HMOX1_PONAB
ID HMOX1_PONAB Reviewed; 288 AA.
AC Q5R7E3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Heme oxygenase 1;
DE Short=HO-1;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:P09601};
DE Contains:
DE RecName: Full=Heme oxygenase 1 soluble form {ECO:0000250|UniProtKB:P09601};
GN Name=HMOX1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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 -!- 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:0000250|UniProtKB:P09601};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000250|UniProtKB:P09601};
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; CR860175; CAH92317.1; -; mRNA.
DR RefSeq; NP_001126358.1; NM_001132886.1.
DR AlphaFoldDB; Q5R7E3; -.
DR SMR; Q5R7E3; -.
DR STRING; 9601.ENSPPYP00000013121; -.
DR GeneID; 100173339; -.
DR KEGG; pon:100173339; -.
DR CTD; 3162; -.
DR eggNOG; KOG4480; Eukaryota.
DR InParanoid; Q5R7E3; -.
DR OrthoDB; 1424194at2759; -.
DR Proteomes; UP000001595; 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:0004392; F:heme oxygenase (decyclizing) activity; ISS: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:0006788; P:heme oxidation; IEA:InterPro.
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 2: Evidence at transcript 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_0000317707"
FT CHAIN 1..265
FT /note="Heme oxygenase 1 soluble form"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT /id="PRO_0000455624"
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 223..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..260
FT /note="Polar residues"
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 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09601"
SQ SEQUENCE 288 AA; 32712 MW; 10400CCCCA98F7F3 CRC64;
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTREGFKLV MASLYHIYVA
LEEEIEHNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE
VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALGLPSS GEGLAFFTFP NIASATKFKQ
LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA
SNKAQDSAPV ETPRGKTPLN THSQAPLLRW VLTLSFLVAT VAVGLYAM
