HMOX1_CHICK
ID HMOX1_CHICK Reviewed; 296 AA.
AC P14791;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heme oxygenase 1;
DE Short=HO-1;
DE EC=1.14.14.18 {ECO:0000269|PubMed:1996964, ECO:0000269|PubMed:2158889};
DE Contains:
DE RecName: Full=Heme oxygenase 1 soluble form {ECO:0000250|UniProtKB:P09601};
GN Name=HMOX1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=1996964; DOI=10.1042/bj2730659;
RA Evans C.O., Healey J.F., Greene Y., Bonkovsky H.L.;
RT "Cloning, sequencing and expression of cDNA for chick liver haem oxygenase.
RT Comparison of avian and mammalian cDNAs and deduced proteins.";
RL Biochem. J. 273:659-666(1991).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=2158889; DOI=10.1111/j.1432-1033.1990.tb15472.x;
RA Bonkovsky H.L., Healey J.F., Pohl J.;
RT "Purification and characterization of heme oxygenase from chick liver.
RT Comparison of the avian and mammalian enzymes.";
RL Eur. J. Biochem. 189:155-166(1990).
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:1996964, PubMed:2158889). Affords
CC protection against programmed cell death and this cytoprotective effect
CC relies on its ability to catabolize free heme and prevent it from
CC sensitizing cells to undergo apoptosis (By similarity).
CC {ECO:0000250|UniProtKB:P09601, ECO:0000269|PubMed:1996964,
CC ECO:0000269|PubMed:2158889}.
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:1996964, ECO:0000269|PubMed:2158889};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000305|PubMed:1996964};
CC -!- ACTIVITY REGULATION: Inhibited by metalloporphyrins in the following
CC order of decreasing potency: tin mesoporphyrin > tin protoporphyrin >
CC zinc protoporphyrin > manganese protoporphyrin > cobalt protoporphyrin.
CC {ECO:0000269|PubMed:2158889}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for heme b {ECO:0000269|PubMed:2158889};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:2158889};
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; X56201; CAA39661.1; -; mRNA.
DR PIR; S15123; S15123.
DR RefSeq; NP_990675.1; NM_205344.1.
DR AlphaFoldDB; P14791; -.
DR SMR; P14791; -.
DR STRING; 9031.ENSGALP00000036970; -.
DR PaxDb; P14791; -.
DR GeneID; 396287; -.
DR KEGG; gga:396287; -.
DR CTD; 3162; -.
DR VEuPathDB; HostDB:geneid_396287; -.
DR eggNOG; KOG4480; Eukaryota.
DR InParanoid; P14791; -.
DR OrthoDB; 1424194at2759; -.
DR PhylomeDB; P14791; -.
DR SABIO-RK; P14791; -.
DR PRO; PR:P14791; -.
DR Proteomes; UP000000539; Unplaced.
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: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:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd19165; HemeO; 1.
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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..296
FT /note="Heme oxygenase 1"
FT /id="PRO_0000209696"
FT CHAIN 1..273
FT /note="Heme oxygenase 1 soluble form"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT /id="PRO_0000455629"
FT TOPO_DOM 1..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT TRANSMEM 274..296
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REGION 231..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT BINDING 28
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 137
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT BINDING 186
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT SITE 143
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P09601"
SQ SEQUENCE 296 AA; 33509 MW; 22DAA9324494CC0E CRC64;
METSQPHNAE SMSQDLSELL KEATKEVHEQ AENTPFMKNF QKGQVSLHEF KLVTASLYFI
YSALEEEIER NKDNPVYAPV YFPMELHRKA ALEKDLEYFY GSNWRAEIPC PEATQKYVER
LHVVGKKHPE LLVAHAYTRY LGDLSGGQVL KKIAQKALQL PSTGEGLAFF TFDGVSNATK
FKQLYRSRMN ALEMDHATKK RVLEEAKKAF LLNIQVFEAL QKLVSKSQEN GHAVQPKAEL
RTRSVNKSHE NSPAAGKESE RTSRMQADML TTSPLVRWLL ALGFIATTVA VGLFAM
