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Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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. 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 sitei19 – 191HemeBy similarity
Metal bindingi26 – 261Iron (heme axial ligand)By similarity
Binding sitei135 – 1351HemeBy similarity
Binding sitei184 – 1841HemeBy similarity

GO - Molecular functioni

  1. heme binding Source: Ensembl
  2. heme oxygenase (decyclizing) activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. signal transducer activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to arsenic-containing substance Source: Ensembl
  3. cellular response to cadmium ion Source: Ensembl
  4. cellular response to hypoxia Source: Ensembl
  5. erythrocyte homeostasis Source: Ensembl
  6. heme catabolic process Source: Ensembl
  7. heme oxidation Source: InterPro
  8. iron ion homeostasis Source: Ensembl
  9. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  10. negative regulation of smooth muscle cell proliferation Source: Ensembl
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  12. positive regulation of smooth muscle cell proliferation Source: Ensembl
  13. protein homooligomerization Source: Ensembl
  14. regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
  15. response to nicotine Source: Ensembl
  16. response to oxidative stress Source: Ensembl
  17. wound healing involved in inflammatory response Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 908.
ReactomeiREACT_286479. Heme degradation.
REACT_353286. Iron uptake and transport.
SABIO-RKQ5E9F2.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.99.3)
Short name:
HO-1
Gene namesi
Name:HMOX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. nucleus Source: Ensembl
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Heme oxygenase 1PRO_0000209686Add
BLAST

Proteomic databases

PRIDEiQ5E9F2.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020701.

Structurei

3D structure databases

ProteinModelPortaliQ5E9F2.
SMRiQ5E9F2. Positions 1-224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG5398.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiQ5E9F2.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG7JQBNR.
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.

Q5E9F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL
60 70 80 90 100
VMASLYHIYV ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP
110 120 130 140 150
RWQEAIPYTQ ATKRYVQRLQ EVGRTEPELL VAHAYTRYLG DLSGGQVLKK
160 170 180 190 200
IAQKALNLPS SGEGLAFFTF PNIASATKFK QLYRSRMNTL EMTPEVRQRV
210 220 230 240 250
LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR AGSKVQDLAP
260 270 280
TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM
Length:289
Mass (Da):32,940
Last modified:March 15, 2005 - v1
Checksum:i8EAEA06BCCA4B96C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281Q → E AA sequence (PubMed:1700666).Curated
Sequence conflicti100 – 1001P → PH AA sequence (PubMed:1700666).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
PIRiS13265.
RefSeqiNP_001014912.1. NM_001014912.1.
UniGeneiBt.4001.

Genome annotation databases

EnsembliENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneIDi513221.
KEGGibta:513221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
PIRiS13265.
RefSeqiNP_001014912.1. NM_001014912.1.
UniGeneiBt.4001.

3D structure databases

ProteinModelPortaliQ5E9F2.
SMRiQ5E9F2. Positions 1-224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020701.

Chemistry

ChEMBLiCHEMBL1255146.

Proteomic databases

PRIDEiQ5E9F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneIDi513221.
KEGGibta:513221.

Organism-specific databases

CTDi3162.

Phylogenomic databases

eggNOGiCOG5398.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiQ5E9F2.
KOiK00510.
OMAiYAPLYFP.
OrthoDBiEOG7JQBNR.
TreeFamiTF314786.

Enzyme and pathway databases

BRENDAi1.14.99.3. 908.
ReactomeiREACT_286479. Heme degradation.
REACT_353286. Iron uptake and transport.
SABIO-RKQ5E9F2.

Miscellaneous databases

NextBioi20870758.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Structural studies on bovine spleen heme oxygenase. Immunological and structural diversity among mammalian heme oxygenase enzymes."
    Schacter B.A., Cripps V., Troxler R.F., Offner G.D.
    Arch. Biochem. Biophys. 282:404-412(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND 200-205.
    Tissue: Spleen.

Entry informationi

Entry nameiHMOX1_BOVIN
AccessioniPrimary (citable) accession number: Q5E9F2
Secondary accession number(s): Q3ZCK7, Q7M338
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 15, 2005
Last modified: April 1, 2015
This is version 73 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

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.