ID   HMOX1_PIG               Reviewed;         288 AA.
AC   P32394;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Heme oxygenase 1;
DE            Short=HO-1;
DE            EC=1.14.14.18 {ECO:0000269|PubMed:96115};
DE   Contains:
DE     RecName: Full=Heme oxygenase 1 soluble form {ECO:0000250|UniProtKB:P09601};
GN   Name=HMOX1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1288499;
RA   Suzuki T., Sato M., Ishikawa K., Yoshida T.;
RT   "Nucleotide sequence of cDNA for porcine heme oxygenase and its expression
RT   in Escherichia coli.";
RL   Biochem. Int. 28:887-893(1992).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=96115; DOI=10.1016/s0021-9258(17)34707-5;
RA   Yoshida T., Kikuchi G.;
RT   "Purification and properties of heme oxygenase from pig spleen
RT   microsomes.";
RL   J. Biol. Chem. 253:4224-4229(1978).
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:96115). 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:96115}.
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
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000269|PubMed:96115};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC         Evidence={ECO:0000305|PubMed:96115};
CC   -!- SUBUNIT: Homodimer and higher order homooligomer. Oligomerization is
CC       crucial for its stability and function in the endoplasmic reticulum.
CC       Interacts with FLVCR2; this interaction is potentiated in the presence
CC       of heme. {ECO:0000250|UniProtKB:P14901}.
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   -!- DOMAIN: The transmembrane domain is necessary for its oligomerization.
CC       {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; X60677; CAA43092.1; -; mRNA.
DR   PIR; S37687; S37687.
DR   RefSeq; NP_001004027.1; NM_001004027.1.
DR   AlphaFoldDB; P32394; -.
DR   SMR; P32394; -.
DR   STRING; 9823.ENSSSCP00000066228; -.
DR   PeptideAtlas; P32394; -.
DR   Ensembl; ENSSSCT00055012067.1; ENSSSCP00055009535.1; ENSSSCG00055006201.1.
DR   GeneID; 445512; -.
DR   KEGG; ssc:445512; -.
DR   CTD; 3162; -.
DR   InParanoid; P32394; -.
DR   OrthoDB; 1366343at2759; -.
DR   BRENDA; 1.14.14.18; 6170.
DR   Reactome; R-SSC-189483; Heme degradation.
DR   Reactome; R-SSC-917937; Iron uptake and transport.
DR   Reactome; R-SSC-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   Reactome; R-SSC-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-SSC-9707587; Regulation of HMOX1 expression and activity.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR   GO; GO:0020037; F:heme binding; ISS:AgBase.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:AgBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:AgBase.
DR   GO; GO:0071276; P:cellular response to cadmium ion; ISS:AgBase.
DR   GO; GO:0034101; P:erythrocyte homeostasis; ISS:AgBase.
DR   GO; GO:0042167; P:heme catabolic process; ISS:AgBase.
DR   GO; GO:0042168; P:heme metabolic process; ISS:AgBase.
DR   GO; GO:0006788; P:heme oxidation; ISS:AgBase.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:AgBase.
DR   GO; GO:0043922; P:negative regulation by host of viral transcription; IMP:AgBase.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:AgBase.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:AgBase.
DR   GO; GO:1903901; P:negative regulation of viral life cycle; IMP:AgBase.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:AgBase.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:AgBase.
DR   GO; GO:0035094; P:response to nicotine; ISS:AgBase.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:AgBase.
DR   GO; GO:0002246; P:wound healing involved in inflammatory response; ISS:AgBase.
DR   CDD; cd00232; HemeO-like; 1.
DR   Gene3D; 1.20.910.10; Heme oxygenase-like; 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; HEME OXYGENASE; 1.
DR   PANTHER; PTHR10720:SF1; HEME OXYGENASE 1; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..288
FT                   /note="Heme oxygenase 1"
FT                   /id="PRO_0000209689"
FT   CHAIN           1..265
FT                   /note="Heme oxygenase 1 soluble form"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT                   /id="PRO_0000455623"
FT   TOPO_DOM        1..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT   TRANSMEM        266..288
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT   BINDING         25
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         134
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT   BINDING         183
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P09601"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06762"
SQ   SEQUENCE   288 AA;  33074 MW;  156D6175A308E0D2 CRC64;
     MEHSQPNSMP QDLSEALKEA TKEVHVQAEN AEFMKNFQKG EVTREGFKLV MASLYHIYDA
     LEEEIEHNKE NPVYTPLYFP EELHRRAALE QDMAFWYGPR WQEAIPYTQA TKRYVRRLQQ
     VGRFEPELLV AHAYTRYMGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NVANATKFKQ
     LYRSRMNTLE MTPEVKQRVL EEAKTAFLLN IQLFEEVQEL LTQDTKDQRP SQASDIRKRA
     GSRVQDSTPV TTPRGKPQLS VLSQVPLIRW VLTLSFLVAT VAMGLYAM
//