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P32394

- HMOX1_PIG

UniProt

P32394 - HMOX1_PIG

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Protein

Heme oxygenase 1

Gene
HMOX1
Organism
Sus scrofa (Pig)
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.

Catalytic activityi

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Heme By similarity
Metal bindingi25 – 251Iron (heme axial ligand) By similarity
Binding sitei134 – 1341Heme By similarity
Binding sitei183 – 1831Heme By 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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Heme oxygenase 1PRO_0000209689Add
BLAST

Expressioni

Inductioni

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin.

Structurei

3D structure databases

ProteinModelPortaliP32394.
SMRiP32394. Positions 1-223.

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.

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.

P32394-1 [UniParc]FASTAAdd to Basket

« Hide

MEHSQPNSMP QDLSEALKEA TKEVHVQAEN AEFMKNFQKG EVTREGFKLV    50
MASLYHIYDA LEEEIEHNKE NPVYTPLYFP EELHRRAALE QDMAFWYGPR 100
WQEAIPYTQA TKRYVRRLQQ VGRFEPELLV AHAYTRYMGD LSGGQVLKKI 150
AQKALDLPSS GEGLAFFTFP NVANATKFKQ LYRSRMNTLE MTPEVKQRVL 200
EEAKTAFLLN IQLFEEVQEL LTQDTKDQRP SQASDIRKRA GSRVQDSTPV 250
TTPRGKPQLS VLSQVPLIRW VLTLSFLVAT VAMGLYAM 288
Length:288
Mass (Da):33,074
Last modified:October 1, 1993 - v1
Checksum:i156D6175A308E0D2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60677 mRNA. Translation: CAA43092.1.
PIRiS37687.
RefSeqiNP_001004027.1. NM_001004027.1.
UniGeneiSsc.115.

Genome annotation databases

GeneIDi445512.
KEGGissc:445512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60677 mRNA. Translation: CAA43092.1 .
PIRi S37687.
RefSeqi NP_001004027.1. NM_001004027.1.
UniGenei Ssc.115.

3D structure databases

ProteinModelPortali P32394.
SMRi P32394. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 445512.
KEGGi ssc:445512.

Organism-specific databases

CTDi 3162.

Phylogenomic databases

HOVERGENi HBG005982.
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. "Nucleotide sequence of cDNA for porcine heme oxygenase and its expression in Escherichia coli."
    Suzuki T., Sato M., Ishikawa K., Yoshida T.
    Biochem. Int. 28:887-893(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiHMOX1_PIG
AccessioniPrimary (citable) accession number: P32394
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 16, 2013
This is version 82 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

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