PPOX_MOUSE
ID PPOX_MOUSE Reviewed; 477 AA.
AC P51175; P97344; Q99M34;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protoporphyrinogen oxidase;
DE Short=PPO;
DE EC=1.3.3.4;
GN Name=Ppox;
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], FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=8554330; DOI=10.1006/abbi.1995.0051;
RA Dailey T.A., Dailey H.A., Meissner P., Prasad A.R.;
RT "Cloning, sequence, and expression of mouse protoporphyrinogen oxidase.";
RL Arch. Biochem. Biophys. 324:379-384(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Erythroleukemia;
RX PubMed=7607249; DOI=10.1111/j.1432-1033.1995.0760h.x;
RA Taketani S., Yoshinaga T., Furukawa T., Kohno H., Tokunaga R.,
RA Nishimura K., Inokuchi H.;
RT "Induction of terminal enzymes for heme biosynthesis during differentiation
RT of mouse erythroleukemia cells.";
RL Eur. J. Biochem. 230:760-765(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=3346226; DOI=10.1016/s0021-9258(18)69000-3;
RA Ferreira G.C., Andrew T.L., Karr S.W., Dailey H.A.;
RT "Organization of the terminal two enzymes of the heme biosynthetic pathway.
RT Orientation of protoporphyrinogen oxidase and evidence for a membrane
RT complex.";
RL J. Biol. Chem. 263:3835-3839(1988).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and
RC 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: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000269|PubMed:8554330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC Evidence={ECO:0000269|PubMed:8554330};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by acifluorfen.
CC {ECO:0000269|PubMed:8554330}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC -!- SUBUNIT: Monomer. Homodimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:3346226}; Peripheral membrane protein
CC {ECO:0000269|PubMed:3346226}; Intermembrane side
CC {ECO:0000269|PubMed:3346226}.
CC -!- INDUCTION: During erythroid differentiation.
CC {ECO:0000269|PubMed:7607249}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily. {ECO:0000305}.
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DR EMBL; U25114; AAA96003.1; -; mRNA.
DR EMBL; D45185; BAA08126.1; -; mRNA.
DR EMBL; BC002047; AAH02047.1; -; mRNA.
DR CCDS; CCDS15487.1; -.
DR PIR; S65684; S65684.
DR PIR; S68367; S68367.
DR RefSeq; NP_032937.1; NM_008911.2.
DR RefSeq; XP_006496770.1; XM_006496707.3.
DR AlphaFoldDB; P51175; -.
DR SMR; P51175; -.
DR BioGRID; 202334; 2.
DR IntAct; P51175; 4.
DR STRING; 10090.ENSMUSP00000072863; -.
DR iPTMnet; P51175; -.
DR PhosphoSitePlus; P51175; -.
DR EPD; P51175; -.
DR MaxQB; P51175; -.
DR PaxDb; P51175; -.
DR PeptideAtlas; P51175; -.
DR PRIDE; P51175; -.
DR ProteomicsDB; 289741; -.
DR Antibodypedia; 34299; 270 antibodies from 28 providers.
DR DNASU; 19044; -.
DR Ensembl; ENSMUST00000073120; ENSMUSP00000072863; ENSMUSG00000062729.
DR GeneID; 19044; -.
DR KEGG; mmu:19044; -.
DR UCSC; uc007dns.1; mouse.
DR CTD; 5498; -.
DR MGI; MGI:104968; Ppox.
DR VEuPathDB; HostDB:ENSMUSG00000062729; -.
DR eggNOG; KOG1276; Eukaryota.
DR GeneTree; ENSGT00390000008744; -.
DR HOGENOM; CLU_009629_2_1_1; -.
DR InParanoid; P51175; -.
DR OMA; WFDQWFG; -.
DR OrthoDB; 1578484at2759; -.
DR PhylomeDB; P51175; -.
DR TreeFam; TF323479; -.
DR Reactome; R-MMU-189451; Heme biosynthesis.
DR UniPathway; UPA00251; UER00324.
DR BioGRID-ORCS; 19044; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ppox; mouse.
DR PRO; PR:P51175; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P51175; protein.
DR Bgee; ENSMUSG00000062729; Expressed in fetal liver hematopoietic progenitor cell and 249 other tissues.
DR ExpressionAtlas; P51175; baseline and differential.
DR Genevisible; P51175; MM.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IDA:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; IDA:MGI.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046501; P:protoporphyrinogen IX metabolic process; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Heme biosynthesis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..477
FT /note="Protoporphyrinogen oxidase"
FT /id="PRO_0000135272"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 57..60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 454..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 64
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="A -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> S (in Ref. 2; BAA08126)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> Q (in Ref. 3; AAH02047)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="W -> C (in Ref. 2; BAA08126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 50871 MW; 8CFB48120728DE6F CRC64;
MGRTVIVLGG GISGLAASYH LIRGPSPPKV ILVEGSKRLG GWIRSIRGSD GAIFELGPRG
IRPAGALGAR TLLLVSELGL ESEVLPVRGD HPAAQNRFLY VGGTLHPLPS GLRGLLRPSP
PFSKPLFWAG LRELLKPRGK EPDETVHSFA QRRLGPEVAS LAMDSLCRGV FAGNSRELSI
RSCFPSLFQA EQTHRSILLG LLLGAGQSPQ PDSSLIRQAR AERWSQWSLR GGLEVLPQAL
HNHLASKGVT VLSGQPVCGL SLQPEGRWKV SLGDSSLEAD HIISAIPASE LSKLLPAEAA
PLARILSTIK AVSVAVVNLQ YRGACLPVQG FGHLVPSSED PTVLGIVYDS VAFPEQDGNP
PSLRVTVMLG GYWLQKLKAA GHQLSPELFQ QQAQEAAATQ LGLKEPPSHC LVHLHKNCIP
QYTIGHWQKL DSAMQFLTAQ RLPLTLAGAS YEGVAVNDCI ESGRQAAVAV LGTESNS
