HMOX2_RABIT
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 03-AUG-2022, entry version 112.
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 [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.
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.ENSOCUP00000005212; -.
DR PRIDE; P43242; -.
DR Ensembl; ENSOCUT00000006018; ENSOCUP00000005212; ENSOCUG00000006018.
DR GeneID; 100009523; -.
DR KEGG; ocu:100009523; -.
DR CTD; 3163; -.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR InParanoid; P43242; -.
DR OrthoDB; 1424194at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000006018; Expressed in testis and 18 other 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; -; 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..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