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P23711

- HMOX2_RAT

UniProt

P23711 - HMOX2_RAT

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Protein

Heme oxygenase 2

Gene
Hmox2
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. 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 bindingi44 – 441Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. heme oxygenase (decyclizing) activity Source: RGD
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct

GO - Biological processi

  1. heme oxidation Source: RGD
  2. response to hypoxia Source: Ensembl
  3. response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP23711.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 2 (EC:1.14.99.3)
Short name:
HO-2
Gene namesi
Name:Hmox2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi67402. Hmox2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
  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 – 11Removed By similarity
Chaini2 – 315314Heme oxygenase 2PRO_0000209694Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23711.
PRIDEiP23711.

Expressioni

Tissue specificityi

Widely distributed in body with a high concentration in the brain.

Inductioni

Heme oxygenase 2 activity is non-inducible.

Gene expression databases

GenevestigatoriP23711.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CALMP621573EBI-2910092,EBI-397403From a different organism.
Calm3P621612EBI-2910092,EBI-397530

Protein-protein interaction databases

IntActiP23711. 2 interactions.
MINTiMINT-4565100.
STRINGi10116.ENSRNOP00000005031.

Structurei

3D structure databases

ProteinModelPortaliP23711.
SMRiP23711. Positions 29-247.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati263 – 2686HRM 1
Repeati280 – 2856HRM 2

Sequence similaritiesi

Belongs to the heme oxygenase family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5398.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP23711.
KOiK00510.
OMAiMDRNKDH.
OrthoDBiEOG7JQBNR.
PhylomeDBiP23711.
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.

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

P23711-1 [UniParc]FASTAAdd to Basket

« Hide

MSSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT    50
QFVKDFLKGN IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT 100
ELHRKEALIK DMEYFFGENW EEQVKCSEAA QKYVDRIHYV GQNEPELLVA 150
HAYTRYMGDL SGGQVLKKVA QRALKLPSTG EGTQFYLFEH VDNAQQFKQF 200
YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG SMLTKETLED 250
GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA 300
ASVALVAGLL AWYYM 315
Length:315
Mass (Da):35,762
Last modified:November 1, 1991 - v1
Checksum:i981AADE01DE1AFCF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1465QNEPE → EFRNK in AAA41347. 1 Publication
Sequence conflicti230 – 2323MQI → TEF in AAA41347. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05405 mRNA. Translation: AAA41340.1.
U05013 Genomic DNA. Translation: AAA19130.1.
BC062061 mRNA. Translation: AAH62061.1.
M18918 mRNA. Translation: AAA41347.1.
PIRiA35199.
RefSeqiNP_001264002.1. NM_001277073.1.
NP_077363.1. NM_024387.2.
XP_006245889.1. XM_006245827.1.
UniGeneiRn.10241.

Genome annotation databases

EnsembliENSRNOT00000005031; ENSRNOP00000005031; ENSRNOG00000003773.
GeneIDi79239.
KEGGirno:79239.
UCSCiRGD:67402. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05405 mRNA. Translation: AAA41340.1 .
U05013 Genomic DNA. Translation: AAA19130.1 .
BC062061 mRNA. Translation: AAH62061.1 .
M18918 mRNA. Translation: AAA41347.1 .
PIRi A35199.
RefSeqi NP_001264002.1. NM_001277073.1.
NP_077363.1. NM_024387.2.
XP_006245889.1. XM_006245827.1.
UniGenei Rn.10241.

3D structure databases

ProteinModelPortali P23711.
SMRi P23711. Positions 29-247.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P23711. 2 interactions.
MINTi MINT-4565100.
STRINGi 10116.ENSRNOP00000005031.

Chemistry

BindingDBi P23711.
ChEMBLi CHEMBL3348.

Proteomic databases

PaxDbi P23711.
PRIDEi P23711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000005031 ; ENSRNOP00000005031 ; ENSRNOG00000003773 .
GeneIDi 79239.
KEGGi rno:79239.
UCSCi RGD:67402. rat.

Organism-specific databases

CTDi 3163.
RGDi 67402. Hmox2.

Phylogenomic databases

eggNOGi COG5398.
GeneTreei ENSGT00390000017673.
HOGENOMi HOG000233221.
HOVERGENi HBG005982.
InParanoidi P23711.
KOi K00510.
OMAi MDRNKDH.
OrthoDBi EOG7JQBNR.
PhylomeDBi P23711.
TreeFami TF314786.

Enzyme and pathway databases

SABIO-RK P23711.

Miscellaneous databases

NextBioi 614672.
PROi P23711.

Gene expression databases

Genevestigatori P23711.

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. "Isolation, characterization, and expression in Escherichia coli of a cDNA encoding rat heme oxygenase-2."
    Rotenberg M.O., Maines M.D.
    J. Biol. Chem. 265:7501-7506(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "The structure, organization and differential expression of the gene encoding rat heme oxygenase-2."
    McCoubrey W.K. Jr., Maines M.D.
    Gene 139:155-161(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  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: Prostate.
  4. "Evidence suggesting that the two forms of heme oxygenase are products of different genes."
    Cruse I., Maines M.D.
    J. Biol. Chem. 263:3348-3353(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-232, PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver and Testis.

Entry informationi

Entry nameiHMOX2_RAT
AccessioniPrimary (citable) accession number: P23711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 117 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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