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Q2PG53

- HMOX2_MACFA

UniProt

Q2PG53 - HMOX2_MACFA

Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter By similarity.By similarity

    Catalytic activityi

    Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Iron (heme axial ligand)By similarity

    GO - Molecular functioni

    1. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. heme oxidation Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heme oxygenase 2 (EC:1.14.99.3)
    Short name:
    HO-2
    Gene namesi
    Name:HMOX2
    ORF Names:QbsB-11392
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 316315Heme oxygenase 2PRO_0000317708Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ2PG53.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2PG53.
    SMRiQ2PG53. Positions 30-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati264 – 2696HRM 1
    Repeati281 – 2866HRM 2

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG005982.
    KOiK00510.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q2PG53-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN    50
    TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPTFAPLYFP 100
    MELHRKEALT KDMEYFFGEN WEEQVQCPKA AKKYVERIHY IGQNEPELLV 150
    AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ 200
    LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE 250
    DGFPVHDGKG DMRKCPFYAG EQDKGALEGS SCPFRTAMAV LRKPSLQFIL 300
    AAGMALAAGL LAWYYM 316
    Length:316
    Mass (Da):36,081
    Last modified:February 7, 2006 - v1
    Checksum:i40A85866272B219E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB220384 mRNA. Translation: BAE72917.1.
    RefSeqiNP_001270155.1. NM_001283226.1.
    UniGeneiMfa.8715.

    Genome annotation databases

    GeneIDi102143766.
    KEGGimcf:102143766.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB220384 mRNA. Translation: BAE72917.1 .
    RefSeqi NP_001270155.1. NM_001283226.1.
    UniGenei Mfa.8715.

    3D structure databases

    ProteinModelPortali Q2PG53.
    SMRi Q2PG53. Positions 30-248.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q2PG53.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102143766.
    KEGGi mcf:102143766.

    Organism-specific databases

    CTDi 3163.

    Phylogenomic databases

    HOVERGENi HBG005982.
    KOi K00510.

    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. "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA oligo-chips."
      Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S., Hashimoto K.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain stem.

    Entry informationi

    Entry nameiHMOX2_MACFA
    AccessioniPrimary (citable) accession number: Q2PG53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3