Q5E9F2 (HMOX1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heme oxygenase 1
Short name=HO-1
EC=1.14.99.3

Gene names

Name:

HMOX1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.
Subcellular location	Microsome By similarity. Endoplasmic reticulum By similarity.
Sequence similarities	Belongs to the heme oxygenase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme oxygenase (decyclizing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 289	289	Heme oxygenase 1		PRO_0000209686
Sites
	Metal binding	26	1	Iron (heme axial ligand) By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	40	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	28	1	Q → E AA sequence Ref.3
	Sequence conflict	100	1	P → PH AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q5E9F2 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 8EAEA06BCCA4B96C	FASTA	289	32,940
	10 20 30 40 50 60 MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL VMASLYHIYV 70 80 90 100 110 120 ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP RWQEAIPYTQ ATKRYVQRLQ 130 140 150 160 170 180 EVGRTEPELL VAHAYTRYLG DLSGGQVLKK IAQKALNLPS SGEGLAFFTF PNIASATKFK 190 200 210 220 230 240 QLYRSRMNTL EMTPEVRQRV LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR 250 260 270 280 AGSKVQDLAP TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] 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: 1700666] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND 200-205. Tissue: Spleen.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT020968 mRNA. Translation: AAX08985.1. BC102105 mRNA. Translation: AAI02106.4.
IPI	IPI00690186.
PIR	S13265.
RefSeq	NP_001014912.1. NM_001014912.1.
UniGene	Bt.4001.
3D structure databases
ProteinModelPortal	Q5E9F2.
SMR	Q5E9F2. Positions 1-224.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5E9F2.
Proteomic databases
PRIDE	Q5E9F2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneID	513221.
KEGG	bta:513221.
Organism-specific databases
CTD	3162.
Phylogenomic databases
eggNOG	maNOG09761.
GeneTree	ENSGT00390000017673.
HOVERGEN	HBG005982.
InParanoid	Q5E9F2.
OrthoDB	EOG4TF0KR.
Family and domain databases
InterPro	IPR002051. Haem_Oase. IPR016053. Haem_Oase-like. IPR016084. Haem_Oase-like_multi-hlx. IPR018207. Haem_oxygenase_CS. [Graphical view]
Gene3D	G3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
KO	K00510.
PANTHER	PTHR10720. Haem_Oase. 1 hit.
Pfam	PF01126. Heme_oxygenase. 1 hit. [Graphical view]
PIRSF	PIRSF000343. Haem_Oase. 1 hit.
PRINTS	PR00088. HAEMOXYGNASE.
SUPFAM	SSF48613. Heme_oxygenase. 1 hit.
PROSITE	PS00593. HEME_OXYGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMOX1_BOVIN

Accession

Primary (citable) accession number: Q5E9F2
Secondary accession number(s): Q3ZCK7, Q7M338

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 15, 2005
Last modified:	November 16, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program