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P43242

- HMOX2_RABIT

UniProt

P43242 - HMOX2_RABIT

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Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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. 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
Complete GO annotation...

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-KW
  2. plasma membrane Source: Ensembl
Complete GO annotation...

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.
InParanoidiP43242.

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAEVETSEG VDEPEEKNFG ENHIRMADLS ELLKEGTKEA HDRAENTKFV
60 70 80 90 100
KDFLKGNIKK EIFKLATTAL YFTYSALEEE MDRNKDHPAF APLYFPMELH
110 120 130 140 150
RKEALTKDME YFFGENWEEQ VQCSEAAQKY VERIHYIGQN EPELLVAHAY
160 170 180 190 200
TRYMGDLSGG QVLKKVAQRA LKLPSTGEGT QFYLFENVDN AQQFKQFYRA
210 220 230 240 250
RMNALDLNLK TKERIVEEAN KAFEYNMQIF SELDQAGSAP ASETVEDRIP
260 270 280 290 300
VHDGKGDVRK CPYYAAGQVN GALEGSSCPF RAAMAVLRKP SLQLVLAAAV
310
ALAAGLLAWY YM
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.
InParanoidi P43242.

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 29, 2014
This is version 86 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