CP2CT_MOUSE
ID CP2CT_MOUSE Reviewed; 490 AA.
AC Q64458; E9QMD8; Q8WUN8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cytochrome P450 2C29;
DE EC=1.14.14.1 {ECO:0000269|PubMed:9721182};
DE AltName: Full=Aldehyde oxygenase;
DE AltName: Full=CYPIIC29;
DE AltName: Full=Cytochrome P-450 MUT-2;
DE Flags: Precursor;
GN Name=Cyp2c29 {ECO:0000303|PubMed:9721182, ECO:0000312|MGI:MGI:103238};
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=C57BL/6J; TISSUE=Liver;
RX PubMed=8130255; DOI=10.1016/0005-2728(94)90237-2;
RA Matsunaga T., Watanabe K., Yamamoto I., Negishi M., Gonzalez F.J.,
RA Yoshimura H.;
RT "cDNA cloning and sequence of CYP2C29 encoding P-450 MUT-2, a microsomal
RT aldehyde oxygenase.";
RL Biochim. Biophys. Acta 1184:299-301(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND PATHWAY.
RX PubMed=9721182; DOI=10.1006/abbi.1998.0806;
RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.;
RT "Cloning and expression of murine CYP2Cs and their ability to metabolize
RT arachidonic acid.";
RL Arch. Biochem. Biophys. 357:45-57(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249; LYS-252 AND LYS-375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: A cytochrome P450 monooxygenase that selectively catalyzes
CC the epoxidation of 14,15 double bond of (5Z,8Z,11Z,14Z)-
CC eicosatetraenoic acid (arachidonate) forming 14,15-epoxyeicosatrienoic
CC acid (14,15-EET) regioisomer. Mechanistically, uses molecular oxygen
CC inserting one oxygen atom into a substrate, and reducing the second
CC into a water molecule, with two electrons provided by NADPH via
CC cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase).
CC {ECO:0000269|PubMed:9721182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51472, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:84024; Evidence={ECO:0000269|PubMed:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51473;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:9721182}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in liver as well as in extrahepatic
CC tissues including brain, kidney, lung, heart, and intestine.
CC {ECO:0000269|PubMed:9721182}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D17674; BAA04555.1; -; mRNA.
DR EMBL; AC120840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019908; AAH19908.1; -; mRNA.
DR CCDS; CCDS29793.1; -.
DR PIR; I49610; I49610.
DR RefSeq; NP_031841.3; NM_007815.3.
DR AlphaFoldDB; Q64458; -.
DR SMR; Q64458; -.
DR BioGRID; 199015; 27.
DR STRING; 10090.ENSMUSP00000003137; -.
DR SwissLipids; SLP:000001668; -.
DR iPTMnet; Q64458; -.
DR PhosphoSitePlus; Q64458; -.
DR SwissPalm; Q64458; -.
DR jPOST; Q64458; -.
DR MaxQB; Q64458; -.
DR PaxDb; Q64458; -.
DR PeptideAtlas; Q64458; -.
DR PRIDE; Q64458; -.
DR ProteomicsDB; 283616; -.
DR Ensembl; ENSMUST00000003137; ENSMUSP00000003137; ENSMUSG00000003053.
DR GeneID; 13095; -.
DR KEGG; mmu:13095; -.
DR UCSC; uc008hjz.1; mouse.
DR CTD; 13095; -.
DR MGI; MGI:103238; Cyp2c29.
DR VEuPathDB; HostDB:ENSMUSG00000003053; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155736; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; Q64458; -.
DR OMA; IPNIWVM; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q64458; -.
DR TreeFam; TF352043; -.
DR SABIO-RK; Q64458; -.
DR UniPathway; UPA00383; -.
DR BioGRID-ORCS; 13095; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Cyp2c29; mouse.
DR PRO; PR:Q64458; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q64458; protein.
DR Bgee; ENSMUSG00000003053; Expressed in liver and 39 other tissues.
DR ExpressionAtlas; Q64458; baseline and differential.
DR Genevisible; Q64458; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IDA:UniProtKB.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01685; EP450ICYP2B.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..490
FT /note="Cytochrome P450 2C29"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051717"
FT BINDING 435
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 106
FT /note="I -> M (in Ref. 3; AAH19908)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="G -> A (in Ref. 1; BAA04555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55716 MW; 17D6FF46002E169A CRC64;
MDLVVFLALT LSCLILLSLW RQSSGRGKLP PGPTPLPIIG NFLQIDVKNI SQSFTNFSKA
YGPVFTLYLG SKPTVILHGY EAVKEALIDR GEEFAGRGSF PMAEKIIKGF GVVFSNGNRW
KEMRRFTLMT LRNLGMGKRN IEDRVQEEAQ CLVEELRKTK GSPCDPTFIL SCAPCNVICS
IIFQNRFDYK DKEFLILMDK INENVKILSS PWLQVCNSFP SLIDYCPGSH HKIVKNFNYL
KSYLLEKIKE HKESLDVTNP RDFIDYYLIK QKQVNHIEQS EFSLENLAST INDLFGAGTE
TTSTTLRYAL LLLLKYPDVT AKVQEEIDRV VGRHRSPCMQ DRSHMPYTDA MIHEVQRFID
LLPTSLPHAV TCDIKFRKYL IPKGTTVITS LSSVLHDSKE FPNPEMFDPG HFLNGNGNFK
KSDYFMPFST GKRICAGEGL ARMELFLILT TILQNFKLKS LVHPKEIDIT PVMNGFASLP
PPYQLCFIPL
