HMOX2_MOUSE
ID HMOX2_MOUSE Reviewed; 315 AA.
AC O70252; O70626;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Heme oxygenase 2;
DE Short=HO-2;
DE EC=1.14.14.18 {ECO:0000250|UniProtKB:P30519};
DE Contains:
DE RecName: Full=Heme oxygenase 2 soluble form {ECO:0000250|UniProtKB:P30519};
GN Name=Hmox2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RA Mount D.B.;
RT "Sequence of mouse heme oxygenase-2.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9795203; DOI=10.1016/s0378-1119(98)00477-6;
RA Gibbs L., Willis D., Morgan M.J.;
RT "The identification and expression of heme oxygenase-2 alternative
RT transcripts in the mouse.";
RL Gene 221:171-177(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: [Heme oxygenase 2]: 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. {ECO:0000250|UniProtKB:P30519}.
CC -!- FUNCTION: [Heme oxygenase 2 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:P30519}.
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:P30519};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000250|UniProtKB:P30519};
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P30519}; Single-pass type IV membrane protein
CC {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-
CC pass type IV membrane protein {ECO:0000255}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P09601}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|Ref.1}.
CC -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC anchor. {ECO:0000250|UniProtKB:P30519}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
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DR EMBL; AF029874; AAC17981.1; -; mRNA.
DR EMBL; AF054670; AAC82364.1; -; mRNA.
DR EMBL; AF054669; AAC82363.1; -; mRNA.
DR EMBL; BC002011; AAH02011.1; -; mRNA.
DR CCDS; CCDS27924.1; -.
DR PIR; JC5149; JC5149.
DR RefSeq; NP_001129538.1; NM_001136066.2.
DR RefSeq; NP_034573.2; NM_010443.2.
DR AlphaFoldDB; O70252; -.
DR SMR; O70252; -.
DR BioGRID; 200345; 6.
DR IntAct; O70252; 1.
DR MINT; O70252; -.
DR STRING; 10090.ENSMUSP00000004172; -.
DR iPTMnet; O70252; -.
DR PhosphoSitePlus; O70252; -.
DR SwissPalm; O70252; -.
DR EPD; O70252; -.
DR jPOST; O70252; -.
DR PaxDb; O70252; -.
DR PeptideAtlas; O70252; -.
DR PRIDE; O70252; -.
DR ProteomicsDB; 269578; -.
DR Antibodypedia; 11116; 654 antibodies from 40 providers.
DR DNASU; 15369; -.
DR Ensembl; ENSMUST00000004172; ENSMUSP00000004172; ENSMUSG00000004070.
DR Ensembl; ENSMUST00000118885; ENSMUSP00000113110; ENSMUSG00000004070.
DR Ensembl; ENSMUST00000120232; ENSMUSP00000112397; ENSMUSG00000004070.
DR GeneID; 15369; -.
DR KEGG; mmu:15369; -.
DR UCSC; uc007yag.2; mouse.
DR CTD; 3163; -.
DR MGI; MGI:109373; Hmox2.
DR VEuPathDB; HostDB:ENSMUSG00000004070; -.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_057050_0_1_1; -.
DR InParanoid; O70252; -.
DR OMA; ANRAFEY; -.
DR OrthoDB; 1424194at2759; -.
DR PhylomeDB; O70252; -.
DR TreeFam; TF314786; -.
DR BRENDA; 1.14.14.18; 3474.
DR Reactome; R-MMU-189483; Heme degradation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 15369; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Hmox2; mouse.
DR PRO; PR:O70252; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O70252; protein.
DR Bgee; ENSMUSG00000004070; Expressed in spermatid and 268 other tissues.
DR ExpressionAtlas; O70252; baseline and differential.
DR Genevisible; O70252; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
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: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:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30519"
FT CHAIN 2..315
FT /note="Heme oxygenase 2"
FT /id="PRO_0000209692"
FT CHAIN 2..294
FT /note="Heme oxygenase 2 soluble form"
FT /evidence="ECO:0000250|UniProtKB:P30519"
FT /id="PRO_0000455627"
FT TOPO_DOM 2..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09601"
FT TRANSMEM 295..315
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REPEAT 263..268
FT /note="HRM 1"
FT REPEAT 280..285
FT /note="HRM 2"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 44
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:P30519"
FT BINDING 153
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P30519"
FT BINDING 198
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P30519"
FT BINDING 202
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P30519"
FT SITE 159
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P09601"
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"
FT CONFLICT 172..174
FT /note="RAL -> SSS (in Ref. 2; AAC82364/AAC82363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35739 MW; EA382EB2C7CED6D1 CRC64;
MSSEVETSEG VDESEKNSMA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN
IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKAALIK DMKYFFGENW
EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG
EGTQFYLFEH VDNAQQFKQF YRARMNALDL NLKTKERIVE EANKAFEYNM QIFSELDQAG
SMLARETLED GLPVHDGKGD IRKCPFYAAQ PDKGTLGGSN CPFQTTVAVL RKPSLQLILA
ASVALVAGLL AWYYM
