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Protein

Heme oxygenase 2

Gene

Hmox2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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 [reduced NADPH--hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H2O.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi44Iron (heme axial ligand)By similarity1

GO - Molecular functioni

  • heme binding Source: GO_Central
  • heme oxygenase (decyclizing) activity Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • heme catabolic process Source: GO_Central
  • heme oxidation Source: RGD
  • iron ion homeostasis Source: GO_Central
  • response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 5301.
ReactomeiR-RNO-189483. Heme degradation.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-917937. Iron uptake and transport.
SABIO-RKP23711.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 2 (EC:1.14.14.18By similarity)
Short name:
HO-2
Gene namesi
Name:Hmox2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi67402. Hmox2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3348.
GuidetoPHARMACOLOGYi1442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002096942 – 315Heme oxygenase 2Add BLAST314

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP23711.
PRIDEiP23711.

PTM databases

iPTMnetiP23711.
PhosphoSitePlusiP23711.

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

BgeeiENSRNOG00000003773.
GenevisibleiP23711. RN.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP23711.

Structurei

3D structure databases

ProteinModelPortaliP23711.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati263 – 268HRM 16
Repeati280 – 285HRM 26

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP23711.
KOiK00510.
OMAiMEYFFGE.
OrthoDBiEOG091G0AS0.
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]
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

        10         20         30         40         50
MSSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT
60 70 80 90 100
QFVKDFLKGN IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT
110 120 130 140 150
ELHRKEALIK DMEYFFGENW EEQVKCSEAA QKYVDRIHYV GQNEPELLVA
160 170 180 190 200
HAYTRYMGDL SGGQVLKKVA QRALKLPSTG EGTQFYLFEH VDNAQQFKQF
210 220 230 240 250
YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG SMLTKETLED
260 270 280 290 300
GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA
310
ASVALVAGLL AWYYM
Length:315
Mass (Da):35,762
Last modified:November 1, 1991 - v1
Checksum:i981AADE01DE1AFCF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti142 – 146QNEPE → EFRNK in AAA41347 (PubMed:3343248).Curated5
Sequence conflicti230 – 232MQI → TEF in AAA41347 (PubMed:3343248).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006245827.3.
UniGeneiRn.10241.

Genome annotation databases

EnsembliENSRNOT00000005031; ENSRNOP00000005031; ENSRNOG00000003773.
ENSRNOT00000077164; ENSRNOP00000075102; ENSRNOG00000003773.
GeneIDi79239.
KEGGirno:79239.
UCSCiRGD:67402. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006245827.3.
UniGeneiRn.10241.

3D structure databases

ProteinModelPortaliP23711.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP23711.
ChEMBLiCHEMBL3348.
GuidetoPHARMACOLOGYi1442.

PTM databases

iPTMnetiP23711.
PhosphoSitePlusiP23711.

Proteomic databases

PaxDbiP23711.
PRIDEiP23711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005031; ENSRNOP00000005031; ENSRNOG00000003773.
ENSRNOT00000077164; ENSRNOP00000075102; ENSRNOG00000003773.
GeneIDi79239.
KEGGirno:79239.
UCSCiRGD:67402. rat.

Organism-specific databases

CTDi3163.
RGDi67402. Hmox2.

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP23711.
KOiK00510.
OMAiMEYFFGE.
OrthoDBiEOG091G0AS0.
PhylomeDBiP23711.
TreeFamiTF314786.

Enzyme and pathway databases

BRENDAi1.14.99.3. 5301.
ReactomeiR-RNO-189483. Heme degradation.
R-RNO-6798695. Neutrophil degranulation.
R-RNO-917937. Iron uptake and transport.
SABIO-RKP23711.

Miscellaneous databases

PROiP23711.

Gene expression databases

BgeeiENSRNOG00000003773.
GenevisibleiP23711. RN.

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]
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.