HMOX1_BOVIN
ID HMOX1_BOVIN Reviewed; 289 AA.
AC Q5E9F2; Q3ZCK7; Q7M338;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Heme oxygenase 1;
DE Short=HO-1;
DE EC=1.14.14.18 {ECO:0000269|PubMed:6806282};
DE Contains:
DE RecName: Full=Heme oxygenase 1 soluble form {ECO:0000250|UniProtKB:P09601};
GN Name=HMOX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-33; 41-49; 88-113; 138-147; 155-158; 187-196 AND
RP 200-205.
RC TISSUE=Spleen;
RX PubMed=1700666; DOI=10.1016/0003-9861(90)90136-m;
RA Schacter B.A., Cripps V., Troxler R.F., Offner G.D.;
RT "Structural studies on bovine spleen heme oxygenase. Immunological and
RT structural diversity among mammalian heme oxygenase enzymes.";
RL Arch. Biochem. Biophys. 282:404-412(1990).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=6806282; DOI=10.1016/s0021-9258(18)34449-1;
RA Yoshinaga T., Sassa S., Kappas A.;
RT "Purification and properties of bovine spleen heme oxygenase. Amino acid
RT composition and sites of action of inhibitors of heme oxidation.";
RL J. Biol. Chem. 257:7778-7785(1982).
CC -!- FUNCTION: [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme
CC at the alpha-methene bridge carbon, released as carbon monoxide (CO),
CC to generate biliverdin IXalpha, while releasing the central heme iron
CC chelate as ferrous iron (PubMed:6806282). Affords protection against
CC programmed cell death and this cytoprotective effect relies on its
CC ability to catabolize free heme and prevent it from sensitizing cells
CC to undergo apoptosis (By similarity). {ECO:0000250|UniProtKB:P09601,
CC ECO:0000269|PubMed:6806282}.
CC -!- FUNCTION: [Heme oxygenase 1 soluble form]: Catalyzes the oxidative
CC cleavage of heme at the alpha-methene bridge carbon, released as carbon
CC monoxide (CO), to generate biliverdin IXalpha, while releasing the
CC central heme iron chelate as ferrous iron.
CC {ECO:0000250|UniProtKB:P09601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000269|PubMed:6806282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000305|PubMed:6806282};
CC -!- ACTIVITY REGULATION: Inhibited by metalloporphyrins such as Sn-, Co-,
CC Mn- and Zn-protoporphyrins. {ECO:0000269|PubMed:6806282}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.93 uM for heme b {ECO:0000269|PubMed:6806282};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
CC -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC anchor. {ECO:0000250|UniProtKB:P09601}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR EMBL; BT020968; AAX08985.1; -; mRNA.
DR EMBL; BC102105; AAI02106.4; -; mRNA.
DR PIR; S13265; S13265.
DR RefSeq; NP_001014912.1; NM_001014912.1.
DR AlphaFoldDB; Q5E9F2; -.
DR SMR; Q5E9F2; -.
DR STRING; 9913.ENSBTAP00000020701; -.
DR ChEMBL; CHEMBL1255146; -.
DR PaxDb; Q5E9F2; -.
DR PRIDE; Q5E9F2; -.
DR Ensembl; ENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
DR GeneID; 513221; -.
DR KEGG; bta:513221; -.
DR CTD; 3162; -.
DR VEuPathDB; HostDB:ENSBTAG00000015582; -.
DR VGNC; VGNC:29885; HMOX1.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_057050_0_1_1; -.
DR InParanoid; Q5E9F2; -.
DR OrthoDB; 1424194at2759; -.
DR TreeFam; TF314786; -.
DR BRENDA; 1.14.14.18; 908.
DR SABIO-RK; Q5E9F2; -.
DR Proteomes; UP000009136; Chromosome 5.
DR ExpressionAtlas; Q5E9F2; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042167; P:heme catabolic process; IBA:GO_Central.
DR GO; GO:0006788; P:heme oxidation; IBA:GO_Central.
DR GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:AgBase.
DR GO; GO:1903901; P:negative regulation of viral life cycle; IMP:AgBase.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR Gene3D; 1.20.910.10; -; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR018207; Haem_oxygenase_CS.
DR PANTHER; PTHR10720; PTHR10720; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; SSF48613; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Heme oxygenase 1"
FT /id="PRO_0000209686"
FT CHAIN 1..266
FT /note="Heme oxygenase 1 soluble form"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT /id="PRO_0000455620"
FT TOPO_DOM 1..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT TRANSMEM 267..289
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT BINDING 26
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT BINDING 135
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT BINDING 184
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT SITE 141
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06762"
FT CONFLICT 28
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="P -> PH (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32940 MW; 8EAEA06BCCA4B96C CRC64;
MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL VMASLYHIYV
ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP RWQEAIPYTQ ATKRYVQRLQ
EVGRTEPELL VAHAYTRYLG DLSGGQVLKK IAQKALNLPS SGEGLAFFTF PNIASATKFK
QLYRSRMNTL EMTPEVRQRV LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR
AGSKVQDLAP TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM
