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P06762

- HMOX1_RAT

UniProt

P06762 - HMOX1_RAT

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Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181HemeBy similarity
Metal bindingi25 – 251Iron (heme axial ligand)
Binding sitei134 – 1341HemeBy similarity
Binding sitei183 – 1831HemeBy similarity

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. heme binding Source: RGD
  3. heme oxygenase (decyclizing) activity Source: BHF-UCL
  4. metal ion binding Source: UniProtKB-KW
  5. oxidoreductase activity Source: RGD
  6. phospholipase D activity Source: RGD
  7. signal transducer activity Source: Ensembl

GO - Biological processi

  1. angiogenesis Source: RGD
  2. cell death Source: BHF-UCL
  3. cellular response to arsenic-containing substance Source: Ensembl
  4. cellular response to cadmium ion Source: Ensembl
  5. cellular response to hypoxia Source: Ensembl
  6. cellular response to nutrient Source: RGD
  7. erythrocyte homeostasis Source: Ensembl
  8. heme catabolic process Source: RGD
  9. heme oxidation Source: RGD
  10. intracellular signal transduction Source: RGD
  11. intrinsic apoptotic signaling pathway in response to DNA damage Source: RGD
  12. iron ion homeostasis Source: Ensembl
  13. negative regulation of cell proliferation Source: RGD
  14. negative regulation of DNA binding Source: RGD
  15. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  16. negative regulation of mast cell cytokine production Source: RGD
  17. negative regulation of mast cell degranulation Source: RGD
  18. negative regulation of muscle cell apoptotic process Source: RGD
  19. negative regulation of neuron apoptotic process Source: RGD
  20. negative regulation of sequence-specific DNA binding transcription factor activity Source: RGD
  21. negative regulation of smooth muscle cell proliferation Source: RGD
  22. phospholipid metabolic process Source: RGD
  23. positive regulation of angiogenesis Source: RGD
  24. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  25. positive regulation of smooth muscle cell proliferation Source: Ensembl
  26. protein homooligomerization Source: Ensembl
  27. regulation of blood pressure Source: RGD
  28. regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  29. regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
  30. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: BHF-UCL
  31. response to estrogen Source: RGD
  32. response to hydrogen peroxide Source: BHF-UCL
  33. response to hypoxia Source: RGD
  34. response to nicotine Source: Ensembl
  35. response to oxidative stress Source: RGD
  36. small GTPase mediated signal transduction Source: RGD
  37. wound healing involved in inflammatory response Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP06762.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.99.3)
Short name:
HO-1
Alternative name(s):
HSP32
Gene namesi
Name:Hmox1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 19

Organism-specific databases

RGDi2806. Hmox1.

Subcellular locationi

GO - Cellular componenti

  1. caveola Source: RGD
  2. cytosol Source: RGD
  3. endoplasmic reticulum Source: BHF-UCL
  4. nucleolus Source: RGD
  5. nucleus Source: BHF-UCL
  6. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Heme oxygenase 1PRO_0000209690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP06762.
PRIDEiP06762.

PTM databases

PhosphoSiteiP06762.

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

GenevestigatoriP06762.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2917
Helixi32 – 398
Helixi44 – 6724
Turni68 – 703
Turni72 – 743
Helixi75 – 773
Helixi80 – 834
Helixi86 – 9712
Helixi101 – 1033
Helixi109 – 12416
Helixi126 – 1283
Helixi129 – 14012
Helixi143 – 15513
Helixi165 – 1673
Helixi175 – 18612
Helixi193 – 22129

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 7-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06762.

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG5398.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP06762.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG7JQBNR.
PhylomeDBiP06762.
TreeFamiTF314786.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

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:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02722 Genomic DNA. Translation: AAA41346.1 .
BC091164 mRNA. Translation: AAH91164.1 .
PIRi A92645. OHRTD.
RefSeqi NP_036712.1. NM_012580.2.
UniGenei Rn.3160.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P06762.
SMRi P06762. Positions 7-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246615. 1 interaction.
MINTi MINT-4996356.
STRINGi 10116.ENSRNOP00000019192.

Chemistry

BindingDBi P06762.
ChEMBLi CHEMBL5035.

PTM databases

PhosphoSitei P06762.

Proteomic databases

PaxDbi P06762.
PRIDEi P06762.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 COG5398.
GeneTreei ENSGT00390000017673.
HOGENOMi HOG000233221.
HOVERGENi HBG005982.
InParanoidi P06762.
KOi K00510.
OMAi YAPLYFP.
OrthoDBi EOG7JQBNR.
PhylomeDBi P06762.
TreeFami TF314786.

Enzyme and pathway databases

SABIO-RK P06762.

Miscellaneous databases

EvolutionaryTracei P06762.
NextBioi 603359.
PROi P06762.

Gene expression databases

Genevestigatori P06762.

Family and domain databases

Gene3Di 1.20.910.10. 1 hit.
InterProi IPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view ]
PANTHERi PTHR10720. PTHR10720. 1 hit.
Pfami PF01126. Heme_oxygenase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000343. Haem_Oase. 1 hit.
PRINTSi PR00088. HAEMOXYGNASE.
SUPFAMi SSF48613. SSF48613. 1 hit.
PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHMOX1_RAT
AccessioniPrimary (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: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [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

External Data

Dasty 3