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Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Iron (heme axial ligand)By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. heme oxidation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP14791.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.99.3)
Short name:
HO-1
Gene namesi
Name:HMOX1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Heme oxygenase 1PRO_0000209696Add
BLAST

Proteomic databases

PaxDbiP14791.
PRIDEiP14791.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036970.

Structurei

3D structure databases

ProteinModelPortaliP14791.
SMRiP14791. Positions 1-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP14791.
KOiK00510.
PhylomeDBiP14791.

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.

P14791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METSQPHNAE SMSQDLSELL KEATKEVHEQ AENTPFMKNF QKGQVSLHEF
60 70 80 90 100
KLVTASLYFI YSALEEEIER NKDNPVYAPV YFPMELHRKA ALEKDLEYFY
110 120 130 140 150
GSNWRAEIPC PEATQKYVER LHVVGKKHPE LLVAHAYTRY LGDLSGGQVL
160 170 180 190 200
KKIAQKALQL PSTGEGLAFF TFDGVSNATK FKQLYRSRMN ALEMDHATKK
210 220 230 240 250
RVLEEAKKAF LLNIQVFEAL QKLVSKSQEN GHAVQPKAEL RTRSVNKSHE
260 270 280 290
NSPAAGKESE RTSRMQADML TTSPLVRWLL ALGFIATTVA VGLFAM
Length:296
Mass (Da):33,509
Last modified:February 29, 1992 - v2
Checksum:i22DAA9324494CC0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56201 mRNA. Translation: CAA39661.1.
PIRiS15123.
RefSeqiNP_990675.1. NM_205344.1.
UniGeneiGga.2039.

Genome annotation databases

GeneIDi396287.
KEGGigga:396287.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56201 mRNA. Translation: CAA39661.1.
PIRiS15123.
RefSeqiNP_990675.1. NM_205344.1.
UniGeneiGga.2039.

3D structure databases

ProteinModelPortaliP14791.
SMRiP14791. Positions 1-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000036970.

Proteomic databases

PaxDbiP14791.
PRIDEiP14791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396287.
KEGGigga:396287.

Organism-specific databases

CTDi3162.

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP14791.
KOiK00510.
PhylomeDBiP14791.

Enzyme and pathway databases

SABIO-RKP14791.

Miscellaneous databases

NextBioi20816338.
PROiP14791.

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...

Publicationsi

  1. "Cloning, sequencing and expression of cDNA for chick liver haem oxygenase. Comparison of avian and mammalian cDNAs and deduced proteins."
    Evans C.O., Healey J.F., Greene Y., Bonkovsky H.L.
    Biochem. J. 273:659-666(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Purification and characterization of heme oxygenase from chick liver. Comparison of the avian and mammalian enzymes."
    Bonkovsky H.L., Healey J.F., Pohl J.
    Eur. J. Biochem. 189:155-166(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiHMOX1_CHICK
AccessioniPrimary (citable) accession number: P14791
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 31, 1990
Last sequence update: February 29, 1992
Last modified: March 31, 2015
This is version 96 of the entry and version 2 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

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.