ID   HMOX2_MACFA             Reviewed;         316 AA.
AC   Q2PG53;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Heme oxygenase 2;
DE            Short=HO-2;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=HMOX2; ORFNames=QbsB-11392;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain stem;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene
CC       bridge to form biliverdin. Biliverdin is subsequently converted to
CC       bilirubin by biliverdin reductase. Under physiological conditions, the
CC       activity of heme oxygenase is highest in the spleen, where senescent
CC       erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be
CC       implicated in the production of carbon monoxide in brain where it could
CC       act as a neurotransmitter. {ECO:0000250}.
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:O48782};
CC   -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; AB220384; BAE72917.1; -; mRNA.
DR   RefSeq; NP_001270155.1; NM_001283226.1.
DR   AlphaFoldDB; Q2PG53; -.
DR   SMR; Q2PG53; -.
DR   STRING; 9541.XP_005591175.1; -.
DR   GeneID; 102143766; -.
DR   CTD; 3163; -.
DR   eggNOG; KOG4480; Eukaryota.
DR   OrthoDB; 1424194at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006788; P:heme oxidation; IEA:InterPro.
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   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   Acetylation; Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30519"
FT   CHAIN           2..316
FT                   /note="Heme oxygenase 2"
FT                   /id="PRO_0000317708"
FT   REPEAT          264..269
FT                   /note="HRM 1"
FT   REPEAT          281..286
FT                   /note="HRM 2"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
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"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30519"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P30519"
SQ   SEQUENCE   316 AA;  36081 MW;  40A85866272B219E CRC64;
     MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG
     NIKKELFKLA TTALYFTYSA LEEEMERNKD HPTFAPLYFP MELHRKEALT KDMEYFFGEN
     WEEQVQCPKA AKKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST
     GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA
     GSTLARETLE DGFPVHDGKG DMRKCPFYAG EQDKGALEGS SCPFRTAMAV LRKPSLQFIL
     AAGMALAAGL LAWYYM