ID   HMOX2_RABIT             Reviewed;         312 AA.
AC   P43242;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 116.
DE   RecName: Full=Heme oxygenase 2;
DE            Short=HO-2;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=HMOX2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1929402; DOI=10.1016/0003-9861(91)90549-x;
RA   Rotenberg M.O., Maines M.D.;
RT   "Characterization of a cDNA-encoding rabbit brain heme oxygenase-2 and
RT   identification of a conserved domain among mammalian heme oxygenase
RT   isozymes: possible heme-binding site?";
RL   Arch. Biochem. Biophys. 290:336-344(1991).
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.
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:0000250|UniProtKB:O48782};
CC   -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR   EMBL; S61699; AAB20093.1; -; mRNA.
DR   PIR; S18387; S18387.
DR   RefSeq; NP_001076216.1; NM_001082747.1.
DR   AlphaFoldDB; P43242; -.
DR   SMR; P43242; -.
DR   STRING; 9986.ENSOCUP00000044148; -.
DR   PaxDb; 9986-ENSOCUP00000005212; -.
DR   Ensembl; ENSOCUT00000006018.3; ENSOCUP00000005212.3; ENSOCUG00000006018.3.
DR   GeneID; 100009523; -.
DR   KEGG; ocu:100009523; -.
DR   CTD; 3163; -.
DR   eggNOG; KOG4480; Eukaryota.
DR   GeneTree; ENSGT00390000017673; -.
DR   InParanoid; P43242; -.
DR   OrthoDB; 1366343at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000006018; Expressed in testis and 18 other cell types or tissues.
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; 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:SF2; HEME OXYGENASE 2; 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   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..312
FT                   /note="Heme oxygenase 2"
FT                   /id="PRO_0000209693"
FT   REPEAT          260..265
FT                   /note="HRM 1"
FT   REPEAT          277..282
FT                   /note="HRM 2"
FT   BINDING         41
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   312 AA;  35373 MW;  2D33FF39FA1F5505 CRC64;
     MSAEVETSEG VDEPEEKNFG ENHIRMADLS ELLKEGTKEA HDRAENTKFV KDFLKGNIKK
     EIFKLATTAL YFTYSALEEE MDRNKDHPAF APLYFPMELH RKEALTKDME YFFGENWEEQ
     VQCSEAAQKY VERIHYIGQN EPELLVAHAY TRYMGDLSGG QVLKKVAQRA LKLPSTGEGT
     QFYLFENVDN AQQFKQFYRA RMNALDLNLK TKERIVEEAN KAFEYNMQIF SELDQAGSAP
     ASETVEDRIP VHDGKGDVRK CPYYAAGQVN GALEGSSCPF RAAMAVLRKP SLQLVLAAAV
     ALAAGLLAWY YM
//