Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H2O.HMP:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18HemeHMP:1
Metal bindingi25Iron (heme axial ligand)1
Binding sitei134HemeHMP:1
Binding sitei183HemeHMP:1

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • heme binding Source: RGD
  • heme oxygenase (decyclizing) activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • phospholipase D activity Source: RGD
  • protein homodimerization activity Source: RGD
  • signal transducer 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 proliferation Source: RGD
  • negative regulation of DNA binding 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 sequence-specific DNA binding transcription factor activity Source: RGD
  • negative regulation of smooth muscle cell proliferation Source: RGD
  • negative regulation of vascular 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 I-kappaB kinase/NF-kappaB signaling Source: RGD
  • positive regulation of macroautophagy Source: RGD
  • positive regulation of smooth muscle cell proliferation Source: RGD
  • protein homooligomerization Source: RGD
  • regulation of blood pressure Source: RGD
  • regulation of sequence-specific 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 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 functionOxidoreductase
Biological processApoptosis
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 5301.
ReactomeiR-RNO-189483. Heme degradation.
R-RNO-917937. Iron uptake and transport.
SABIO-RKiP06762.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.14.18HMP:)
Short name:
HO-1
Alternative name(s):
HSP32
Gene namesi
Name:Hmox1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi2806. Hmox1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5035.
GuidetoPHARMACOLOGYi1441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002096901 – 289Heme oxygenase 1Add BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei229PhosphoserineHMP:1
Modified residuei242PhosphoserineND:1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP06762.
PRIDEiP06762.

PTM databases

iPTMnetiP06762.
PhosphoSitePlusiP06762.

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

BgeeiENSRNOG00000014117.
GenevisibleiP06762. RN.

Interactioni

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi246615. 1 interactor.
MINTiMINT-4996356.
STRINGi10116.ENSRNOP00000019192.

Chemistry databases

BindingDBiP06762.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 29ND:17
Helixi32 – 39ND:8
Helixi44 – 67ND:24
Turni68 – 70ND:3
Turni72 – 74ND:3
Helixi75 – 77ND:3
Helixi80 – 83ND:4
Helixi86 – 97ND:12
Helixi101 – 103ND:3
Helixi109 – 124ND:16
Helixi126 – 128ND:3
Helixi129 – 140ND:12
Helixi143 – 155ND:13
Helixi165 – 167ND:3
Helixi175 – 186ND:12
Helixi193 – 221ND:29

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DVEX-ray2.40A1-267[»]
1DVGX-ray2.20A/B1-267[»]
1IRMX-ray2.55A/B/C1-267[»]
1IVJX-ray1.90A1-267[»]
1IX3X-ray2.00A1-267[»]
1IX4X-ray1.80A1-267[»]
1J02X-ray1.70A1-267[»]
1J2CX-ray2.40A1-267[»]
1UBBX-ray2.30A1-267[»]
1ULXX-ray2.00A1-267[»]
1VGIX-ray1.90A1-267[»]
2DY5X-ray2.70A1-267[»]
2E7EX-ray1.85A1-267[»]
2ZVUX-ray2.20A1-267[»]
3I9TX-ray2.15A1-261[»]
3I9UX-ray2.25A1-261[»]
3WKTX-ray4.30C/D1-267[»]
4G7LX-ray1.80A1-267[»]
4G7PX-ray1.90A1-267[»]
4G7TX-ray1.90A1-267[»]
4G7UX-ray1.90A1-267[»]
4G8PX-ray1.90A1-267[»]
4G8UX-ray2.10A1-267[»]
4G8WX-ray2.40A1-267[»]
4G98X-ray2.30A1-267[»]
4G99X-ray2.30A1-267[»]
4MECX-ray3.20A/B/C/D/E/F/G1-232[»]
ProteinModelPortaliP06762.
SMRiP06762.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06762.

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.IKR:

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP06762.
KOiK00510.
OMAiKKSHTMA.
OrthoDBiEOG091G0AS0.
PhylomeDBiP06762.
TreeFamiTF314786.

Family and domain databases

CDDicd00232. HemeO. 1 hit.
Gene3Di1.20.910.10. 1 hit.
InterProiView protein in InterPro
IPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiView protein in Pfam
PF01126. Heme_oxygenase. 1 hit.
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiView protein in PROSITE
PS00593. HEME_OXYGENASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P06762-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:289
Mass (Da):33,006
Last modified:January 1, 1988 - v1
Checksum:iEF7D2B98048AF44D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02722 Genomic DNA. Translation: AAA41346.1.
BC091164 mRNA. Translation: AAH91164.1.
PIRiA92645. OHRTD.
RefSeqiNP_036712.1. NM_012580.2.
UniGeneiRn.3160.

Genome annotation databases

EnsembliENSRNOT00000019192; ENSRNOP00000019192; ENSRNOG00000014117.
GeneIDi24451.
KEGGirno:24451.
UCSCiRGD:2806. rat.

Similar proteinsi

Entry informationi

Entry nameiHMOX1_RAT
AccessioniPrimary (citable) accession number: P06762
Secondary accession number(s): Q5BK87
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 22, 2017
This is version 155 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families