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P43242

- HMOX2_RABIT

UniProt

P43242 - HMOX2_RABIT

Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi41 – 411Iron (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
    2. response to hypoxia Source: Ensembl

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 312311Heme oxygenase 2PRO_0000209693Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP43242.

    Interactioni

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000005212.

    Structurei

    3D structure databases

    ProteinModelPortaliP43242.
    SMRiP43242. Positions 26-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati260 – 2656HRM 1
    Repeati277 – 2826HRM 2

    Sequence similaritiesi

    Belongs to the heme oxygenase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5398.
    HOGENOMiHOG000233221.
    HOVERGENiHBG005982.

    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.

    P43242-1 [UniParc]FASTAAdd to Basket

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    MSAEVETSEG VDEPEEKNFG ENHIRMADLS ELLKEGTKEA HDRAENTKFV    50
    KDFLKGNIKK EIFKLATTAL YFTYSALEEE MDRNKDHPAF APLYFPMELH 100
    RKEALTKDME YFFGENWEEQ VQCSEAAQKY VERIHYIGQN EPELLVAHAY 150
    TRYMGDLSGG QVLKKVAQRA LKLPSTGEGT QFYLFENVDN AQQFKQFYRA 200
    RMNALDLNLK TKERIVEEAN KAFEYNMQIF SELDQAGSAP ASETVEDRIP 250
    VHDGKGDVRK CPYYAAGQVN GALEGSSCPF RAAMAVLRKP SLQLVLAAAV 300
    ALAAGLLAWY YM 312
    Length:312
    Mass (Da):35,373
    Last modified:November 1, 1995 - v1
    Checksum:i2D33FF39FA1F5505
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S61699 mRNA. Translation: AAB20093.1.
    PIRiS18387.
    RefSeqiNP_001076216.1. NM_001082747.1.
    UniGeneiOcu.3307.

    Genome annotation databases

    GeneIDi100009523.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S61699 mRNA. Translation: AAB20093.1 .
    PIRi S18387.
    RefSeqi NP_001076216.1. NM_001082747.1.
    UniGenei Ocu.3307.

    3D structure databases

    ProteinModelPortali P43242.
    SMRi P43242. Positions 26-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000005212.

    Proteomic databases

    PRIDEi P43242.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009523.

    Organism-specific databases

    CTDi 3163.

    Phylogenomic databases

    eggNOGi COG5398.
    HOGENOMi HOG000233221.
    HOVERGENi HBG005982.

    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. "Characterization of a cDNA-encoding rabbit brain heme oxygenase-2 and identification of a conserved domain among mammalian heme oxygenase isozymes: possible heme-binding site?"
      Rotenberg M.O., Maines M.D.
      Arch. Biochem. Biophys. 290:336-344(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiHMOX2_RABIT
    AccessioniPrimary (citable) accession number: P43242
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 85 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3