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Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: 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 (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

GO - Biological processi

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
ORF Names:QbsB-11392
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

        10         20         30         40         50
MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN
60 70 80 90 100
TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPTFAPLYFP
110 120 130 140 150
MELHRKEALT KDMEYFFGEN WEEQVQCPKA AKKYVERIHY IGQNEPELLV
160 170 180 190 200
AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ
210 220 230 240 250
LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE
260 270 280 290 300
DGFPVHDGKG DMRKCPFYAG EQDKGALEGS SCPFRTAMAV LRKPSLQFIL
310
AAGMALAAGL LAWYYM
Length:316
Mass (Da):36,081
Last modified:February 7, 2006 - v1
Checksum:i40A85866272B219E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB220384 mRNA. Translation: BAE72917.1.
RefSeqiNP_001270155.1. NM_001283226.1.
UniGeneiMfa.8715.

3D structure databases

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

Proteomic databases

PRIDEiQ2PG53.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102143766.
KEGGimcf:102143766.

Organism-specific databases

CTDi3163.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 40 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

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 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.