen and 21 other tissues |
Genevisiblei | P06762, RN |
Family and domain databases
Gene3Di | 1.20.910.10, 1 hit |
InterProi | View protein in InterPro IPR002051, Haem_Oase IPR016053, Haem_Oase-like IPR016084, Haem_Oase-like_multi-hlx IPR018207, Haem_oxygenase_CS |
PANTHERi | PTHR10720, PTHR10720, 1 hit |
Pfami | View protein in Pfam PF01126, Heme_oxygenase, 1 hit |
PIRSFi | PIRSF000343, Haem_Oase, 1 hit |
PRINTSi | PR00088, HAEMOXYGNASE |
SUPFAMi | SSF48613, SSF48613, 1 hit |
PROSITEi | View protein in PROSITE PS00593, HEME_OXYGENASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HMOX1_RAT | |
Accessioni | P06762Primary (citable) accession number: P06762 Secondary accession number(s): Q5BK87 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | December 2, 2020 | |
This is version 177 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families