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P06762

- HMOX1_RAT

UniProt

P06762 - HMOX1_RAT

Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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. protein binding Source: RGD
    8. 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 oxidative stress Source: BHF-UCL
    30. response to estrogen Source: RGD
    31. response to hydrogen peroxide Source: BHF-UCL
    32. response to hypoxia Source: RGD
    33. response to nicotine Source: Ensembl
    34. response to oxidative stress Source: RGD
    35. small GTPase mediated signal transduction Source: RGD
    36. wound healing involved in inflammatory response Source: Ensembl

    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. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. nucleolus Source: RGD
    6. nucleus Source: BHF-UCL
    7. plasma membrane Source: RGD

    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[»]
    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

    MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV    50
    MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH 100
    WQEAIPYTPA TQHYVKRLHE VGGTHPELLV AHAYTRYLGD LSGGQVLKKI 150
    AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ LYRARMNTLE MTPEVKHRVT 200
    EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP ASLVQDTTSA 250
    ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM 289
    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 [» ]
    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

    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 1, 2014
    This is version 127 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