HMOX1_PIG
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 03-AUG-2022, entry version 112.
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 [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:96115};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000305|PubMed:96115};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PeptideAtlas; P32394; -.
DR PRIDE; P32394; -.
DR Ensembl; ENSSSCT00055012067; ENSSSCP00055009535; ENSSSCG00055006201.
DR GeneID; 445512; -.
DR KEGG; ssc:445512; -.
DR CTD; 3162; -.
DR InParanoid; P32394; -.
DR OrthoDB; 1424194at2759; -.
DR BRENDA; 1.14.14.18; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:AgBase.
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: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:0006879; P:cellular iron ion homeostasis; ISS:AgBase.
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:0055072; P: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 I-kappaB kinase/NF-kappaB signaling; ISS:AgBase.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:AgBase.
DR GO; GO:0034395; P:regulation of transcription from RNA polymerase II promoter in response to iron; 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 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 PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; SSF48613; 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
