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Q5R7E3

- HMOX1_PONAB

UniProt

Q5R7E3 - HMOX1_PONAB

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Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis (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
Binding sitei18 – 181HemeBy similarity
Metal bindingi25 – 251Iron (heme axial ligand)
Binding sitei134 – 1341HemeBy similarity
Binding sitei183 – 1831HemeBy similarity

GO - Molecular functioni

  1. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. heme oxidation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.99.3)
Short name:
HO-1
Gene namesi
Name:HMOX1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Heme oxygenase 1PRO_0000317707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5R7E3.

Structurei

3D structure databases

ProteinModelPortaliQ5R7E3.
SMRiQ5R7E3. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiQ5R7E3.
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.

Q5R7E3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTREGFKLV
60 70 80 90 100
MASLYHIYVA LEEEIEHNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR
110 120 130 140 150
WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI
160 170 180 190 200
AQKALGLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI
210 220 230 240 250
EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKAQDSAPV
260 270 280
ETPRGKTPLN THSQAPLLRW VLTLSFLVAT VAVGLYAM
Length:288
Mass (Da):32,712
Last modified:December 21, 2004 - v1
Checksum:i10400CCCCA98F7F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860175 mRNA. Translation: CAH92317.1.
RefSeqiNP_001126358.1. NM_001132886.1.

Genome annotation databases

GeneIDi100173339.
KEGGipon:100173339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR860175 mRNA. Translation: CAH92317.1 .
RefSeqi NP_001126358.1. NM_001132886.1.

3D structure databases

ProteinModelPortali Q5R7E3.
SMRi Q5R7E3. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R7E3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100173339.
KEGGi pon:100173339.

Organism-specific databases

CTDi 3162.

Phylogenomic databases

HOGENOMi HOG000233221.
HOVERGENi HBG005982.
InParanoidi Q5R7E3.
KOi K00510.

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiHMOX1_PONAB
AccessioniPrimary (citable) accession number: Q5R7E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 51 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