ID   HMOX3_RAT               Reviewed;         290 AA.
AC   O70453;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative heme oxygenase 3;
DE            Short=HO-3;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=Hmox3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9266719; DOI=10.1111/j.1432-1033.1997.00725.x;
RA   McCoubrey W.K. Jr., Huang T.J., Maines M.D.;
RT   "Isolation and characterization of a cDNA from the rat brain that encodes
RT   hemoprotein heme oxygenase-3.";
RL   Eur. J. Biochem. 247:725-732(1997).
RN   [2]
RP   IDENTIFICATION AS A PSEUDOGENE.
RX   PubMed=15246535; DOI=10.1016/j.gene.2004.04.002;
RA   Hayashi S., Omata Y., Sakamoto H., Higashimoto Y., Hara T., Sagara Y.,
RA   Noguchi M.;
RT   "Characterization of rat heme oxygenase-3 gene. Implication of processed
RT   pseudogenes derived from heme oxygenase-2 gene.";
RL   Gene 336:241-250(2004).
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. Heme oxygenase 3 could be implicated
CC       in some heme-dependent regulatory role in the cell.
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   -!- TISSUE SPECIFICITY: Found in the spleen, liver, thymus, prostate,
CC       heart, kidney, brain and testis.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. Encoded by a single-exon
CC       gene, absent in other mammals, including mouse, and not supported by
CC       EST data. Expression could not be detected at the mRNA level in a
CC       genomic DNA-free liver library, nor at the protein level in kidney
CC       (PubMed:15246535). {ECO:0000305|PubMed:15246535}.
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; AF058787; AAC14142.1; -; mRNA.
DR   AlphaFoldDB; O70453; -.
DR   SMR; O70453; -.
DR   PRIDE; O70453; -.
DR   RGD; 1565339; Hmox3.
DR   InParanoid; O70453; -.
DR   PhylomeDB; O70453; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042167; P:heme catabolic process; IBA:GO_Central.
DR   GO; GO:0006788; P:heme oxidation; IBA:GO_Central.
DR   GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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; 2.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   5: Uncertain;
KW   Heme; Iron; Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN           1..290
FT                   /note="Putative heme oxygenase 3"
FT                   /id="PRO_0000209695"
FT   REPEAT          238..243
FT                   /note="HRM 1"
FT   REPEAT          255..260
FT                   /note="HRM 2"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  32592 MW;  6600235CE8485829 CRC64;
     MSSEVETAEA VDESEKNSMA SEKENHSKIA DFSDLLKEGT KEADDRAENT QFVKDFLKGN
     IKKELFKLAT TALSYSAPEE EMDSLTKDME YFFGENWEEK VKCSEAAQTY VDQIHYVGQN
     EPEHLVAHTY STYMGGNLSG DQVLKKETQP VPFTREGTQF YLFEHVDNAK QFKLFYCARL
     NALDLNLKTK ERIVEEATKA FEYNMQIFSE LDQAGSIPVR ETLKNGLSIL DGKGGVCKCP
     FNAAQPDKGT LGGSNCPFQM SMALLRKPNL QLILVASMAL VAGLLAWYYM